TITLE: Biotechnology: Gene Expression in Cereal Crops, June 1992 - May1994, QB 94-57  PUBLICATION DATE: May 1994ENTRY DATE: November, 1994EXPIRATION DATE: NoneUPDATE FREQUENCY: As neededCONTACT: Biotechnology Information Center(biotech@nalusda.gov)         National Agricultural LibraryDOCUMENT TYPE: TextDOCUMENT SIZE: 460 K
**Gene Expression in Cereal Crops**
                             SEARCH STRATEGY
     SET       ITEMS     DESCRIPTION      S1872    (EXPRESS? (3W)(GENE OR GENES))/TI      S2   9327     GENE(W)EXPRESS?/DE      S3   9568     S1 OR S2      S4 113032     BARLEY OR MAIZE OR CORN OR MILLET OR OAT OR RICE               OR RYE OR TRITICALE OR WHEAT OR SORGHUM OR MILO               OR BUCKWHEAT OR ((CEREAL OR GRAIN)()CROP?)      S5 108166     S4/TI,DE      S6  39947     HORDEUM OR ((AVENA OR ORYZA)()SATIVA) OR               SECALE()CEREALE OR ZEA()MAYS OR TRITICUM()AESTIVUM      S7 117412     S5 OR S6      S8   1201     S3 AND S7      S9391    S8 AND PY=1992:1994
1                                                     NAL Call. No.: QK710.P62A 168 bp derivative of Suppressor-mutator/Enhancer is responsible for themaize o2-23 mutation.Aukerman, M.J.; Schmidt, R.J.Dordrecht : Kluwer Academic Publishers; 1993 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (2): p. 355-362; 1993 Jan.Includes references.
Language:  English
Descriptors: Zea mays; Transposable elements; Loci; Alleles; Opaque-2 maize;Structural genes; Dna binding proteins; Exons; Mutations; Mutants;Mutagenesis; Genetic regulation; Gene expression; Messenger  RNA
Abstract:  From a directed transposon tagging of the maize Opaque-2 gene (O2),we have isolated a stable mutant o2 allele, o2-23. Cloning and molecularanalysis of the allele revealed a 168 nucleotide insertion in the third exonof o2. The sequence of this small insertion indicated identity with the 5' and3' ends of the 8.3 kb Suppressor-mutator/Enhancer (Spm/En) transposableelement. This represents the smallest deletion derivative of Spm (dSpm) thusfar characterized in maize. Genetic crosses of plants homozygous for o2-23with plants homozygous for both an o2 null allele (o2-R) and an autonomous Spmproduce stable opaque seed having no apparent sectors of vitreous endosperm.DNA fragments of the size expected if the dSpm were to excise were notdetectable by Southern analysis, suggesting that this element is unable totranspose. Northern analysis detected an o2-23 mRNA that was much moreabundant in o2-23 seeds lacking Spm than in o2-23 seeds containing Spm,consistent with the idea that Spm transacting functions can suppress theaccumulation of the o2-23 transcript.
2                                                     NAL Call. No.: QK710.P683'-end processing of the maize 27 kDa zein mRNA.Wu, L.; Ueda, T.; Messing, J.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Sep.The Plant journal : for cell and molecular biology v. 4 (3): p. 535-544; 1993Sep.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Messenger  RNA; Mutagenesis;Mutations; Nucleotide sequences; Transcription; Zein
3                                                     NAL Call. No.: QK710.P685' distal and proximal cis-acting regulator elements are required fordevelopmental control of a rice seed storage protein glutelin gene.Zheng, Z.; Kawagoe, Y.; Xiao, S.; Li, Z.; Okita, T.; Hau, T.; Lin, A.; Murai,N.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Aug.The Plant journal : for cell and molecular biology v. 4 (2): p. 357-366; 1993Aug.  Includes references.
Language:  English
Descriptors: Oryza sativa; Transgenics; Transcription; Gene expression;Glutelins; Seeds; Binding site; Endosperm; Mutations; Promoters
4                                                      NAL Call. No.: 450 P693                                                                        PUSDAx                                                                    NSUQK1.P73
Aberrations in plastid transcripts and deficiency of plastid DNA in stripedand albino mutants in maize.Han, C.D.; Patrie, W.; Polacco, M.; Coe, E.H. JrBerlin ; New York : Springer-Verlag, 1925-; 1993.Planta v. 191 (4): p. 552-563; 1993.  Includes references.
Language:  English
Descriptors: Zea mays; Mutants; Plastids; Genome analysis; Gene expression;Transcription; Dna; Quantitative analysis; Albinos; Protein transport; Geneticregulation
Abstract:  To better understand the regulatory roles of nuclear genes inchloroplast genomic expression during leaf development in maize (Zea mays L.),we studied a striped mutant, ii1 (iojap 1), two albino mutants, w1 (white 1)and w2 (white 2), and their double mutants with 1 (luteus). Homozygous ij1plants as a female parent produce albino seedlings, called maternalexceptions, among their progeny, even when the nuclear genotype of the maleparent is normal (+/+). In contrast to albinos that are blocked in thebiosynthetic pathway of carotenoids, w1 and w2 seedlings fall to accumulatechlorophyll and carotenoids up to the normal level even under dim lightconditions. In ij1-affected plastids, the plastid-encoded proteins andnuclear-encoded proteins that are associated with thylakoid membranes were notdetecable. However, the 33-kDa protein of the oxygen-evolving complex andferredoxin: NADP oxidoreductase, which are localized extrinsically, wereaccumulated even though the level of the proteins was decreased. Both ij1 andw1 albino seedlings contain a normal level of plastid DNA. However, both showsimilar aberrant patterns among the transcripts of all the plastid genesexamined (psbB, psbH, petB, petD, atpA, psaB, psbA, and rbcL). Not only wereadditional transcripts detected but some of the normal transcripts were notdetectable or were barely detectable by Northern hybridization. These factsindicate that the transcripts of ij1- and w1-affected plastids may havealtered synthesis, processing or stability. Therefore, the block in expressionof the plastid genome by the nuclear mutants ij1 and w1 may be due toalterations in the transcriptional or post-transcriptional processes. The factthat ij1 and maternal-exception progeny show almost identical patterns oftranscripts indicates that the effects of ij1 on plastid gene expressionpersist in the subsequent generation even after the nuclear gene, lj1,restores the normal function. In contrast to ij1 and w1, the levels of allplastid transcripts in w2 seedlings, whether l or +, are uniformly reduced.Compared to normal sibling seedlings, the patterns of the RNA species arerelatively unaltered. Relative to the level of a nuclear rDNA, the plastid DNAcontent of w2 is decreased 20-fold. Therefore, the limited expression of thew2-affected plastids may be due to failure to maintain the copy number ofplastid genomes. Thus, albinisms of these mutants result from limiting ofexpression of plastids due to alteration of transcripts on the one hand, or tolowered DNA content on the other.
5                                                     NAL Call. No.: QH506.E46Abscisic acid is involved in the iron-induced synthesis of maize ferritin.Lobreaux, S.; Hardy, T.; Briat, J.F.Oxford, Eng. : IRL Press; 1993 Feb.The EMBO journal - European Molecular Biology Organization v. 12 (2): p.651-657; 1993 Feb.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Transcription; Structural genes;Messenger  RNA; Ferritin; Genetic regulation; Abscisic acid; Iron; Nutrientavailability; Stress; Roots; Leaves
Abstract:  The ubiquitous iron storage protein ferritin has a highly conservedstructure in plants and animals, but a distinct cytological location and adifferent level of control in response to iron excess. Plant ferritins areplastid-localized and transcriptionally regulated in response to iron, whileanimal ferritins are found in the cytoplasm and have their expression mainlycontrolled at the translational level. In order to understand the basis ofthese differences, we developed hydroponic cultures of maize plantlets whichallowed an increase in the intracellular iron concentration, leading to atransient accumulation of ferritin mRNA and protein (Lobreaux, S., Massenet,O. and Briat, J.F., 1992, Plant Mol. Biol, 19, 563-575). Here, it is shownthat iron induces ferritin and RAB (Responsive to Abscisic Acid) mRNAaccumulation relatively with abscisic acid (ABA) accumulation. Ferritin mRNAalso accumulates in response to exogenous ABA. Synergistic experimentsdemonstrate that the ABA and iron responses are linked, although fullexpression of the ferritin genes cannot be entirely explained by an increasein ABA concentration. Inducibility of ferritin mRNA accumulation by iron isdramatically decreased in the maize ABA-deficient mutant vp2 and can berescued by addition of exogenous ABA, confirming the involvement of ABA in theiron response in plants. Therefore, it is concluded that a major part of theiron-induced biosynthesis of ferritin is achieved through a pathway involvingan increase in the level of the plant hormone ABA. The general conclusion ofthis work is that the synthesis of the same protein in response to the sameenvironmental signal can be controlled by separate and distinct mechanisms inplants and animals.
6                                                     NAL Call. No.: QH506.E46Abscisic acid is involved in the iron-induced synthesis of maize ferritin.Lobreaux, S.; Hardy, T.; Briat, J.F.Oxford, Eng. : IRL Press; 1993 Feb.The EMBO journal - European Molecular Biology Organization v. 12 (2): p.651-657; 1993 Feb.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Transcription; Structural genes;Messenger  RNA; Ferritin; Genetic regulation; Abscisic acid; Iron; Nutrientavailability; Stress; Roots; Leaves
Abstract:  The ubiquitous iron storage protein ferritin has a highly conservedstructure in plants and animals, but a distinct cytological location and adifferent level of control in response to iron excess. Plant ferritins areplastid-localized and transcriptionally regulated in response to iron, whileanimal ferritins are found in the cytoplasm and have their expression mainlycontrolled at the translational level. In order to understand the basis ofthese differences, we developed hydroponic cultures of maize plantlets whichallowed an increase in the intracellular iron concentration, leading to atransient accumulation of ferritin mRNA and protein (Lobreaux, S., Massenet,O. and Briat, J.F., 1992, Plant Mol. Biol, 19, 563-575). Here, it is shownthat iron induces ferritin and RAB (Responsive to Abscisic Acid) mRNAaccumulation relatively with abscisic acid (ABA) accumulation. Ferritin mRNAalso accumulates in response to exogenous ABA. Synergistic experimentsdemonstrate that the ABA and iron responses are linked, although fullexpression of the ferritin genes cannot be entirely explained by an increasein ABA concentration. Inducibility of ferritin mRNA accumulation by iron isdramatically decreased in the maize ABA-deficient mutant vp2 and can berescued by addition of exogenous ABA, confirming the involvement of ABA in theiron response in plants. Therefore, it is concluded that a major part of theiron-induced biosynthesis of ferritin is achieved through a pathway involvingan increase in the level of the plant hormone ABA. The general conclusion ofthis work is that the synthesis of the same protein in response to the sameenvironmental signal can be controlled by separate and distinct mechanisms inplants and animals.
7                                                     NAL Call. No.: QK710.P55An abscisic-acid-responsive, low temperature barley gene has homology with amaize phospholipid transfer protein.Hughes, M.A.; Dunn, M.A.; Pearce, R.S.; White, A.J.; Zhang, L.Oxford : Blackwell Scientific Publications; 1992 Sep.Plant, cell and environment v. 15 (7): p. 861-865; 1992 Sep.  Includesreferences.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Binding proteins; Nucleotidesequences; Amino acid sequences; Gene expression; Genetic regulation;Messenger  RNA; Abscisic acid; Shoot meristems; Cold tolerance;Acclimatization
8                                                     NAL Call. No.: QK710.P68The accumulation of zein polypeptides and zein mRNA in cultured endosperms ofmaize is modulated by nitrogen supply.Balconi, C.; Rizzi, E.; Motto, M.; Salamini, F.; Thompson, R.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Feb.The plant journal v. 3 (2): p. 325-334; 1993 Feb.  Paper presented at the"Symposium on the use of Mutants to Study Plant Metabolism and Development,"Annual Meeting of the Society of Experimental Biology, April, 1992.  Includesreferences.
Language:  English
Descriptors: Zea mays; Transcription; Gene expression; Messenger  RNA; Zein;Structural genes; Endosperm; Genetic regulation; Nutrient availability;Nitrogen; Dna binding proteins; Opaque-2 maize; Protein content; Proteincomposition
9                                                     NAL Call. No.: QK710.P62Activity of a maize ubiquitin promoter in transgenic rice.Cornejo, M.J.; Luth, D.; Blankenship, K.M.; Anderson, O.D.; Blechl, A.E.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (3): p. 567-581; 1993 Nov.  Includes references.
Language:  English
Descriptors: Zea mays; Oryza sativa; Promoters; Ubiquitin; Exons; Introns;Recombinant  DNA; Reporter genes; Beta-glucuronidase; Luciferase;Acyltransferases; Genetic transformation; Transgenic plants; Gene expression;Callus; Protoplasts; Histoenzymology; Cell division; Enzyme activity;Herbicide resistance; Bilanafos; Heat shock
Abstract:  We have used the maize ubiquitin 1 promoter, first exon and firstintron (UBI) for rice (Oryza sativa L. cv. Taipei 309) transformationexperiments and studied its expression in transgenic calli and plants. UBIdirected significantly higher levels of transient gene expression than otherpromoter/intron combinations used for rice transformation. We exploited thesehigh levels of expression to identify stable transformants obtained fromcallus-derived protoplastsco-transfected with two chimeric genes. The genesconsisted of UBI fused to the coding regions of the uidA and bar marker genes(UBI:GUS and UBI:BAR). UBI:GUS expression increased in response to thermalstress in both transfected protoplasts and transgenic rice calli.Histochemical localization of GUS activity revealed that UBI was most activein rapidly dividing cells. This promoter is expressed in many, but not all,rice tissues and undergoes important changes in activity during thedevelopment of transgenic rice plants.
10                                                   NAL Call. No.: QD341.A2N8Activity of yeast FLP recombinase in maize and rice protoplasts.Lyznik, L.A.; Mitchell, J.C.; Hirayama, L.; Hodges, T.K.Oxford : IRL Press; 1993 Feb25.Nucleic acids research v. 21 (4): p. 969-975; 1993 Feb25.  Includesreferences.
Language:  English
Descriptors: Saccharomyces cerevisiae; Zea mays; Oryza sativa; Recombination;Dna binding proteins; Enzymes; Protoplasts; Dna; Genetic transformation; Geneexpression; Reporter genes
Abstract:  We have demonstrated that a yeast FLP/FRT site-specificrecombination system functions in maize and rice protoplasts. FLP recombinaseactivity was monitored by reactivation of beta-glucuronidase (GUS) expressionfrom vectors containing the gusA gene inactivated by insertion of two FRTs(FLP recombination targets) and a 1.31 kb DNA fragment. The stimulation of GUSactivity in protoplasts cotransformed with vectors containing FRT inactivatedgusA gene and a chimeric FLP gene depended on both the expression of the FLPrecombinase and the presence and structure of the FRT sites. The FLP enzymecould mediate inter- and intramolecular recombination in plant protoplasts.These results provide evidence that a yeast recombination system can functionefficiently in plant cells, and that its performance can be manipulated bystructural modification of the FRT sites.
11                                                    NAL Call. No.: QK710.P62Agrobacterium-mediated production of transgenic rice plants expressing achimeric alpha-amylase promoter/beta-glucuronidase gene.Chan, M.T.; Chang, H.H.; Ho, S.L.; Tong, W.F.; Yu, S.M.Dordrecht : Kluwer Academic Publishers; 1993 Jun.Plant molecular biology v. 22 (3): p. 491-506; 1993 Jun.  Includes references.
Language:  English
Descriptors: Oryza sativa; Agrobacterium tumefaciens; Genetic transformation;Transgenic plants; Alpha-amylase; Promoters; Recombinant  DNA;Beta-glucuronidase; Phosphotransferases; Reporter genes; Solanum tuberosum;Cell suspensions; Gene expression; Histoenzymology; Enzyme activity;Inheritance; Structural genes
Abstract:  We have successfully transferred and expressed a reporter genedriven by an alpha-amylase promoter in a japonica type of rice (Oryza sativaL. cv. Tainung 62) using the Agrobacterium-mediated gene transfer system.Immature rice embryos (10-12 days after anthesis) were infected with anAgrobacterium strain carrying a plasmid containing chimeric genes ofbeta-glucuronidase (uidA) and neomycin phosphotransferase (nptII).Co-incubation of potato suspension culture (PSC) with the Agrobacteriuminoculum significantly improved the transformation efficiency of rice. TheuidA and nptII genes, which are under the control of promoters of a ricealpha-amylase gene (alpha Amy8) and Agrobacterium nopaline synthase gene(nos), respectively, were both expressed in G418-resistant calli andtransgenic plants. Integration of foreign genes into the genomes of transgenicplants was confirmed by Southern blot analysis. Histochemical localization ofGUS activity in one transgenic plant (R0) revealed that the rice alpha-amylasepromoter functions in all cell types of the mature leaves, stems, sheaths androots, but not in the very young leaves. This transgenic plant grew moreslowly and produced less seeds than the wild-type plant, but its R1 and R2progenies grew normally and produced as much seeds as the wild-type plant.Inheritance of foreign genes to the progenies was also confirmed by Southernblot analysis. These data demonstrate successful gene transfer and sexualinheritance of the chimeric genes.
12                                                    NAL Call. No.: QK710.P62Aleurone nuclear proteins bind to similar elements in the promoter regions oftwo gibberellin-regulated alpha-amylase genes.Rushton, P.J.; Hooley, R.; Lazarus, C.M.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 891-901; 1992 Sep.Includes references.
Language:  English
Descriptors: Triticum aestivum; Avena fatua; Promoters; Structural genes;Alpha-amylase; Binding site; Dna binding proteins; Nucleoproteins; Aleuronecells; Protoplasts; Gene expression; Nucleotide sequences; Controllingelements; Transcription
Abstract:  Binding of nuclear proteins from wild oat aleurone protoplasts tothe promoter regions of two gibberellin-regulated wheat alpha-amylase genes(alpha-Amy1/18 and alpha-Amy2/54) has been studied by gel retardation andDNase 1 footprinting. Gel retardation studies using 300-430 bp fragments ofthe promoters showed similar binding characteristics with nuclear extractsfrom both gibberellin A1-treated and untreated protoplasts. DNase 1 footprintslocalised binding of nuclear proteins from gibberellin A1-treated aleuroneprotoplasts to regions in both promoters. Similar sequence elements in thepromoter regions of both genes were protected from digestion although thelocation and number of footprints in each promoter region were different. Eachfootprint contained either a sequence similar to the cAMP and/or phorbol esterresponse elements, or a hyphenated palindrome sequence. The presence of cAMPand/or phorbol ester response element-like sequences in the footprintssuggests that transcription factors of the bZIP type may be involved in theexpression of alpha-amylase genes in aleurone cells. Footprints containinghyphenated palindrome sequences, found in the promoter regions of both genes,suggest the possible involvement of other classes of transcription factor. Theconserved alpha-amylase promoter sequence TAACAGA was also shown to bindnuclear protein in the alpha-Amy2/54 promoter. These observations arediscussed in relation to alpha-amylase gene expression in aleurone and tofunctional data concerning these genes.
13                                                     NAL Call. No.: 450 P692Alteration of gene expression associated with abscisic acid-induced chillingtolerance in maize suspension-cultured cells.Xin, Z.; Li, P.H.Rockville, Md. : American Society of Plant Physiologists; 1993 Jan.Plant physiology v. 101 (1): p. 227-284; 1993 Jan.  Includes references.
Language:  English
Descriptors: Zea mays; Cell suspensions; Rna; Protein synthesis; Regulation;Abscisic acid; Induction; Chilling; Cold tolerance; Gene expression;Temperature
Abstract:  ABA induces chilling tolerance in maize (Zea mays L., cv BlackMexican Sweet) suspension-cultured cells at 28 degrees C when ABA was added tothe culture medium at least 6 h prior to chilling (4 degrees C), and thisinduction can be inhibited by blocking protein synthesis with cycloheximidetreatment (Z. Xin, P.H. Li [1992] Plant Physiol 99: 707-711). De novosynthesis of proteins and changes in poly(A+) RNAs were investigated duringthe ABA induction of chilling tolerance at 28 degrees C as well as duringchilling exposure. At 28 degrees C, ABA increased the net synthesis of 11proteins. Five of these proteins, whose net synthesis was also increased bychilling (4 degrees C), were called group I ABA-induced proteins; theremaining six proteins, whose net synthesis was not altered by chilling, werecalled group II ABA-induced proteins. Chilling suppressed the net synthesis ofthree proteins. ABA treatment prior to chilling did not alleviate thissuppression. ABA applied at the inception of chilling induced neither chillingtolerance nor accumulation of any of the group II proteins; however, once thegroup II proteins appeared, they were continually synthesized even in achilling regimen. ABA induced seven in vitro translation products at 28degrees C. Three of these products could also be induced by chilling; theremaining four were induced by ABA only at 28 degrees C. These results suggestthat ABA-induced alteration of protein synthesis at 28 degrees C is associatedwith an increased chilling tolerance in maize suspension-cultured cells.
14                                               NAL Call. No.: QK725.P56 1993Altered nuclear, mitochondrial and plastid gene expression in white barleycells containing ribosome-deficient plastids.Borner, T.; Hess, W.R.Weinheim ; New York : VCH; 1993.Plant mitochondria : with emphasis on RNA editing and cytoplasmic malesterility /. p. 207-219; 1993.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Gene expression; Transcription; Structuralgenes; Genomes; Chloroplasts; Mitochondria; Nuclei; Mitochondrial genetics;Chloroplast genetics; Nucleocytoplasmic interaction; Ribosomes; Deficiency;Mutants; Messenger  RNA
Abstract:  The progeny of the barley mutant line albostrians consists ofgreen, white and green-white striped seedlings. Cells from white tissuecontain plastids which lack ribosomes and, consequently, all proteins encodedin plastid DNA. In spite of this drastic defect, cells of white leaves haveplastids and plastid DNA in quantities comparable to green leaves. Plastidgenes for ribosomal proteins (rps2, rps15) and subunits of a putative RNApolymerase (rpoA, rpoB, rpoC1) are transcribed and the mRNAs accumulate to adistinctly higher level (rps15, rpoB/C1) in white compared to green leaves.Genes encoding chloroplast proteins involved in bioenergetic functions (psbA,rbcL, atpI-H), and also tRNA(Glu) and plastid rRNAs, showed little or noaccumulation of their transcripts. The data provide strong evidence for aplastid RNA polymerase originating entirely from the nucleo-cytoplasmiccompartment. Messengers of mitochondrial genes encoding proteins involved inrespiration (coxII, coxIII, atpA, atp6, cob) were found to accumulate to ahigher level in white vs. green leaves, whereas mitochondrial 18S and 26SrRNAs were distinctly less affected by the presence of mutant,undifferentiated plastids. Nuclear genes which are light-induced and normallyspecifically expressed in green tissue (rbcS, cab, genes encoding Calvin cycleenzymes) showed an extremely low accumulation of their mRNAs in white leavesdue to a reduced rate of transcription. Although at a very low level, thetranscription of these genes was still light-inducible, and a circadian rhythmof cab-mRNA accumulation could be observed. The data are discussed in relationto regulatory interactions between the genomes of plant cells.
15                                                   NAL Call. No.: QK725.P532Alternative splicing induced by insertion of retrotransposons into the maizewaxy gene.Varagona, M.J.; Purugganan, M.; Wessler, S.R.Rockville, Md. : American Society of Plant Physiologists; 1992 Jul.The Plant cell v. 4 (7): p. 811-820; 1992 Jul.  Includes references.
Language:  English
Descriptors: Zea mays; Transposable elements; Insertional mutagenesis;Alternative splicing; Structural genes; Nucleotidyltransferases; Alleles; Geneexpression; Introns; Exons; Induced mutations; Messenger  RNA; Nucleotidesequences; Enzyme activity; Endosperm
Abstract:  The molecular basis for the low level expression of three allelesof the maize waxy (Wx) gene has been described. Each allele contains aretrotransposon in intron sequences. These insertions represent previouslyundescribed elements, and their association with three wx alleles indicatesthat retrotransposon elements are important agents of spontaneous mutation inmaize. For each allele, element sequences are spliced from pre-mRNA with thesurrounding intron even though the insertions increase intron length byapproximately 40- to 60-fold. In addition, despite differences in elementsequences, insertion sites, and relative orientations, each element disruptslong-range splice site recognition leading to novel Wx transcripts where exonsboth upstream and downstream of the insertion site are skipped. The expressionof wx alleles with large insertions in introns provides support for studiesthat indicate that the primary cis requirement for maize introns is the splicedonor and acceptor sites.
16                                                    NAL Call. No.: QK710.P68Analysis of maize alpha-tubulin gene promoter by transient expression and intransgenic tobacco plants.Rigau, J.; Capellades, M.; Montoliu, L.; Torres, M.A.; Romera, C.;Martinez-Izquierdo, J.A.; Tagu, D.; Puigdomenech, P.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Dec.The Plant journal : for cell and molecular biology v. 4 (6): p. 1043-1050;1993 Dec.  Includes references.
Language:  English
Descriptors: Zea mays; Nicotiana tabacum; Transgenics; Beta-glucuronidase;Gene expression; Genetic analysis; Genetic transformation; Histochemistry;Promoters; Protoplasts; Tubulin
17                                                    NAL Call. No.: QK710.P62Analysis of nuclear proteins interacting with a wheat alpha/beta-gliadin andstorage protein gene.Vellanoweth, R.L.; Okita, T.W.Dordrecht : Kluwer Academic Publishers; 1993 Apr.Plant molecular biology v. 22 (1): p. 25-41; 1993 Apr.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Promoters; Structural genes; Gliadin; Bindingsite; Dna binding proteins; Nucleotide sequences; Seeds; Seed development;Gene expression; Genetic regulation
Abstract:  The promoter region (-524 to -46) of the wheat alpha/beta-gliadinseed storage protein gene was analyzed for interactions with nuclear proteinsfrom developing wheat seeds. Six complexes were detected within the first 165bp upstream of the transcriptional start site. One of the proteins was anon-sequence specific AT-binding protein. The remaining five proteins bound ina sequence specific manner. One (CABP) mapped to a conserved CA-rich elementat -134 to -112 while another (PalBP) mapped to an adjacent, palindromicsequence at -112 to -106. Three proteins (CTBPs 1-3) formed complexes at two,independent homologous sites. The activities of four of the binding proteins,CTBPs 1-3 and CABP, exhibited similar patterns of expression during seeddevelopment: they first appeared at early to mid stages, reached a maximum atmid stage and subsequently decreased, paralleling the pattern of gliadin mRNAaccumulation. The non-specific AT-binding protein was detected at relativelyhigh levels only at mid development. PAlBP activity, on the other hand, firstappeared at mid stage and was present at a constant level throughout laterstages of development. The results suggest that the binding proteins mayregulate gliadin expression in an antagonistic manner.
18                                                    NAL Call. No.: QK710.P62Analysis of the gibberellin-responsive promoter of a cathepsin B-like genefrom wheat.Cejudo, F.J.; Ghose, T.K.; Stabel, P.; Baulcombe, D.C.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (5): p. 849-859; 1992 Dec.Includes references.
Language:  English
Descriptors: Triticum aestivum; Promoters; Structural genes; Plant proteins;Cathepsins; Recombinant  DNA; Beta-glucuronidase; Reporter genes; Geneexpression; Genetic regulation; Gibberellic acid; Aleurone layer; Nucleotidesequences; Controlling elements
Abstract:  A wheat gene (A121) encoding a protein with sequence similarity tomammalian cathepsin B is regulated by gibberellic acid (GA) in aleurone layersof germinating grains. To analyse the mechanism of A121 regulation, itspromoter was fused to the beta-glucuronidase reporter gene (GUS) andintroduced by micro-projectile bombardment into aleurone layers of oat. With2.3 kb of promoter sequence, the GUS expression was enhanced by GA treatment.This effect was reversed by abscisic acid (ABA). This result showed for A121,like the alpha-amylase genes, that the regulation by GA and ABA was at thelevel of transcription. The GA responsiveness of the promoter was retainedwith as little as 276 bp of promoter sequence. Sequence comparison with a GAresponsive promoter of an alpha-amylase gene identified the conserved elementGCAACGGCAACGATGG which is required intact for full expression of bothpromoters. However, there was no identifiable similarity in the cathepsin-likepromoter with the GA-responsive element of alpha-amylase promoters with theconsensus sequence TAACAAA, suggesting that GA affects more than one mechanismof transcriptional control.
19                                                    NAL Call. No.: QK710.P68Analysis of three tissue-specific elements from the wheat Cab-1 enhancer.Gotor, C.; Romero, L.C.; Inouye, K.; Lam, E.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Apr.The plant journal v. 3 (4): p. 509-518; 1993 Apr.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Nicotiana tabacum; Genetic code; Lightharvesting complexes; Chlorophyll a/b binding protein; Gene expression;Regulation; Light; Transcription; Enhancers; Transgenic plants; Gene mapping;Nucleotide sequences; Dna footprinting
20                                                     NAL Call. No.: 442.8 Z8Antisense regulation of the rice waxy gene expression using a PCR-amplifiedfragment of the rice genome reduces the amylose content in grain starch.Shimada, H.; Tada, Y.; Kawasaki, T.; Fujimura, T.Berlin, W. Ger. : Springer International; 1993 Jul.Theoretical and applied genetics v. 86 (6): p. 665-672; 1993 Jul.  Includesreferences.
Language:  English
Descriptors: Oryza sativa; Structural genes; Hexosyltransferases; Geneexpression; Genetic regulation; Antisense  DNA; Gene transfer; Genetictransformation; Transgenic plants; Recombinant  DNA; Reporter genes;Beta-glucuronidase; Enzyme activity; Histoenzymology; Amylose; Starch;Carbohydrate metabolism; Seeds; Callus
Abstract:  The waxy gene encodes a granule-bound starch synthase. A 1.0-kbportion of the sequence of the rice waxy gene, which includes the regionbetween exon 4 and exon 9, was inserted in an antisense orientation betweenthe 35 S promoter and the GUS gene of pBI221. The resultant plasmid, pWXA23,was introduced into rice protoplasts by electroporation. GUS activity wasclearly detected in derived callus lines, suggesting that the antisensecomponent of the fusion gene was also expressed. Transgenic rice plants wereregenerated from these callus lines and their GUS activity was confirmed. Someof the rice seeds from these transformants showed a significant reduction inthe amylose content of grain starch, even though they had become polyploid.These results suggest that even when intron sequences are included, antisenseconstructs can bring about a reduced level of expression of a target gene. Theutility of GUS, included as a reporter gene, for the simple detection ofexpression of an antisense gene, was apparent from these results.
21                                                    NAL Call. No.: QK710.P62AT-rich promoter elements of soybean heat shock gene Gmhsp17.5E bind twodistinct sets of nuclear proteins in vitro.Czarnecka, E.; Ingersoll, J.C.; Gurley, W.B.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 985-1000; 1992 Sep.Includes references.
Language:  English
Descriptors: Glycine max; Agrobacterium tumefaciens; Helianthus annuus;Structural genes; Multigene families; Heat shock proteins; Promoters; Bindingsite; Dna binding proteins; Nucleotide sequences; Genetic regulation; Geneexpression; Transcription; Alcohol dehydrogenase; Zea mays; Genetictransformation; Ultraviolet radiation; Chemical reactions
Abstract:  A 33 bp double-stranded oligonucleotide homologous to two AT-richsequences located upstream (-907 to -889 and -843 to -826) to the start oftranscription of heat shock gene Gmhsp7.5E of soybean stimulated transcriptionwhen placed 5' to a truncated (-140) maize Adh1 promoter. The chimericpromoter was assayed in vivo utilizing anaerobically stressed sunflower tumorstransformed by a pTi-based vector of Agrobacterium tumefaciens. Nuclearproteins extracted from soybean plumules were shown to bind double-strandedoligonucleotides homologous to AT-rich sequences in the 5' flanking regions ofsoybean beta-conglycinin, lectin, leghemoglobin and heat shock genes. Theseproteins were also shown to bind AT-rich probes homologous to homeobox proteinbinding sites from the Antennapedia and engrailed/fushi tarazu genes ofDrosophila. Binding activity specific for AT-rich sequences showed a widedistribution among various plant organs and species. Preliminarycharacterization indicated that two sets of nuclear proteins from soybean bindAT-rich DNA sequences: a diverse high-molecular-weight (ca. 46-69 kDa) group,and a low-molecular-weight (23 and 32 kDa) group of proteins. The latter meetsthe operational criteria for high-mobility group proteins (HMGs).
22                                                    NAL Call. No.: QK710.P62Bare-1, a copia-like retroelement in barley (Hordeum vulgare L.).Manninen, I.; Schulman, A.H.Dordrecht : Kluwer Academic Publishers; 1993 Aug.Plant molecular biology v. 22 (5): p. 829-846; 1993 Aug.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Retrotransposons; Repetitive  DNA; Nucleotidesequences; Southern blotting; Gene expression; Messenger  RNA; Restrictionmapping; Molecular mapping; Amino acid sequences; Plant proteins; Proteinases;Nucleases; Reverse transcriptase
Abstract:  Retroviruses and retrotransposons make up the broad class ofretroelements replicating and transposing via reverse transcriptase.Retroelements have recently been found to be ubiquitous in the plants. Wereport here the isolation, sequence and analysis of a retroelement from barley(Hordeum vulgare L.) with all the features of a copia-like retrotransposon.This is named BARE-1 (for Barley Retroelement 1), the first such elementdescribed for barley. BARE-1 is 12 088 bp, with long terminal repeats (LTRs)of 1829 bp containing perfect 6 bp inverted repeats at their ends and flankedby 4 bp direct repeats in the host DNA. Between the long terminal repeats isan internal domain with a derived amino acid sequence of 1285 residues,bearing homology to the gag, pro, int and rt domains of retroviruses and bothplant and non-plant copia-like retrotransposons. Cultivated barley containsabout 5000 elements in the genome similar to the BARE-1 putative gag domain,but ten-fold more hybridizing to rt or LTR probes. The particular BARE-1element reported here appears to be inactive, as the putative protein-codingdomain is interrupted by four stop codons and a frameshift. In addition, the3' LTR is 4% divergent from the 5' LTR and contains a 3135 bp insertion.Nevertheless, we have recently detected transcripts hybridizing to BARE-1 onnorthern blots, presumably from active copies. Analysis of BARE-1 expressionand function in barley is currently underway.
23                                                    NAL Call. No.: QK710.P62A barley cDNA clone encoding a type III chlorophyll a/b binding polypeptide ofthe light-harvesting complex II.Brandt, J.; Nielsen, V.S.; Thordal-Christensen, H.; Simpson, D.J.; Okkels,J.S.Dordrecht : Kluwer Academic Publishers; 1992 Jul.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (4): p. 699-703; 1992 Jul.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Multigene families; Structural genes;Chlorophyll a/b binding protein; Dna; Nucleotide sequences; Amino acidsequences; Thylakoids; Gene expression; Messenger  RNA; Genetic regulation;Light; Light harvesting complexes
Abstract:  The nucleotide sequence of a leaf cDNA clone encoding a Type IIIchlorophyll a/b-binding (CAB) protein of light-harvesting complex II (LHCII)in barley is reported. Sequence comparisons and results from in vitro importinto chloroplasts demonstrate that the cDNA clone encodes a functional transitpeptide of 45 amino acid residues and a mature polypeptide of 223 residueswith a predicted molecular mass of 24.3 kDa. After insertion into thylakoids,the mature protein is resistant to protease attack. Hybridization analysisusing a gene-specific probe shows that the gene is expressed in dark-grownseedlings and that the amount of mRNA increases during illumination.
24                                                    NAL Call. No.: 442.8 Z34Barley embryo globulin 1 gene, Beg1: characterization of cDNA, chromosomemapping and regulation of expression.Heck, G.R.; Chamberlain, A.K.; Ho, T.H.D.Berlin, W. Ger. : Springer International; 1993 May.Molecular & general genetics : MGG v. 239 (1/2): p. 209-218; 1993 May.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Globulins; Plant embryos;Complementary  DNA; Nucleotide sequences; Amino acid sequences; Gene location;Chromosomes; Chromosome maps; Gene expression; Messenger  RNA; Seeddevelopment; Aleurone layer
Abstract:  We report identification of a 2189 bp cDNA clone from barleycorresponding to a single-copy gene, Beg] (Barley embryo globulin), onchromosome 4, which encodes a storage globulin. In barley, the major proteinreserve in the aleurone layer belongs to the 7S globulin class of proteinsfound in many seeds. Electrophoretically and antigenically similar proteinsare present in the barley embryo. Accumulation of Beg1 mRNA was notedbeginning 15-20 days post-anthesis in both the aleurone layer and embryo ofthe developing barley grain but not in the starchy endosperm. A high level ofBeg1 mRNA is also present in the mature imbibed aleurones, which can berepressed by treatment with gibberellic acid. This repressive effect ofgibberellin on the levels of Beg1 mRNA is confirmed in the gibberellinresponse-constitutive mutant, slender, whose aleurone layers do not accumulateBeg1 mRNA even in the absence of applied gibberellic acid. The deduced primarytranslation product of the Beg1 mRNA is a 637 amino acid (72 kDa) protein withhomology to maize embryo globulin 1 (GLB1) and a partial sequence of a wheat7S globulin. The internal amino acid sequence of BEG1 closely matches theN-terminal sequence of isolated barley aleurone globulin. Seven imperfecttandem repeats of 16 amino acids each are present near the N-terminus of BEG1,which conform to the consensus HGEGEREEEXGRGRGR, and contribute to theobserved unusual amino acid composition of this protein. A second, distinctbarley globulin gene, Beg2, which is homologous to maize Glb2, was detected byNorthern and Southern analysis. Beg2 and Beg1 are regulated differently whichmay indicate variation in storage or utilization properties among the barleyglobulins.
25                                                    NAL Call. No.: QK725.P54beta-Glucuronidase gene expression and mRNA stability in oat protoplasts.Higgs, D.C.; Colbert, J.T.Berlin, W. Ger. : Springer International; 1993.Plant cell reports v. 12 (7/8): p. 445-452; 1993.  Includes references.
Language:  English
Descriptors: Avena sativa; Cell suspensions; Protoplasts; Gene expression;Messenger  RNA; Dna; Electroporation; Plasmids; Gene transfer; Genetic code;Beta-glucuronidase; Reporter genes; Enzyme activity; Radioactive tracers; Halflife; Transcription; Regulation
Abstract:  Protoplasts derived from oat (Avena sativa L.) suspension culturecells (7 days after subculturing) were electroporated with plasmid DNAcontaining the Escherichia coli uidA gene encoding the beta-glucuronidasereporter enzyme. Consistently high enzyme activity was observed withelectroporation conditions of 500 micro F and 1125 volts/cm. Enzyme activityand mRNA accumulation time courses were determined. The maximum enzymeactivity was detected at 24 hours after electroporation, while the maximummRNA level was detected at 12 hours after electroporation. beta-glucuronidasemRNA was in vitro synthesized with and without a 5' methylated cap and thenelectroporated into protoplasts. Only capped mRNA produced significant enzymeactivity. By electroporating radiolabeled, in vitro synthesized mRNA, thebeta-glucuronidase mRNA half-life was estimated to be approximately 35 minutesin oat protoplasts.
26                                                     NAL Call. No.: QH442.B5Bialaphos treatment of transgenic rice plants expressing a bar gene preventsinfection by the sheath blight pathogen (Rhizoctonia solani).Uchimiya, H.; Iwata, M.; Nojirl, C.; Samarajeewa, P.K.; Takamatsu, S.; Ooba,S.; Anzai, H.; Christensen, A.H.; Quail, P.H.; Toki, S.New York, N.Y. : Nature Publishing,; 1993 Jul.Bio/technology v. 11 (7): p. 835-836; 1993 Jul.  Includes references.
Language:  English
Descriptors: Oryza sativa; Rhizoctonia solani; Transgenic plants; Genetictransformation; Disease resistance; Glyphosate; Herbicide resistance; Blight;Structural genes; Acyltransferases
27                                              NAL Call. No.: S494.5.B563B554Biochemical and molecular studies of stress tolerance in barley.Stanca, A.M.; Terzi, V.; Cattivelli, L.Wallingford, Oxford, UK : CAB International; 1992.Biotechnology in agriculture (5): p. 277-288; 1992.  In the series analytic:Barley : genetics, biochemistry, molecular biology and biotechnology / editedby P.R. Shewry.  Includes references.
Language:  English
Descriptors: Hordeum; Environmental factors; Stress factors; Stress response;Genetic regulation; Gene expression; Molecular genetics; Biochemical pathways;Heat shock; Cold hardening; Drought; Salinity; Heavy metals; Oxygen
28                                                     NAL Call. No.: 450 P692Bronze-2 gene expression and intron splicing patterns in cells and tissues ofZea mays L.Nash, J.; Walbot, V.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Sep.Plant physiology v. 100 (1): p. 464-471; 1992 Sep.  Includes references.
Language:  English
Descriptors: Zea mays; Genes; Gene expression; Messenger  RNA; Introns;Alternative splicing; Cell culture; Protoplasts
Abstract:  A large fraction of the transcripts of the Bronze-2 (Bz2) gene ofmaize (Zea mays L.) are unspliced in purple husk tissues. The accumulation ofunspliced messages could have destructive potential if the intron-bearingmRNAs are translated into aberrant proteins. Our initial studies suggestedthat both genetic and physiological factors may influence the degree ofsplicing failure. Nuclear background rather than cis-sequence effects is shownto contribute to the genetic component. The accumulation of unspliced messagedoes not appear to be directly influenced by diurnal effects on transcriptabundance, by the expression level of the Bz2 gene, or by thermal stress. Wealso show that maize cell cultures (Black Mexican Sweet, BMS) can be used toexamine the molecular details involved in splicing failure. Much like wholemaize plants, the BMS cells excise the Bz2 intron with varying degrees ofefficiency. In contrast with heterologous constructs containing plant introns,splicing of the native Bz2 intron can appproach 100% in BMS cells. Splicing oftranscripts from a marked, introduced gene can be compared to the endogeneousBz2 gene facilitating analysis of the impact of sequence changes.
29                                                    NAL Call. No.: QK710.P62The cab-m7 gene: a light-inducible, mesophyll-specific gene of maize.Becker, T.W.; Templeman, T.S.; Viret, J.F.; Bogorad, L.Dordrecht : Kluwer Academic Publishers; 1992 Oct.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (1): p. 49-60; 1992 Oct.  Includesreferences.
Language:  English
Descriptors: Zea mays; Multigene families; Multiple genes; Chlorophyll a/bbinding protein; Gene expression; Messenger  RNA; Genetic regulation; Light;Mesophyll; Etiolation; Nucleotide sequences; Amino acid sequences
Abstract:  Southern blot analysis has revealed the existence in maize ofperhaps 12 members of the nuclear cab multigene family encoding thechlorophyll a- and b-binding proteins of the photosystem II light-harvestingcomplex. Hybridization with 3' probes derived from unsequenced cDNA clonesshowed that six members of this family differ from one another with respect toexpression in mesophyll and/or bundle sheath cells and regulation by light. Anadditional member of this family, designated cab-m7, that encodes a 28 kDaprimary translation product has now been identified. It has been cloned from amaize genomic library and sequenced to begin to define the bases fordifferences in the expression of these genes. This cab gene is shown to bestrongly preferentially expressed in the mesophyll (vs. bundle sheath) cellsof maize. Furthermore, the gene is photo-responsive; although small amounts ofcab-m7 mRNA are present in etiolated leaves, the mRNA pool is 8-fold largerafter six hours of illumination. DNA sequences upstream of the cab-m7 generesemble those found in the 5'-flanking regions of some other plant genes.
30                                                    NAL Call. No.: QK710.P62A cDNA clone for a pathogenesis-related protein 1 from barley.Muradov, A.; Petrasovits, L.; Davidson, A.; Scott, K.J.Dordrecht : Kluwer Academic Publishers; 1993 Oct.Plant molecular biology v. 23 (2): p. 439-442; 1993 Oct.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Complementary  DNA; Pathogenesis-relatedproteins; Nucleotide sequences; Amino acid sequences; Gene expression;Messenger  RNA; Genetic regulation; Fungal diseases; Erysiphe graminis f.sp.hordei; Ethylene; Salicylic acid; Jasmonic acid; Nicotinic acid; Derivatives
Abstract:  A barley cDNA clone (PRb-1) corresponding to an mRNA differentiallyinduced in resistant compared to susceptible barley cultivars by powderymildew infection was isolated and characterised. The deduced amino acidsequence revealed 24 amino acids comprising the signal peptide and 140 aminoacids of the mature peptide (15 kDa). This showed close homology to PR-1-likeproteins, which have been isolated from maize, tobacco, tomato and Arabidopsisthaliana. Northern blot analysis showed accumulation of the corresponding mRNA12 h after inoculation of resistant barley cultivars with Erysiphe graminis.Increased expression of the PRb-1 gene was also observed in resistant comparedwith near-isogenic susceptible barley plants following treatment withethylene, salicylic acid, methyl jasmonate and 2,6-dichloro-isonicotinic acid.
31                                                    NAL Call. No.: SB599.P45cDNA cloning and characterization of two barley peroxidase transcripts induceddifferentially by the powdery mildew fungus Erysiphe graminis.Thordal-Christensen, H.; Brandt, J.; Cho, B.H.; Rasmussen, S.K.; Gregersen,P.L.; Smedegaard-Petersen, V.; Collinge, D.B.London : Academic Press; 1992 Jun.Physiological and molecular plant pathology v. 40 (6): p. 395-409; 1992 Jun.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Peroxidase; Dna libraries; Erysiphe graminis;Nucleotide sequences; Amino acid sequences; Gene expression
Abstract:  A cDNA library of RNA from barley leaves inoculated with Erysiphegraminis was screened using labelled cDNA enriched for specific sequences bysubtractive hybridization against RNA from non-inoculated leaves. Thisresulted in isolation of several clones representing pathogen induced genes.By cross-hybridization and sequence analysis, one of the cDNAs (pBT6-3) wasfound to be a partial clone representing a putative peroxidase, for which afull-length cDNA clone (pBH6-301) was subsequently isolated. The predictedamino acid sequence revealed a 21 amino acid signal peptide and a 294 aminoacid mature protein (31 kDa) and shows 56% amino acid identity to a basicperoxidase from turnip, 89% to a putative peroxidase from wheat, but only 38%to the amino acid sequence derived from the cDNA clone (pcD1311) of a secondputative barley peroxidase expressed in leaves. Northern blot analysis showedthat the pBT6-3 (pBH6-301) transcript is elevated as early as 4 h afterinoculation with E. graminis f. sp hordei and that two maxima in transcriptlevels appear, which can be correlated with penetration attempts by thefungus. The amount of the pcD1311 transcript was also found to increase ininoculated leaves but at a later time point.
32                                                    NAL Call. No.: QK710.P62cDNA cloning and gene expression of the major prolamins of rice.Shyur, L.F.; Wen, T.N.; Chen, C.S.Dordrecht : Kluwer Academic Publishers; 1992 Oct.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (2): p. 323-326; 1992 Oct.Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Dna; Prolamins; Nucleotidesequences; Amino acid sequences; Peptides; Seed development; Gene expression;Messenger  RNA
Abstract:  A full-length cDNA (pS 18) encoding the 16 kDa rice prolamincomposed of 158 amino acids was sequenced. Analysis of N-terminal amino acidsequence of a major rice prolamin indicated that an 18 amino acid signalpeptide was removed from 16 kDa precursor prolamin to form the 14 kDa prolaminduring seed development. Synthesis of the 16 kDa precursor prolamin beganaround 8 days after flowering (DAF), increased remarkably at 8-11 DAF andgradually reached maximum levels with the maturation of rice seeds.
33                                                     NAL Call. No.: 450 P692cDNA cloning and sequence analysis of a pathogen-induced thaumatin-likeprotein from rice (Oryza sativa).Reimmann, C.; Dudler, R.Rockville, Md. : American Society of Plant Physiologists; 1993 Mar.Plant physiology v. 101 (3): p. 1113-1114; 1993 Mar.  Includes references.
Language:  English
Descriptors: Oryza sativa; Complementary  DNA; Cloning; Pathogenesis-relatedproteins; Nucleotide sequences; Amino acid sequences; Gene expression; Geneticregulation; Pseudomonas syringae pv. syringae
34                                                    NAL Call. No.: QK710.P62cDNA nucleotide sequence and expression of a maize cytoplasmic ribosomalprotein S13 gene.Joanin, P.; Gigot, C.; Philipps, G.Dordrecht : Kluwer Academic Publishers; 1993 Feb.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (4): p. 701-704; 1993 Feb.Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Multigene families; Ribosomes;Proteins; Nucleotide sequences; Amino acid sequences; Cytoplasm; Geneexpression; Transcription; Messenger  RNA; Cell differentiation
Abstract:  The complete amino acid sequence of a cytoplasmic ribosomal proteinS13 of maize was deduced from the cDNA isolated from a maize cDNA library. Theencoded protein is 151 amino acids long and shows a homology of 73% with thecorresponding protein S13 of rat. Southern blots analysis shows that the maizeprotein S13 is encoded by a small multigene family conserved in plant speciesclosely related to maize. The S13 RNAs accumulate preferentially inproliferating tissues and cells and their transcription occurs in parallel tothe DNA synthesis.
35                                                    NAL Call. No.: QK710.P62cDNA nucleotide sequence and expression of a maize cytoplasmic ribosomalprotein S13 gene.Joanin, P.; Gigot, C.; Philipps, G.Dordrecht : Kluwer Academic Publishers; 1993 Feb.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (4): p. 701-704; 1993 Feb.Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Multigene families; Ribosomes;Proteins; Nucleotide sequences; Amino acid sequences; Cytoplasm; Geneexpression; Transcription; Messenger  RNA; Cell differentiation
Abstract:  The complete amino acid sequence of a cytoplasmic ribosomal proteinS13 of maize was deduced from the cDNA isolated from a maize cDNA library. Theencoded protein is 151 amino acids long and shows a homology of 73% with thecorresponding protein S13 of rat. Southern blots analysis shows that the maizeprotein S13 is encoded by a small multigene family conserved in plant speciesclosely related to maize. The S13 RNAs accumulate preferentially inproliferating tissues and cells and their transcription occurs in parallel tothe DNA synthesis.
36                                                     NAL Call. No.: 450 AM36Cell- and tissue-specific expression of rice histone gene transcripts duringanther and pollen development in henbane (Hyoscyamus niger).Raghavan, V.; Jiang, C.; Bimal, R.Columbus, Ohio : Botanical Society of America; 1992 Jul.American journal of botany v. 79 (7): p. 778-783; 1992 Jul.  Includesreferences.
Language:  English
Descriptors: Hyoscyamus niger; Anthers; Pollen; Gene expression; Histones;Hybridization; Transcription; Plant development; Spores; Ultrastructure; Oryzasativa
Abstract:  We have monitored by in situ hybridization the cell- andtissue-specific expression of a rice histone H3 gene during anther and pollendevelopment in henbane (Hyoscyamus niger). Autoradiographic silver grainsgenerated by hybridization of 35S-labeled antisense probe were present in moreor less the same density in all the cells of the anther primordium. Duringlater development of the anther, there was a sequential accumulation ofhistone mRNA beginning in the epidermis on the outside and ending in thetapetum inside. These changes in transcript abundance in the sporophytic cellsof the anther were also related to the stage of microsporogenesis. Transcriptlevel increased during sporogenesis and reached a maximum in mature pollengrains collected from open flowers.
37                                                     NAL Call. No.: 500 N21PCell type-preferred expression of maize cab-m1: repression in bundle sheathcells and enhancement in mesophyll cells.Bansal, K.C.; Bogorad, L.Washington, D.C. : The Academy; 1993 May01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (9): p. 4057-4061; 1993 May01.  Includes references.
Language:  English
Descriptors: Zea mays; Chlorophyll a/b binding protein; Gene expression;Genetic code; Light harvesting complexes; Nucleotide sequences; Photosystemii; Transcription
Abstract:  Different sets of genes for photosynthesis are expressed inmesophyll cells (MCs) and bundle sheath cells (BSCs)--the two adjacent butmorphologically and functionally distinct types of photosynthetic cells inleaves of maize and other C4 plants. For example, light-harvesting chlorophylla/b-binding proteins of photosystem II, which are encoded by a family of cabgenes, are 3- to 4-fold more abundant in maize MCs than in BSCs. Each maizecab gene is different from the others in its relative expression in MCs vs.BSCs and in its degree of photoresponsiveness. The gene cab-m1 is positivelyphotoregulated and is highly preferentially expressed in MCs. A 159-bpsequence in the 5' flanking region of this gene (-1026 to -868 relative to thetranslation start site) is required for MC-preferred expression of a reportergene in greening maize leaves. Deletion as well as gain-of-functionexperiments have now shown that all of the sequence information required forMC-preferred expression resides within this mesophyll-specifying region andthat cab-m1 is preferentially expressed in MCs because of the presence of twotypes of sequence elements: one is required for suppressing expression in BSCsand the other for promoting expression in MCs. One of the four cis-actingregions mapped within the mesophyll-specifying region resembles the AT-1 boxof some plant gene negative regulatory elements. Various combinations of suchMC-specific enhancing and BSC-specific repressing regions could make maize cabgene family members different from one another in their relative expression inMCs vs. BSCs.
38                                              NAL Call. No.: S494.5.B563B554Cell wall metabolism in barley.Fincher, G.B.Wallingford, Oxford, UK : CAB International; 1992.Biotechnology in agriculture (5): p. 413-437; 1992.  In the series analytic:Barley : genetics, biochemistry, molecular biology and biotechnology / editedby P.R. Shewry.  Includes references.
Language:  English
Descriptors: Hordeum; Cell walls; Cell wall components; Metabolism;Beta-glucanase; Isoenzymes; Nucleotide sequences; Genetic regulation; Geneexpression; Genetic engineering; Genetic transformation; Malting quality; Seedgermination; Grain; Ultrastructure; Evolution
39                                                    NAL Call. No.: QK710.P62Cell-type specific expression of three rice genes GOS2, GOS5 and GOS9.Rey, P.; Diaz, C.; Schilperorrt, R.A.; Hensgens, L.A.M.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 889-894; 1993 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Gene expression; Messenger  RNA; Transcription;Structural genes; Plant proteins; Leaves; Roots; Parenchyma; Photosystem i
Abstract:  The cell-type-specific expression of three rice genes, GOS2, GOS5and GOS9, was studied by mRNA in situ hybridization. Previous northern blotanalysis revealed that these genes were constitutive, green tissue-specificand root-specific, respectively. In this study, GOS2 transcripts were observedin all leaf cell types. In roots, a temporal and spatial expression patternwas noticed. Higher mRNA levels were observed in lateral roots, especially inparenchymal cells of the vascular cylinder. Expression of GOS5 was mainlyfound in chloroplast-containing cells. For GOS9, significant levels of signalwere observed in root and leaf sections.
40                                                     NAL Call. No.: 450 P692Characterization of a cold-regulated wheat gene related to Arabidopsis cor47.Guo, W.; Ward, R.W.; Thomashow, M.F.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Oct.Plant physiology v. 100 (2): p. 915-922; 1992 Oct.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Arabidopsis thaliana; Complementary  DNA;Structural genes; Plant proteins; Nucleotide sequences; Amino acid sequences;Glycine; Threonine; Histidine; Messenger  RNA; Gene expression; Seeds; Geneticregulation; Cold; Acclimatization; Leaves; Roots; Abscisic acid; Water stress
Abstract:  The cDNA clone pWG1 represents a gene, designated cor39, fromTriticum aestivum L. cv Winoka (a winter wheat) that is related to acold-regulated Arabidopsis thaliana L. (Heyn) gene, cor47. In vitrotranscription/translation experiments in conjunction with DNA sequenceanalysis indicated that cor39 encodes a hydrophilic polypeptide of 39 kD(isoelectric point of 7.5), designated COR39. The polypeptide is composedprimarily of two sequences, each of which is repeated six times. One sequence,which is lysine rich, occurs in COR47 (the polypeptide encoded by Arabidopsiscor47) and group II LEA proteins, polypeptides hypothesized to have roles indesiccation and drought tolerance). Baker, C. Steele, L. Dure III [1988] PlantMol Biol 11: 277-291). The second sequence, which is glycine rich, occurs insome, but not all, group II LEA proteins. Southern analysis indicated thatwheat has a number of loci related to cor39. Transcripts of about 3.3, 1.5,and 0.8 kb that hybridize with cor39 were found to accumulate in leaf, root,and crown tissues of cold-acclimated plants; they accumulated rapidly inresponse to low temperature and returned quickly to low levels when plantswere returned to normal growth temperature. Transcripts hybridizing with cor39were present at relatively high levels in wheat seeds and accumulated inplants in response to exogenous application of ABA and water stress. Thesimilarities in expression of wheat and Arabidopsis cor genes and possiblefunctional relationships among COR39, COR47, and LEA proteins are discussed.
41                                                    NAL Call. No.: QK710.P68Characterization of the catalase antioxidant defense gene Cat1 of maize, andits developmentally regulated expression in transgenic tobacco.Guan, L.; Scandalios, J.G.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Apr.The plant journal v. 3 (4): p. 527-536; 1993 Apr.  Includes references.
Language:  English
Descriptors: Nicotiana tabacum; Zea mays; Genome analysis; Clones; Dna;Nucleotide sequences; Amino acid sequences; Transgenic plants; Geneexpression; Transcription; Beta-glucuronidase; Enzyme activity; Flowering;Developmental stages
42                                                    NAL Call. No.: QK710.P62Characterization of the U3 and U6 snRNA genes from wheat: U3 snRNA genes inmonocot plants are transcribed by RNA polymerase III.Marshallsay, C.; Connelly, S.; Filipowicz, W.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 973-983; 1992 Sep.Includes references.
Language:  English
Descriptors: Triticum aestivum; Multigene families; Small nuclear  RNA;Ribosomal  DNA; Transcription; Gene expression; Rna polymerase; Enzymeactivity; Promoters; Controlling elements; Genetic transformation; Zea mays;Nucleotide sequences; Direct  DNAuptake; Protoplasts; Phylogeny; Molecularconformation
Abstract:  We have demonstrated recently that the genes encoding the U3 smallnuclear RNA (snRNA) in dicot plants are transcribed by RNA polymerase III (polIII), and not RNA polymerase II (pol II) as in all other organisms studied todate. The U3 gene was the first example of a gene transcribed by differentpolymerases in different organisms. Based on phylogenetic arguments weproposed that a polymerase specificity change of the U3 snRNA gene promoteroccurred during plant evolution. To map such an event we are examining the U3gene polymerase specificity in other plant species. We report here thecharacterization of a U3 gene from wheat, a monocot plant. This gene containsthe conserved promoter elements, USE and TATA, in a pol III-specific spacingseen also in a wheat U6 snRNA gene characterized in this report. Both the U3and the U6 genes possess typical pol III termination signals but lack the ciselement, responsible for 3'-end formation, found in all plant pol II-specificsnRNA genes. In addition, expression of the U3 gene in transfected maizeprotoplasts is less sensitive to alpha-amanitin than a pol II-transcribed U2gene. Based on these data we conclude that the wheat U3 gene is transcribed bypol III. This observation suggests that the postulated RNA polymerasespecificity switch of the U3 gene took place prior to the divergence ofangiosperm plants into monocots and dicots.
43                                                    NAL Call. No.: QH426.D32Characterization of two maize HSP90 heat shock protein genes: expressionduring heat shock, embryogenesis, and pollen development.Marrs, K.A.; Casey, E.S.; Capitant, S.A.; Bouchard, R.A.; Dietrich, P.S.;Mettler, I.J.; Sinibaldi, R.M.New York, N.Y. : Wiley-Liss, Inc; 1993.Developmental genetics v. 14 (1): p. 27-41; 1993.  In the special issue: Focuson heat shock genes (part 1) / edited by J.J. Heikkila.  Includes references.
Language:  English
Descriptors: Zea mays; Multigene families; Heat shock proteins; Structuralgenes; Nucleotide sequences; Amino acid sequences; Promoters; Gene expression;Genetic regulation; Heat shock; Embryogenesis; Gametogenesis; Pollen; Bindingsite; Dna binding proteins; Messenger  RNA
Abstract:  We have isolated two genes from Zea mays encoding proteins of 82and 81 kD that are highly homologous to the Drosophila 83-kD heat shockprotein gene and have analyzed the structure and pattern of expression ofthese two genes during heat shock and development. Southern blot analysis andhybrid select translations indicate that the highly homologous hsp82 and hsp81genes are members of a small multigene family composed of at least two andperhaps three or more gene family members. The deduced amino acid sequence ofthese proteins based on the nucleotide sequence of the coding regions shows64-88% amino acid homology to other hsp90 family genes from human, yeast,Drosophila, and Arabidopsis. The promoter regions of both the hsp82 and hsp81genes contain several heat shock elements (HSEs), which are putative bindingsites for heat shock transcription factor (HSF) commonly found in thepromoters of other heat shock genes. Gene-specific oligonucleotide probes weresynthesized and used to examine the mRNA expression patterns of the hsp81 andhsp82 genes during heat shock, embryogenesis, and pollen development. Thehsp81 gene is only mildly heat inducible in leaf tissue, but is stronglyexpressed in the absence of heat shock during the pre-meiotic and meioticprophase stages of pollen development and in embryos, as well as inheat-shocked embryos and tassels. The hsp82 gene shows strong heatinducibility at heat-shock temperatures (37-42 degrees C) and in heat shockedembryos and tassels but is only weakly expressed in the absence of heat shock.Promoter-GUS reporter gene fusions made and analyzed by transient expressionassays in Black Mexican Sweet (BMS) Maize protoplasts also indicate that thehsp82 and hsp81 are regulated differentially. The hsp82 promoter confersstrong heat-inducible expression of the GUS reporter gene in heat-treatedcells (60- to 80-fold over control levels), whereas the hsp81 promoter is onlyweakly heat inducible (5- to 10-fold over control levels).
44                                                    NAL Call. No.: QH506.E46Chloroplasts rps15 and the rpoB/C1/C2 gene cluster are strongly transcribed inribosome-deficient plastids: evidence for a functioningnon-chloroplast-encoded RNA polymerase.Hess, W.R.; Prombona, A.; Fieder, B.; Subramanian, A.R.; Borner, T.Oxford, Eng. : IRL Press; 1993 Feb.The EMBO journal - European Molecular Biology Organization v. 12 (2): p.563-571; 1993 Feb.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Secale cereale; Transcription; Chloroplasts; Rnapolymerase; Enzyme activity; Ribosomes; Gene expression; Messenger  RNA;Structural genes; Mutants
Abstract:  Transcription of plastid genes and transcript accumulation wereinvestigated in white leaves of the albostrians mutant of barley (Hordeumvulgare) and in heat-bleached leaves of rye (Secale cereale) as well as innormal green leaves of both species. Cells of white leaves of the mutant andcells of heat-bleached leaves bear undifferentiated plastids lacking ribosomesand, consequently, plastid translation products, among them the subunits of aputative chloroplast RNA polymerase encoded by the plastid genes rpoA, B, C1and C2. The following results were obtained. (i) Plastid genes are transcribeddespite the lack of chloroplast gene-encoded RNA polymerase subunits. Theplastid origin of these transcripts was proven. This finding provides evidencefor the existence of a plastid RNA polymerase encoded entirely by nucleargenes. (ii) Transcripts of the rpo genes and of rps15, but not of genesinvolved in photosynthesis and related processes (psbA, rbcL, atpI-H), wereabundantly accumulated in ribosome-deficient plastids. In contrast,chloroplasts accumulated transcripts of photosynthetic, but not of the rpogenes. (iii) Differences in transcript accumulation between chloroplasts andribosome-deficient plastids are due to different relative transcription ratesand different transcript stability. (iv) The observed differences intranscription are not caused by an altered pattern of methylation of plastidDNA. Thus, the prokaryotic plastid genome of higher plants is transcribed bytwo RNA polymerases. The observed differences in transcription betweenchloroplasts and undifferentiated plastids might reflect different functionsof the two enzymes.
45                                                    NAL Call. No.: QH506.E46Chloroplasts rps15 and the rpoB/C1/C2 gene cluster are strongly transcribed inribosome-deficient plastids: evidence for a functioningnon-chloroplast-encoded RNA polymerase.Hess, W.R.; Prombona, A.; Fieder, B.; Subramanian, A.R.; Borner, T.Oxford, Eng. : IRL Press; 1993 Feb.The EMBO journal - European Molecular Biology Organization v. 12 (2): p.563-571; 1993 Feb.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Secale cereale; Transcription; Chloroplasts; Rnapolymerase; Enzyme activity; Ribosomes; Gene expression; Messenger  RNA;Structural genes; Mutants
Abstract:  Transcription of plastid genes and transcript accumulation wereinvestigated in white leaves of the albostrians mutant of barley (Hordeumvulgare) and in heat-bleached leaves of rye (Secale cereale) as well as innormal green leaves of both species. Cells of white leaves of the mutant andcells of heat-bleached leaves bear undifferentiated plastids lacking ribosomesand, consequently, plastid translation products, among them the subunits of aputative chloroplast RNA polymerase encoded by the plastid genes rpoA, B, C1and C2. The following results were obtained. (i) Plastid genes are transcribeddespite the lack of chloroplast gene-encoded RNA polymerase subunits. Theplastid origin of these transcripts was proven. This finding provides evidencefor the existence of a plastid RNA polymerase encoded entirely by nucleargenes. (ii) Transcripts of the rpo genes and of rps15, but not of genesinvolved in photosynthesis and related processes (psbA, rbcL, atpI-H), wereabundantly accumulated in ribosome-deficient plastids. In contrast,chloroplasts accumulated transcripts of photosynthetic, but not of the rpogenes. (iii) Differences in transcript accumulation between chloroplasts andribosome-deficient plastids are due to different relative transcription ratesand different transcript stability. (iv) The observed differences intranscription are not caused by an altered pattern of methylation of plastidDNA. Thus, the prokaryotic plastid genome of higher plants is transcribed bytwo RNA polymerases. The observed differences in transcription betweenchloroplasts and undifferentiated plastids might reflect different functionsof the two enzymes.
46                                                    NAL Call. No.: QH301.N32Circadian control of gene expression and morphogenesis by heat shock inbarley.Beator, J.; Kloppstech, K.New York, N.Y. : Plenum Press; 1992.NATO ASI series : Series A : Life sciences v. 226: p. 101-106. ill; 1992.  Inthe series analytic: Regulation of chloroplast biogenesis / edited by J.H.Argyroudi-Akoyunoglou. Proceedings of a NATO Advanced Research Workshop, July28-August 3, 1991, Crete, Greece.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Circadian rhythm; Gene expression; Greening;Heat shock; Morphogenesis; Phytochrome; Messenger  RNA
47                                                    NAL Call. No.: QK710.P62Circadian rhythmicity in the expression of a novel light-regulated rice gene.Reimmann, C.; Dudler, R.Dordrecht : Kluwer Academic Publishers; 1993 Apr.Plant molecular biology v. 22 (1): p. 165-170; 1993 Apr.  Includes references.
Language:  English
Descriptors: Oryza sativa; Complementary  DNA; Structural genes; Plantproteins; Gene expression; Messenger  RNA; Genetic regulation; Circadianrhythm; Light
Abstract:  We have identified and analyzed cDNAs corresponding to asingle-copy gene from rice, designated lir1, whose expression exhibitsdramatic diurnal fluctuations. The cDNAs encode a putative protein of 128amino acids with no homology to known proteins. Lir1 mRNA accumulates in thelight, reaching maximum and minimum steady-state levels at the end of thelight and dark period, respectively. The oscillations of lir1 mRNA abundancepersist after the plants have been transferred to continuous light ordarkness. Plants germinated in the dark have very low levels of lir1 mRNA,whereas plants germinated in continuous light express lir1 at an intermediatebut constant level. These results indicate that lir1 expression is controlledby light and a circadian clock.
48                                                    NAL Call. No.: QK710.P62The cis-regulatory element CCACGTGG is involved in ABA and water-stressresponses of the maize gene rab28.Pla, M.; Vilardell, J.; Guiltinan, M.J.; Marcotte, W.R.; Niogret, M.F.;Quatrano, R.S.; Pages, M.Dordrecht : Kluwer Academic Publishers; 1993 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (2): p. 259-266; 1993 Jan.Includes references.
Language:  English
Descriptors: Zea mays; Genes; Promoters; Controlling elements; Binding site;Dna binding proteins; Gene expression; Genetic regulation; Abscisic acid;Water stress; Plant embryos; Leaves
Abstract:  The maize gene rab28 has been identified as ABA-inducible inembryos and vegetative tissues. It is also induced by water stress in youngleaves. The proximal promoter region contains the conserved cis-acting elementCCACGTGG (ABRE) reported for ABA induction in other plant genes. Transientexpression assays in rice protoplasts indicate that a 134 bp fragment (-194 to-60 containing the ABRE) fused to a truncated cauliflower mosaic viruspromoter (35S) is sufficient to confer ABA-responsiveness upon the GUSreporter gene. Gel retardation experiments indicate that nuclear proteins fromtissues in which the rab28 gene is expressed can interact specifically withthis 134 bp DNA fragment. Nuclear protein extracts from embryo andwater-stressed leaves generate specific complexes of different electrophoreticmobility which are stable in the presence of detergent and high salt. However,by DMS footprinting the same guanine-specific contacts with the ABRE in boththe embryo and leaf binding activities were detected. These results indicatethat the rab28 promoter sequence CCACGTGG is a functional ABA-responsiveelement, and suggest that distinct regulatory factors with apparent similaraffinity for the ABRE sequence may be involved in the hormone action duringembryo development and in vegetative tissues subjected to osmotic stress.
49                                                    NAL Call. No.: QH301.N32Cis-regulatory elements responsible for the tissue-specific expression of thewheat cab-1 gene.Szell, M.; Szekeres, M.; Adam, E.; Fejes, E.; Nagy, F.New York, N.Y. : Plenum Press; 1992.NATO ASI series : Series A : Life sciences v. 226: p. 57-61; 1992.  In theseries analytic: Regulation of chloroplast biogenesis / edited by J.H.Argyroudi-Akoyunoglou. Proceedings of a NATO Advanced Research Workshop, July28-August 3, 1991, Crete, Greece.  Includes references.
Language:  English
Descriptors: Triticum; Chlorophyll a/b binding protein; Gene expression;Light; Photosystem ii; Plant proteins
50                                                     NAL Call. No.: 450 P692Cloning, characterization, and expression of a cDNA encoding a 50-kilodaltonprotein specifically induced by cold acclimation in wheat.Houde, M.; Danyluk, J.; Laliberte, J.F.; Rassart, E.; Dhindsa, R.S.; Sarhan,F.Rockville, Md. : American Society of Plant Physiologists; 1992 Aug.Plant physiology v. 99 (4): p. 1381-1387; 1992 Aug.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Cold tolerance; Acclimatization; Proteinsynthesis; Induction; Clones; Genetic code; Dna; Gene expression; Genotypes;Messenger  RNA; Genetic variation; Nucleotide sequences; Amino acid sequences
Abstract:  We have isolated, sequenced, and expressed a cold-specific cDNAclone, Wcs120, that specifically hybridizes to a major mRNA species ofapproximately 1650 nucleotides from cold-acclimated wheat (Triticum aestivumL.). The accumulation of this mRNA was induced in less than 24 hours of coldtreatment, and remained at a high steady-state level during the entire periodof cold acclimation in the two freezing-tolerant genotypes of wheat tested.The expression of Wcs120 was transient in a less-tolerant genotype even thoughthe genomic organization of the Wcs120 and the relative copy number were thesame in the three genotypes. The mRNA level decreased rapidly duringdeacclimation and was not induced by heat shock, drought, or abscisic acid.The Wcs120 cDNA contains a long open reading frame encoding a protein of 390amino acids. The encoded protein is boiling stable, highly hydrophilic, andhas a compositional bias for glycine (26.7%), threonine (16.7%), and histidine(10.8%), although cysteine, phenylalanine, and tryptophan were absent. TheWCS120 protein contains two repeated domains. Domain A has the consensus aminoacid sequence GEKKGVMENIKEKLPGGHGDHQQ, which is repeated 6 times, whereasdomain B has the sequence TGGTYGQQGHTGTT, which is repeated 11 times. The twodomains were also found in barley dehydrins and rice abscisic acid-inducedprotein families. The expression of this cDNA in Escherichia coli, using theT7 RNA polymerase promoter, produced a protein of 50 kilodaltons with anisoelectric point of 7.3, and this product comigrated with a major proteinsynthesized in vivo and in vitro during cold acclimation.
51                                                    NAL Call. No.: QK710.P62Cloning of cDNA, expression, and chromosomal location of genes encoding thethree types of subunits of the barley tetrameric inhibitor of insectalpha-amylase.Medina, J.; Hueros, G.; Carbonero, P.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (3): p. 532-542; 1993 Nov.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Complementary  DNA; Structural genes; Multigenefamilies; Enzyme inhibitors; Alpha-amylase; Insects; Nucleotide sequences;Amino acid sequences; Defense mechanisms; Gene mapping; Gene location;Chromosomes; Gene expression; Messenger  RNA; Endosperm
Abstract:  Three cDNA clones from barley developing endosperm, correspondingto proteins BTAI-CMa, BTAI-CMb and BTAI-CMd, which are the three types ofsubunits of the tetrameric inhibitor of insect alpha-amylases, have beenidentified and sequenced. The deduced amino acid sequence of BTAI-CMbcorresponds to the CM16/CM17 type of subunit in wheat (92/90% identicalresidues) and has one putative N-glycosylation site (NLT) and a possiblekinase-C phosphorylation site (SCR). The BTAI-CMa sequence differs at fouramino acid residues from a previously reported one from cv. Bomi and thesequence deduced for BTAI-CMd completes (11 N-terminal residues) and confirmspreviously available data. The gene for BTAI-CMa (Iat1) is located in the betaarm of barley chromosome 7H (syn. 1), while genes for both BTAI-CMb (Iat2) andBTAI-CMd (Iat3) are in the long arm of chromosome 4H. The three genes areexpressed in endosperm and their mRNAS are not detected in the other tissuestested, except Iat1, which seems to be expressed at a low level in coleoptileand roots, where it is switched off by 50 micromolars methyl jasmonate.
52                                                   NAL Call. No.: QH442.A1G4Comparison of barley malt alpha-amylase isozymes 1 and 2: construction of cDNAhybrids by in vivo recombination and their expression in yeast.Juge, N.; Sogaard, M.; Chaix, J.C.; Martin-Eauclaire, M.F.; Svensson, B.;Marchis-Mouren, G.; Guo, X.J.Amsterdam : Elsevier Science Publishers; 1993.Gene v. 130 (2): p. 159-166; 1993.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Saccharomyces cerevisiae; Complementary  DNA;Recombinant  DNA; Alpha-amylase; Isoenzymes; Homologous recombination;Hybrids; Genetic transformation; Gene expression; Secretion; Enzyme activity
Abstract:  Germinating barley produces two alpha-amylase isozymes, AMY1 andAMY2, having 80% amino acid (aa) sequence identity and differing with respectto a number of functional properties. Recombinant AMY1 (re-AMY1) and AMY2(re-AMY2) are produced in yeast, but whereas all re-AMY1 is secreted, re-AMY2accumulates within the cell and only traces are secreted. Expression ofAMY1::AMY2 hybrid cDNAs may provide a means of understanding the difference insecretion efficiency between the two isozymes. Here, the efficient homologousrecombination system of the yeast, Saccharomyces cerevisiae, was used togenerate hybrids of barley AMY with the N-terminal portion derived from AMY1,including the signal peptide (SP), and the C-terminal portion from AMY2.Hybrid cDNAs were thus generated that encode either the SP alone, or the SPfollowed by the N-terminal 21, 26, 53, 67 or 90 aa from AMY1 and thecomplementary C-terminal sequences from AMY2. Larger amounts of re-AMY aresecreted by hybrids containing, in addition to the SP, 53 or more aa of AMY1.In contrast, only traces of re-AMY are secreted for hybrids having 26 or feweraa of AMY1. In this case, re-AMY hybrid accumulates intracellularly.Transformants secreting hybrid enzymes also accumulated some re-AMY within thecell. The AMY1 SP, therefore, does not ensure re-AMY2 secretion and a certainportion of the N-terminal sequence of AMY1 is required for secretion of are-AMY1::AMY2 hybrid.
53                                                     NAL Call. No.: 450 P692Complementary DNA cloning and sequence analysis of a pathogen-induced putativeperoxidase from rice.Reimmann, C.; Ringli, C.; Dudler, R.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.Plant physiology v. 100 (3): p. 1611-1612; 1992 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Complementary  DNA; Peroxidase; Nucleotidesequences; Amino acid sequences; Gene expression; Messenger  RNA; Infections;Pseudomonas syringae pv. syringae
54                                                     NAL Call. No.: 450 P692Constitutive and inducible aerobic and anaerobic stress proteins in theEchinochloa complex and rice.Mujer, C.V.; Rumpho, M.E.; Lin, J.J.; Kennedy, R.A.Rockville, Md. : American Society of Plant Physiologists; 1993 Jan.Plant physiology v. 101 (1): p. 217-226; 1993 Jan.  Includes references.
Language:  English
Descriptors: Echinochloa; Echinochloa muricata; Echinochloa oryzoides;Echinochloa crus-galli; Echinochloa crus-pavonis; Oryza sativa; Stressresponse; Protein synthesis; Induction; Anaerobic conditions; Aerobictreatment; Genetic regulation; Gene expression
Abstract:  Anaerobic stress resulted in a change in the protein accumulationpatterns in shoots of several Echinochloa (barnyard grass) species and Oryzasativa (L.) (rice) as resolved by two-dimensional gel electrophoresis. Of thesix Echinochloa species investigated, E. phyllopogon (Stev.) Koss, E. muricata(Beauv.) Fern, E. oryzoides (Ard.) Fritsch Clayton, and E. crus-galli (L.)Beauv. are tolerant of anaerobiosis and germinate in the absence of oxygen, asdoes rice. In contrast, E. crus-pavonis (H.B.K.) Schult and E. colonum (L.)Link are intolerant and do not germinate without oxygen. Computer analysis ofthe protein patterns from the four tolerant species and rice indicated thatthe anaerobic response is of five classes: class 1 proteins, enhanced underanaerobiosis (9 to 13 polypeptides ranging from 16-68 kD); class 2 proteins,unique to anaerobiosis (1 to 5 polypeptides ranging from 17-69 kD); class 3proteins, remained constant under aerobiosis and anaerobiosis; class 4proteins, prominent only in air and repressed under anoxia (3 to 7polypeptides ranging from 19-45 kD); and class 5 proteins, unique toaerobiosis (1 to 4 polypeptides ranging from 18-63 kD). In the intolerantspecies, E. colonum and E. crus-pavonis, no polypeptides were enhanced orrepressed under anoxia (class 1 and class 4, respectively), whereas in thetolerant Echinochloa species and rice, a total of at least 9 to 13 anaerobicstress proteins and 4 to 7 "aerobic" proteins were noted. Immunoblottingidentified two of the major anaerobic stress proteins asfructose-1,6-bisphosphate aldolase and pyruvate decarboxylase. Based on thedifferential response of the intolerant species to anaerobiosis, we suggestthat another set of genes, whose products may not necessarily be among themajor anaerobic stress polypeptides, might confer tolerance in Echinochloaunder prolonged anaerobic stress.
55                                              NAL Call. No.: S494.5.B563B554The control of protein synthesis in developing barley seeds.Kreis, M.; Shewry, P.R.Wallingford, Oxford, UK : CAB International; 1992.Biotechnology in agriculture (5): p. 319-333; 1992.  In the series analytic:Barley : genetics, biochemistry, molecular biology and biotechnology / editedby P.R. Shewry.  Includes references.
Language:  English
Descriptors: Hordeum; Plant embryos; Endosperm; Seed development; Geneticregulation; Protein synthesis; Cereal proteins; Genes; Gene expression;Nucleotide sequences; Amino acid sequences; Amino acids; Composition; Proteinvalue; Grain
56                                                    NAL Call. No.: QK710.P62Coordinate gene expression of five subclass histones and the putativetranscription factors, HBP-1a and HBP-1b, of histone genes in wheat.Minami, M.; Huh, G.H.; Yang, P.; Iwabuchi, M.Dordrecht : Kluwer Academic Publishers; 1993 Oct.Plant molecular biology v. 23 (2): p. 429-434; 1993 Oct.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Gene expression; Messenger  RNA; Histones;Structural genes; Dna binding proteins; Meristems; Transcription; Seedgermination; Seedling growth
Abstract:  The expression of genes encoding five histones (H1,H2A,H2B,H3 andH4) and the putative transcription factors HBP-1a (17) and HBP-1b (c38) wasexamined during early germination and in various tissues of young wheatseedlings. The steady-state levels of core histone (H2A, H2B, H3 and H4) mRNAswere coordinately cell cycle-dependent and paralleled the rate of DNAsynthesis during early germination, whereas the expression pattern of thelinker histone (H1) genes differed. The five subclass histone genes wereactively expressed in the meristematic tissues of young seedlings. Moreover,H1 genes were expressed in leaves that consist mostly of non-proliferatingcells, in which core histone genes showed little expression. Quantitativealterations to the mRNAs of the putative transcription factors HBP-1a (17) andHBP-1b (c38) of wheat histone genes were similar to those of the core histonemRNAs, suggesting that both factors function in the cell cycle-dependentexpression of wheat core histone genes.
57                                                     NAL Call. No.: 450 P692Coordinate gene response to salt stress in Lophopyrum elongatum.Gulick, P.J.; Dvorak, J.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.Plant physiology v. 100 (3): p. 1384-1388; 1992 Nov.  Includes references.
Language:  English
Descriptors: Gramineae; Elymus elongatus; Gene expression; Genes; Geneticregulation; Salinity; Sodium chloride; Stress; Roots; Messenger  RNA;Complementary  DNA; Nucleotide sequences
Abstract:  Lophopyrum elongatum is a highly salt-tolerant relative of wheat. Aprevious study showed that the abundance of a number of mRNA species isenhanced or reduced in the roots of the L. elongatum X Triticum aestivumamphiploid by salt stress. Eleven genes with enhanced expression in the rootsof salt-stressed L. elongatum plants have been cloned as cDNAS. The cloneswere used as probes to characterize temporal expression of these genes inroots after initiation of salt (250 mm NaCl) stress. All 11 genes are inducedwithin 2 h after exposure to 250 mm NaCl and reached peak expression after 6h. The decline of gene expression distinguished two groups, one in which mRNAconcentrations returned to basal levels by 24 h and the other in which thisoccurred between 3 and 7 d. One of the 11 clones was found to be homologous toa multigene family of abscisic acid-induced genes, rab and dhn, identified inother species. We suggest that the coordinate expression of this large numberof genes reflects the existence of a highly specific early response to saltstress. We refer to this response as the 'early salt stress response.'
58                                                     NAL Call. No.: QP501.E8Corn kernel cystein proteinase inhibitor as a novel cystatin superfamilymember of plant origin. Molecular cloning and expression studies.Abe, M.; Abe, K.; Kuroda, M.; Arai, S.New York, NY : Springer-Verlag New York Inc; 1992 Nov.European journal of biochemistry v. 209 (3): p. 933-937; 1992 Nov.  Includesreferences.
Language:  English
Descriptors: Zea mays; Kernels; Cysteine proteinases; Proteinase inhibitors;Plant proteins; Genes; Clones; Gene expression; Nucleotide sequences; Aminoacid sequences; Comparisons; Enzyme activity; Inhibition
Abstract:  A full-length cDNA clone for a cysteine proteinase inhibitor(cystatin) was isolated from a lambda gt10 cDNA library of immature cornkernels by screening with a mixture of cDNA inserts for oryzacystatins I andII. The cDNA clone spans 960 base pairs, encoding a 135-amino-acid proteincontaining a signal peptide fragment. The protein, named corn cystatin 1, isconsidered to be a member of the cystatin superfamily, since it contains thecommonly conserved Gln-Val-Val-Ala-Gly region that exists in most knowncystatins as a probable binding site and is significantly similar to othercystatins in its overall amino acid sequence. Corn cystatin I expressed inEscherichia coli showed a strong papain-inhibitory activity. Northern blotanalysis showed that the amount of mRNA for corn cystatin I reaches a maximum2 weeks after flowering and then decreases gradually.
59                                                    NAL Call. No.: 442.8 Z34Correlation between the size of the intergenic regulatory region, the statusof cytosine methylation of rRNA genes and nucleolar expression in wheat.Sardana, R.; O'Dell, M.; Flavell, R.Berlin, W. Ger. : Springer International; 1993 Jan.M G G : Molecular and general genetics v. 236 (2/3): p. 155-162; 1993 Jan.Includes references.
Language:  English
Descriptors: Triticum aestivum; Ribosomal  DNA; Ribosomal  RNA; Loci;Multigene families; Cytosine; Dna methylation; Nucleolus; Gene expression;Secondary constrictions; Repetitive  DNA; Binding site; Dna binding proteins;Genetic regulation
Abstract:  A large number of wheat rRNA genes are methylated at all the CCGGsites that are present in the intergenic regions. A smaller number of rRNAgenes are not methylated at one or more CCGG sites. A subset of genes wasfound unmethylated at a specific CCGG site just downstream of the array of 135bp A repeats in the intergenic region. In all the genotypes studied, the rDNAloci with larger intergenic regions between their genes also possess a greaternumber of rRNA genes that are unmethylated at one or more CCGG sites in theintergenic regions than do the loci with shorter intergenic regions. In fourgenotypes (for which data were available), rDNA loci with longer intergenicregions had larger secondary constrictions on metaphase chromosomes, a measureof relative locus activity, than the loci with shorter intergenic regions. Theresults have been integrated into a model for the control of rDNA expressionbased on correlations between cytosine methylation patterns and the number ofupstream 135 bp repeats in intergenic regions. According to this model the 135bp repeats play a part in the control of gene activity by binding a protein(s)that is in limiting supply, thereby predisposing the neighbouring gene tobecome active preferentially.
60                                                    NAL Call. No.: QK710.P62Co-transcription pattern of an introgressed operon in the maize chloroplastgenome comprising four ATP synthase subunit genes and the ribosomal rps2.Stahl, D.J.; Rodermel, S.R.; Bogorad, L.; Subramanian, A.R.Dordrecht : Kluwer Academic Publishers; 1993 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (6): p. 1069-1076; 1993 Mar.Includes references.
Language:  English
Descriptors: Zea mays; Transcription; Structural genes;Adenosinetriphosphatase; Ribosomes; Proteins; Introgression; Chloroplasts;Genomes; Chloroplast genetics; Gene expression; Messenger  RNA; Thylakoids
Abstract:  Several examples of the introduction of a gene from one genecomplex into another (introgression) are found when chloroplast RP geneclusters are compared to those in Escherichia coli or cyanobacteria. Here wedescribe the transcript pattern of one such cluster from maize (Zea mays) thatincludes the genes for 4 subunits of the thylakoid ATP synthase (atpI, H, F,-  and the rps2 gene. Twelve transcript species covering the size range from7000 to 800 nt were identified in RNA isolated from dark-grown and greeningmaize seedlings, and several of them were characterized by reversetranscription analysis. A major species of 6200 nt, with its 5' end at 181 ntupstream of the initiating ATG of rps2, contained the transcripts of all the 5genes. Two further sets of transcripts having their 5' ends ca. 120 and 50 ntupstream of the initiation codons of the atpI and atpH genes were alsoidentified. Thus, this plastid gene cluster in maize is functionally organizedas an operon with additional regulatory features to allow for increasedaccumulation of mRNAs for the thylakoid components.  61                                                  NAL Call. No.: SB732.6.M65Cultivar-specific elicitaiton of barley defense reactions by the phytotoxicpeptide NIP1 from Rhynchosporium secalis.Hahn, M.; Jungling, S.; Knogge, W.St. Paul, MN : APS Press, [c1987-; 1993 Nov.Molecular plant-microbe interactions : MPMI v. 6 (6): p. 745-754; 1993 Nov.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Rhynchosporium secalis; Complementary  DNA;Pathogenesis-related proteins; Nucleotide sequences; Amino acid sequences;Gene expression; Messenger  RNA; Gene location; Alleles; Segregation;Dominance; Defense mechanisms; Disease resistance; Multigene families; Fungaldiseases; Pathogenicity; Physiological races; Peptides; Mycotoxins; Cultivars;Genes
62                                                     NAL Call. No.: 450 P692Cytokinin is required to induce the nitrogen-dependent accumulation of mRNAsfor phosphoenolpyruvate carboxylase and carbonic anhydrase in detached maizeleaves.Sugiharto, B.; Burnell, J.N.; Sugiyama, T.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Sep.Plant physiology v. 100 (1): p. 153-156; 1992 Sep.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Messenger  RNA; Carbonate dehydratase;Phosphoenolpyruvate carboxylase; Genetic regulation; Zeatin; Benzyladenine;Nitrate; Nutrient availability; Leaves; Iaa; Abscisic acid
Abstract:  Previous studies with intact maize (Zea mays L.) plants indicatedthat phosphoenolpyruvate carboxylase (PEPC) levels are controlled by nitrogen(N) availability and that this regulation is presumably at the transcriptionallevel (B. Sugiharto, K. Miyata, H. Nakamoto, H. Sasakawa, T. Sugiyama [1990]Plant Physiol 92: 963-969; B. Sugiharto, T. Sugiyama [19921 Plant Physiol 98:1403-1408). In the present study, detached maize leaves were used toinvestigate further the mechanism of N-dependent regulation of gene expressionin C4 plants. PEPC and carbonic anhydrase (CA) mRNA levels decreased in leavesdetached from maize plants. Addition of high nitrate did not prevent thisdecrease. However, the addition of zeatin to solutions bathing the cut ends ofthe detached leaves inhibited the decrease of PEPC and CA mRNA levels.Simultaneous addition of high nitrate and zeatin to leaves detached fromN-deficient maize plants caused a large and rapid increase in PEPC and CA mRNAlevels. Zeatin could be replaced by benzyladenine, but not by indoleaceticacid or abscisic acid. Both CA isozymes were effected and responded in anidentical manner. We conclude that detached maize leaves provide an excellentexperimental system to study the mechanism(s) of N-mediated regulation of PEPCand CA gene expression. However, zeatin is an essential component of thissystem.
63                                                     NAL Call. No.: 450 P692Cytosolic alkalinization mediated by abscisic acid is necessary, but notsufficient, for abscisic acid-induced gene expression in barley aleuroneprotoplasts.Veen, R. van der; Heimovaara-Dijkstra, S.; Wang, M.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Oct.Plant physiology v. 100 (2): p. 699-705; 1992 Oct.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Gene expression; Messenger  RNA; Genes; Geneticregulation; Abscisic acid; Ph; Alkalinity; Cytosol; Protoplasts; Aleuronecells
Abstract:  We investigated whether intracellular pH (phi) is a causal mediatorin abscisic acid (ABA)-induced gene expression. We measured the change in phiby a "null-point" method during stimulation of barley (Hordeum vulgare cvHimalaya) aleurone protoplasts with ABA and found that ABA induces an increasein pHi from 7.11 to 7.30 within 45 min after stimulation. This increase isinhibited by plasma membrane H+-ATPase inhibitors, which induce a decrease inpHi, both in the presence and absence of ABA. This ABA-induced phi increaseprecedes the expression of RAB-16 mRNA, as measured by northern analysis.ABA-induced pHi changes can be bypassed or clamped by addition of either theweak acids 5,5-dimethyl-2,4-oxazolidinedione and propionic acid, whichdecrease the phi, or the weak bases methylamine and ammonia, which increasethe pHi. Artificial phi increases or decreases induced by weak bases or weakacids, respectively, do not induce RAB-16 mRNA expression. Clamping of the pHiat a high value with methylamine or ammonia treatment affected the ABA-inducedincrease of RAB-16 mRNA only slightly. However, inhibition of the ABA-inducedphi increase with weak acid or proton pump inhibitor treatments stronglyinhibited the ABA-induced RAB-16 mRNA expression. We conclude that, althoughthe ABA-induced the pHi increase is correlated with and even precedes theinduction of RAB-16 mRNA expression and is an essential component of thetransduction pathway leading from the hormone to gene expression, it is notsufficient to cause such expression.
64                                                   NAL Call. No.: QK725.P532Definition and functional implications of gibberellin and abscisic acidcis-acting hormone response complexes.Rogers, J.C.; Rogers, S.W.Rockville, Md. : American Society of Plant Physiologists; 1992 Nov.The Plant cell v. 4 (11): p. 1443-1451; 1992 Nov.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Promoters; Alpha-amylase; Controlling elements;Gibberellic acid; Abscisic acid; Transcription; Gene expression; Geneticregulation; Nucleotide sequences; Seed development
Abstract:  The mechanisms by which cis-acting hormone response elements affecttranscription is unclear. In this study, we demonstrated that a second"coupling element," identified as O2S, must be present to allow a single copyof either the gibberellin response element (GARE) or the abscisic acidresponse element (ABRE) to mediate their hormonal effects in the barley Amy32balpha-amylase gene promoter. The interactive effects of the O2S and the GAREare constrained positionally and spatially; thus, together they form agibberellin response complex (GARC). The absolute requirement of the O2S forfunction of the ABRE demonstrates that these together form an abscisic acidresponse complex (ABRC). A second copy of the GARE can substitute for the O2Sin the GARC, but only in one orientation. By expressing the GARC-containingand ABRC-containing promoters in developing aleurone tissue, we showed thathormonal effects prevent alpha-amylase gene expression during the second halfof grain development, but other mechanisms suppress expression earlier. Ourresults suggest that the specific sequence serving as a coupling element in agiven gene promoter will greatly affect where and when the GARE or ABRE willbe able to regulate transcription.
65                                                    NAL Call. No.: QK710.P68Developmental and pathogen-induced expression of three barley genes encodinglipid transfer proteins.Molina, A.; Garcia-Olmedo, F.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Dec.The Plant journal : for cell and molecular biology v. 4 (6): p. 983-991; 1993Dec.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Lipoproteins; Gene expression; Genetic code;Amino acid sequences; Cloning; Dna; Disease resistance; Nucleotide sequences;Plant diseases
66                                                     NAL Call. No.: 450 P692Developmental regulation of (1 leads to 3, 1 leads to 4)-beta-glucanase geneexpression in barley: tissue-specific expression of individual isoenzymes.Slakeski, N.; Fincher, G.B.Rockville, Md. : American Society of Plant Physiologists; 1992 Jul.Plant physiology v. 99 (3): p. 1226-1231; 1992 Jul.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Aleurone layer; Scutellum; Leaves; Roots;Beta-glucanase; Enzyme activity; Regulation; Plant development; Geneexpression; Isoenzymes; Seed germination; Transcription
Abstract:  Two genes encode (1 leads to 3,1 leads to 4)-beta-D-glucan4-glucanohydrolase (EC 3.2.1.73) isoenzymes EI and EII in barley (Hordeumvulgare L.). Specific DNA probes have been used in Northern analyses toexamine the developmental regulation of individual (1 leads to 3,1 leads to4)-beta-glucanase genes in the aleurone and scutellum of germinated grain andin young leaves and young roots. In aleurone and scutella excised fromgerminated grain, mRNAs encoding both isoenzymes are present but developmentalpatterns differ between the two tissues. Thus, levels of both isoenzyme EI andEII mRNA increase significantly in the aleurone between 1 and 3 days after theinitiation of germination. In the scutellum, isoenzyme EI mRNA predominatesand decreases as germination proceeds. Isoenzyme EI mRNA appears in youngleaves approximately 8 days after the initiation of germination and levelsrise until about 20 days. Enzyme activity in leaf extracts parallels thedevelopment of isoenzyme EI mRNA. No isoenzyme EII mRNA is detected in theleaves in this period. Analysis of RNA from different leaf segments indicatesthat the isoenzyme EI mRNA is distributed relatively evenly along the lengthof the leaf. In young roots, mRNA encoding (1 leads to 3,1 leads to4)-beta-glucanase isoenzyme EI is detected at high levels 3 to 6 days afterthe initiation of germination; again, little or no isoenzyme EII mRNA isfound. Overall, transcription of the (1 leads to 3,1 leads to4)-beta-glucanase isoenzyme EII gene appears to be restricted to thegerminating grain, whereas isoenzyme EI is expressed in a wider range oftissues during seedling development.
67                                               NAL Call. No.: S494.5.B563C87Developmental regulation of an ABA- and stress-induced protein in barley.Ho, T.H.D.; Hong, B.; Barg, R.Dordrecht : Kluwer Academic Publishers; 1992.Current plant science and biotechnology in agriculture v. 13: p. 493-499;1992.  In the series analytic: Progress in plant growth regulation / edited byC.M. Karssen, L.C. Van Loon and D. Vreugdenhil.  Proceedings of the 14thInternational Conference on Plant Growth Substances held July 21-26, 1991,Amsterdam, Netherlands.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Gene expression; Messenger  RNA; Plant proteins;Plant embryos; Aleurone layer; Seed development; Genetic regulation; Abscisicacid; Water stress; Seed germination; Seedling growth; Drought; Cold stress;Heat shock; Salinity
68                                                     NAL Call. No.: 450 P693Differences in gene expression between natural and artificially induced leafsenescence.Becker, W.; Apel, K.Berlin ; New York : Springer-Verlag, 1925-; 1993.Planta v. 189 (1): p. 74-79; 1993.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Gene expression; Messenger  RNA; ComplementaryDNA; Leaves; Senescence; Dark; Abscisic acid; Kinetin; Stress; Osmoticpressure; Abiotic injuries
Abstract:  Gene expression during artificially induced senescence of barley(Hordeum vulgare L.) leaves was examined by in-vitro translation and mRNAhybridization with several copy-DNA (cDNA) clones for newly inducedtranscripts. When detached barley leaves were incubated in darkness,senescence symptoms as indicated by chlorophyll loss were rapidly induced. Byin-vitro translation, concomitant changes in translatable mRNA levels wereshown to occur with some translation products decreasing and others increasingin abundance. For closer analysis, cDNA clones for newly induced transcriptswere isolated by differential screening. Six cDNA clones, derived from threedifferent transcripts were identified and classified according to theexpression of the respective mRNAs. Two of the three transcripts showed verysimilar expression patterns: in detached leaves they were induced by abscisicacid and inhibited by kinetin. They were also induced by wounding and osmoticstress, but could not be detected in naturally senescing leaves. The thirdmRNA, represented by only one of the six cDNA clones, behaved differently.There was no significant effect of hormone application, wounding or droughtconditions, but the transcript accumulated during natural senescence of barleyflag leaves. We conclude that only a minor part of the mRNA changes observedduring dark incubation of detached leaves is connected with leaf senescence,whereas stress-related transcripts appear to predominate quantitatively.
69                                                     NAL Call. No.: 442.8 Z8Differences in the heat-shock response between thermotolerant andthermosusceptible cultivars of hexaploid wheat.Weng, J.; Nguyen, H.T.Berlin, W. Ger. : Springer International; 1992 Sep.Theoretical and applied genetics v. 84 (7/8): p. 941-946; 1992 Sep.  Includesreferences.
Language:  English
Descriptors: Triticum aestivum; Multigene families; Heat shock proteins; Geneexpression; Messenger  RNA; Cultivars; Heat tolerance; Heat; Susceptibility;Heat shock; Seedlings; Restriction fragment length polymorphism; Geneticpolymorphism; Lines; Heat stress
Abstract:  Heat-shock protein (HSP) gene expression in two wheat lines cv'Mustang' (heat-tolerant) and cv 'Sturdy' (heat-susceptible) were analyzed todetermine if wheat genotypes differing in heat tolerance also differ inin-vitro HSP synthesis (translatable HSP mRNAs) and steady-state levels of HSPmRNA. Several sets of mRNA were isolated from seedling leaf tissues which hadbeen heat-stressed at 37 degrees C for various time intervals. These mRNAswere hybridized with HSP cDNA or genomic DNA probes (HSP17, 26, 70, 98, andubiquitin). Protein profiles were compared using in-vitro translation and 2-Dgels. The Northern slot-blot data from the heat-stress treatment provideevidence that the heat-tolerant cv 'Mustang' synthesized low molecular weight(LMW) HSP mRNA earlier during exposure to heat shock and at a higher levelthan did the heat-susceptible cv 'Sturdy'. This was especially true for thechloroplast-localized HSP. The protein profiles shown by 2-D gel analysisrevealed that there were not only quantitative differences of individual HSPsbetween the two wheat lines, but also some unique HSPs which were only foundin the 'Mustang' HSP profiles. The high level of RFLP between the two wheatlines was revealed by Southern blot hybridization utilizing a HSP17 probe.These data provide a molecular basis for further genetic analysis of the roleof HSP genes in thermal tolerance in wheat.
70                                                     NAL Call. No.: 450 P699Differential effects of nitrate and light on the expression of glutaminesynthetases and ferredoxin-dependent glutamate synthase in maize.Sakakibara, H.; Kawabata, S.; Hase, T.; Sugiyama, T.Kyoto : Japanese Society of Plant Physiologists; 1992 Dec.Plant and cell physiology v. 33 (8): p. 1193-1198; 1992 Dec.  Includesreferences.
Language:  English
Descriptors: Zea mays; Nitrogen metabolism; Leaves; Glutamate-ammonia ligase;Enzyme activity; Glutamate synthase; Genetic regulation; Gene expression;Regulation; Light; Nitrate; Ferredoxin; Photosynthesis; Protein composition
Abstract:  The effects of nitrate and light on the expression of genes forglutamine synthetase (GS) isoproteins and ferredoxin-dependent glutamatesynthase (Fd-GOGAT) were studied in different organs of maize seedlings byanalyzing the levels of the respective polypeptides and mRNAs. In roots, thelevels of plastidic GS and of a novel, root-specific GS molecule localized inthe extraplastidic compartment were increased markedly by nitrate, whereasFd-GOGAT and cytosolic GS remained at their initial levels. Ammonia was noteffective in inducing the plastidic GS and Fd-GOGAT but it did induce thenovel GS isoprotein. In leaves, cytosolic and plastidic GSs and Fd-GOGAT werepresent in both mesophyll cells (MC) and bundle sheath cells (BSC). Uponaddition of nitrate, the level of plastidic GS increased preferentially in MC,and upon exposure of etiolated seedlings to light, the levels of plastidic GSand Fd-GOGAT increased in BSC in a coordinated manner. The relationshipbetween the expression of genes for GSs and Fd-GOGAT and the physiologicalrole of the GS/GOGAT cycle is discussed in terms of the characteristics ofnitrogen metabolism in roots, MC, and BSC.
71                                                  NAL Call. No.: SB732.6.M65Differential expression and induction of chitinases and beta-1,3-glucanases inresponse to fungal infection during germination of maize seeds.Cordero, M.J.; Raventos, D.; San Segundo, B.St. Paul, MN : APS Press, [c1987-; 1994 Jan.Molecular plant-microbe interactions : MPMI v. 7 (1): p. 23-31; 1994 Jan.Includes references.
Language:  English
Descriptors: Zea mays; Gibberella fujikuroi; Fungal diseases; Chitinase;Beta-glucanase; Pathogenesis-related proteins; Seed germination; Geneexpression; Messenger  RNA; Coleoptiles; Radicles; Plant embryos
72                                                    NAL Call. No.: QK710.P62Differential expression of six glutamine synthase genes in Zea mays.Li, M.G.; Villemur, R.; Hussey, P.J.; Silflow, C.D.; Gantt, J.S.; Snustad,D.P.Dordrecht : Kluwer Academic Publishers; 1993 Oct.Plant molecular biology v. 23 (2): p. 401-407; 1993 Oct.  Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Glutamate-ammonia ligase; Geneexpression; Messenger  RNA; Plant; Nucleotide sequences; Isoenzymes;Chloroplasts; Multigene families
Abstract:  The maize genome has been shown to contain six glutamine synthetase(GS) genes with at least four different expression patterns. Noncoding3'gene-specific probes were constructed from all six GS cDNA clones and usedto examine transcript levels in selected organs by RNA gel blot hybridizationexperiments. The transcript of the single putative chloroplastic GS(2) genewas found to accumulate primarily in green tissues, whereas the transcripts ofthe five putative GS(1) genes were shown to accumulate preferentially inroots. The specific patterns of transcript accumulation were quite distinctfor the five GS(1) genes, with the exception of two closely related genes.
73                                                     NAL Call. No.: 450 P699Differential expression of the catalase and superoxide dismutase genes inmaize ear shoot tissues.Acevedo, A.; Scandalios, J.G.Kyoto : Japanese Society of Plant Physiologists; 1992 Dec.Plant and cell physiology v. 33 (8): p. 1079-1088; 1992 Dec.  Includesreferences.
Language:  English
Descriptors: Zea mays; Maize ears; Shoots; Gene expression; Developmentalstages; Catalase; Superoxide dismutase; Enzyme activity; Messenger  RNA;Transcription; Pollination
Abstract:  The temporal expression of two major antioxidant gene-enzymesystems, catalases and superoxide dismutases, has been characterized in thehusk leaf, silk, pistillate flower, whole kernel, and cob of the maize earshoot. The catalase activity, CAT-2 and CAT-3 protein levels, and thesteady-state mRNA levels of each of the three Cat genes reveal differentialexpression of these transcripts in tissues of the ear shoot. Although Cat1 andCat3 expression is observed in all the aforementioned tissues, Cat2 expressionis detected only at the late stages of whole kernel maturation. Because silkexhibits the same pattern of Cat gene expression as the pericarp, and bothtissues share an identical histological origin, catalase gene expression mightbe associated with cell lineage. The levels of total superoxide dismutaseactivity and corresponding individual Sod transcripts are fairly constantthroughout the temporal profiles of the ear shoot tissues. However, the degreeof accumulation of the multiple Sod mRNAs in the husk leaf is higher than inthe cob. The possibility that the relative position of a tissue within the earshoot influences the degree of accumulation of the various Sod mRNAs isdiscussed.
74                                                    NAL Call. No.: QK710.P62Differential expression of U5snRNA gene variants in maize (Zea mays)protoplasts.Leader, D.; Connelly, S.; Filipowicz, W.; Waugh, R.; Brown, J.W.S.Dordrecht : Kluwer Academic Publishers; 1993 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (1): p. 133-143; 1993 Jan.Includes references.
Language:  English
Descriptors: Zea mays; Small nuclear  RNA; Ribosomal  DNA; Multiple genes;Multigene families; Controlling elements; Gene expression; Protoplasts;Genetic transformation; Nucleotide sequences; Genetic variation
Abstract:  The small nuclear ribonucleoprotein particles U1, U2, U4/U6 and U5participate in the removal of introns from pre-messenger RNAs in the nucleus.Three genes encoding U5snRNAs, the RNA moiety of U5snRNPs, have been isolatedfrom maize. As in other plant UsnRNA gene families the three maize U5snRNAgenes exhibit sequence variation. Two of the gene variants (MzU5.1 and MzU5.2)are clearly expressed after transfection into maize leaf protoplasts while thethird gene variant (MzU5.3) is expressed at very low levels. These differentlevels of expression cannot be directly correlated with sequence changes inthe highly conserved Upstream Sequence Element (USE) required for expressionof Arabidopsis UsnRNA genes nor with differential stability of the U5snRNAtranscripts. Further sequence elements may therefore have a role in regulatingmaize UsnRNA gene expression.
75                                                     NAL Call. No.: 450 P692Differential induction of distinct glutathione-S-transferases of wheat byxenobiotics and by pathogen attack.Mauch, F.; Dudler, R.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug.Plant physiology v. 102 (4): p. 1193-1201; 1993 Aug.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Structural genes; Complementary  DNA;Glutathione transferase; Isoenzymes; Gene transfer; Genetic transformation;Escherichia coli; Gene expression; Messenger  RNA; Genetic regulation;Erysiphe graminis f.sp. tritici; Erysiphe graminis f.sp. hordei; Pucciniarecondita; Salicylic acid; Cadmium; Herbicides; Glutathione; Enzyme activity
Abstract:  We have previously characterized a pathogen-induced gene from wheat(Triticum aestivum L.) that was named GstA1 based on sequence similaritieswith glutathione-S-transferases (GSTs) of maize (R. Dudler, C. Hertig, G.Rebmann, J. Bull, F. Mauch [1991] Mol Plant Microbe Interact 4:14-18). We haveconstructed a full-length GstA1 cDNA by combinatorial polymerase chainreaction and demonstrate by functional expression of the cDNA in Escherichiacoli that the GstA1-encoded protein has GST activity. An antiserum raisedagainst a GstA1 fusion protein specifically recognized a protein with anapparent molecular mass of 29 kD on immunoblots of extracts from bacteriaexpressing the GstA1 cDNA and extracts from wheat inoculated with Erysiphegraminis. The GstA1-encoded protein was named GST29. RNA and immunoblotanalysis showed that GstA1 was only weakly expressed in control plants and wasspecifically induced by pathogen attack and by the GST substrate glutathione,but not by various xenobiotics. In contrast, a structurally and antigenicallyunrelated GST with an apparent molecular mass of 25 kD that was detected withan antiserum raised against GSTs of maize was expressed at a high basal level.This GST25 and an additional immunoreactive protein named GST26 were stronglyinduced by cadmium and by the herbicides atrazine, paraquat, and alachlor, butnot by pathogen attack. Compared with the pathogen-induced GST29, GST25 andGST26 showed a high affinity toward glutathione-agarose and were much moreactive toward the model substrate 1-chloro-2,4-dinitrobenzene. Thus, wheatcontains at least two distinct GST classes that are differentially regulatedby xenobiotics and by pathogen attack and whose members have different enzymicproperties. GST25 and GST26 appear to have a function in xenobioticmetabolism, whereas GST29 is speculated to fulfill a more specific role indefense reactions against pathogens.
76                                                     NAL Call. No.: 450 P693Differential molecular responses to abscisic acid and osmotic stress inviviparous maize embryos.Butler, W.M.; Cumming, A.C.Berlin ; New York : Springer-Verlag, 1925-; 1993.Planta v. 189 (1): p. 47-54; 1993.  Includes references.
Language:  English
Descriptors: Zea mays; Plant embryos; Messenger  RNA; Gene expression; Genes;Plant proteins; Embryogenesis; Genetic regulation; Stress; Osmotic pressure;Abscisic acid; Mutants; Germination; Loci
Abstract:  Substantial quantities of mRNA encoding the abundant "Em"polypeptide accumulate, in planta, in developing embryos of maize (Zea maysL.). By contrast. accumulation of "Em" mRNA is only barely detectable inembryos with the vp-5/vp-5 genotype [an abscisic acid (ABA)-deficientviviparous phenotype]. "Em" mRNA is not detectable within viviparous embryosof the vp-1/vp-1 genotype that are non-responsive to ABA. Culture of immaturewild-type and vp-5/vp-5 embryos in the presence of exogenous ABA or of anosmotically active agent prevents precocious germination and results inexpression of the "Em" genes. When vp-1/vp-1 embryos are cultured undersimilar conditions, only the application of osmotic stress prevents precociousgermination. However. "Em" mRNA does not accumulate either in ABA-treated orstressed, arrested embryos, indicating a requirement for ABA perceptionthrough a VP-1-mediated mechanism for "Em" gene expression. Nevertheless.vp-1/vp-1 embryos do show both ABA and stress responses at the molecularlevel. Treatment with ABA causes the accumulation of mRNA encoding apolypeptide of approx. 30 kDa, whilst osmotic stress induces the accumulationboth of a 30-kDa polypeptide and a set of approx. 20-kDa polypeptides. Thisindicates the existence of discrete, parallel ABA and stress response pathwaysin developing maize embryos.
77                                                      NAL Call. No.: 450 OS7Diurnal rhythms of the chlorophyll a/b binding protein mRNAs in wild emmerwheat and wild barley (Poaceae) in the Fertile Crescent.Nevo, E.; Meyer, H.; Piechulla, B.Wien : Springer; 1993.Plant systematics and evolution v. 185 (3/4): p. 181-188; 1993.  Includesreferences.
Language:  English
Descriptors: Israel; Turkey; Iran; Triticum dicoccoides; Hordeum spontaneum;Messenger  RNA; Chlorophyll a/b binding protein; Circadian rhythm; Geneexpression; Genotypes
78                                                    NAL Call. No.: QK710.P62DNaseI-sensitive and undermethylated rDNA is preferentially expressed in amaize hybrid.Jupe, E.R.; Zimmer, E.A.Dordrecht : Kluwer Academic Publishers; 1993 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (5): p. 805-821; 1993 Mar.Includes references.
Language:  English
Descriptors: Zea mays; Ribosomal  DNA; Ribosomal  RNA; Genes; Dna methylation;Deoxyribonuclease i; Enzyme activity; Dna modification; Molecular mapping;Genetic polymorphism; Nucleotide sequences; Nucleolus; Hybrids; RepetitiveDNA; Inbred lines; Gene expression
Abstract:  An Eco RI polymorphism, present in the 26S ribosomal RNA gene(rDNA) of the maize hybrid Sx19 (B73 X Mo17), was utilized to correlate DNaseIsensitivity, undermethylation and expression in rDNA. We had previously shownthat in double digest experiments with methylation-sensitive restrictionenzymes and Eco RI, Sx19 rDNA fragments originating from repeat units with twoEco RI sites (8.0 kb) are undermethylated, whereas the fragments originatingfrom repeat units with a single Eco RI site (9.1 kb) are completelymethylated. In the present study, Sx19 rDNA chromatin structure was examinedby purifying intact nuclei and digesting them briefly with increasing amountsof DNaseI. Analysis of this DNA with Eco RI showed that the 8.0 kb rDNAfragments are extremely sensitive to DNaseI digestion, while the 9.1 kb rDNAfragments are relatively resistant to digestion even at high levels of DNaseI.Specific sites hypersensitive to DNaseI cleavage were mapped to a region inthe intergenic spacer (IGS) near the major undermethylated site. Analysis ofpolymerase chain reaction (PCR) products synthesized using Sx19, B73, and Mo17DNAs as templates indicated that the Eco RI polymorphism is due to a basechange in the recognition site. Direct rRNA sequencing identified asingle-base change in Mo17 rRNA relative to B73 rRNA. Allele-specificoligonucleotide probes containing the region surrounding and including the EcoRI polymorphic site were utilized to detect a nucleolar dominance effect byquantitating levels of rRNA transcripts in Sx19 and the reciprocal cross.Results from these single-base-pair mismatch hybridization experimentsindicate that the majority of the rRNA transcripts in Sx19 originate from theDNaseI-sensitive, undermethylated, Eco RI-polymorphic rDNA repeat units.
79                                                     NAL Call. No.: 500 N21PDominant transposition-deficient mutants of maize Activator (Ac) transposase.Kunze, R.; Behrens, U.; Courage-Franzkowiak, U.; Feldmar, S.; Kuhn, S.;Lutticke, R.Washington, D.C. : National Academy of Sciences,; 1993 Aug01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (15): p. 7094-7098; 1993 Aug01.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Mutants; Petunia; Transposableelements; Genetic code; Complementation
Abstract:  The maize transposable element Activator (Ac) encodes a transposase(TPase) protein, whose DNA-binding domain is located in a basic region aroundaa 200. The N-terminal 102 aa of the TPase are not required for thetransposition reaction. In transfected petunia protoplasts, we analyzed theprotein levels of the N-terminally truncated TPase and mutants thereof and thecorresponding transposition frequencies. The TPase protein forms largeinsoluble aggregates at high expression levels. There is no proportionalityobserved between TPase levels and transposition frequency. Twenty-onemutations (of 26), which are distributed over the whole length of the protein,inactivate the TPase completely. By coexpressing inactive mutant and activetruncated TPase, it was found that several mutations have a trans-dominantinhibitory effect. Among those are two DNA-binding-deficient mutants,indicating that inhibition of the active TPase is not caused by competitionfor the binding sites on the transposon. Accordingly, Ac TPase acts as anoligo- or multimer formed by protein-protein interactions. Peculiarly, twomutants lacking 53 and 98 aa from the C terminus that are themselvestranspositionally inactive lead to an increased excision frequency when theyare coexpressed with the active truncated TPase.
80                                                    NAL Call. No.: QK710.P62Dynamical behavior of psb gene transcripts in greening wheat seedlings. I.Time course of accumulation of the psbA through psbN gene transcripts duringlight-induced greening.Kawaguchi, H.; Fukuda, I.; Shiina, T.; Toyoshima, Y.Dordrecht : Kluwer Academic Publishers; 1992 Nov.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (4): p. 695-704; 1992 Nov.Includes references.
Language:  English
Descriptors: Triticum aestivum; Structural genes; Plant proteins; Photosystemii; Gene expression; Messenger  RNA; Greening; Seedlings; Transcription;Genetic regulation; Light; Plastids; Chloroplast genetics
Abstract:  The time course of the accumulation of the transcripts from 13 psbgenes encoding a major part of the proteins composing photosystem II duringlight-induced greening of dark-grown wheat seedlings was examined focusing onearly stages of plastid development (0.5 h through 72 h). The 13 genes can bedivided into three groups. (1) The psbA gene is transcribed as a singletranscript of 1.3 kb in the dark-grown seedlings, but its level increases 5-to 7-fold in response to light due to selective increase in RNA stability aswell as in transcription activity. (2) The psbE-F-L-J operon, psbM and psbNgenes are transcribed as a single transcript of 1.1 kb, two transcripts of 0.5and 0.7 kb and a single transcript of 0.3 kb, respectively, in the dark-grownseedlings. The levels of accumulation of every transcript remain unchanged orrather decrease during plastid development under illumination. (3) ThepsbK-I-D-C gene cluster and psbB-H operon exhibit fairly complicated northernhybridization patterns during the greening process. When a psbC or psbD geneprobe was used for northern hybridization, five transcripts differing inlength were detected in the etioplasts from 5-day old dark-grown seedlings.After 2 h illumination, two new transcripts of different length appeared.Light induction of new transcripts was also observed in the psbB-H operon.
81                                                    NAL Call. No.: QK725.P54The effect of different promoter-sequences on transient expression of gusreporter gene in cultured barley (Hordeum vulgare L.) cells.Chibbar, R.N.; Kartha, K.K.; Datla, R.S.S.; Leung, N.; Caswell, K.; Mallard,C.S.; Steinhauer, L.Berlin, W. Ger. : Springer International; 1993.Plant cell reports v. 12 (9): p. 506-509; 1993.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Genetic transformation; Promoters; Structuralgenes; Introns; Actin; Alcohol dehydrogenase; Cauliflower mosaic caulimovirus;Recombinant  DNA; Reporter genes; Beta-glucuronidase; Gene expression;Transgenic plants; Laboratory methods
Abstract:  The cauliflower mosaic virus 35S (35S) and the enhanced 35S (E35S)promoters fused with maize alcoholdehydrogenase (Adh1) intron1 or maizeshrunken locus (sh1) intron1 along with maize Adh1 and rice actin (Act1)promoters fused to their respective first introns were tested for transientexpression of the E.coli beta- glucuronidase (gus) reporter gene in culturedbarley (Hordeum vulgare L) cells. The plasmids, carrying the respectivepromoter- intron combinations to drive the gus fused to nopaline synthase(nos) terminator, were introduced into cultured barley cells using a particlegun. The rice Act1 promoter with its first intron gave the highest expressionof all promoter intron combinations studied. This was followed by the E35Spromoter and no significant differences were observed between the other twopromoters tested. The rice actin promoter is now being used to driveselectable marker genes to obtain stably transformed cereal cells.
82                                                     NAL Call. No.: 450 P692The effect of heat shock on morphogenesis in barley. Coordinated circadianregulation of mRNA levels for light-regulated genes and of the capacity foraccumulation of chlorophyll protein complexes.Beator, J.; Potter, E.; Kloppstech, K.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Dec.Plant physiology v. 100 (4): p. 1780-1786; 1992 Dec.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Gene expression; Messenger  RNA; Chlorophyll a/bbinding protein; Ribulose-bisphosphate carboxylase; Plastocyanins; Structuralgenes; Heat shock; Circadian rhythm; Plant proteins; Genetic regulation;Greening; Chlorophyll; Heat shock proteins; Ubiquitin
Abstract:  The effect of daily heat-shock treatments on gene expression andmorphogenesis of etiolated barley (Hordeum vulgare) was investigated.Heat-shock treatments in the dark induced shortening of the primary leaves andthe coleoptiles to the length of those in light-grown plantlets. In addition,the mRNA levels of the light-induced genes that were investigated were raisedunder these conditions and showed distinct oscillations over a period of atleast 3 d. While the mRNA levels for chlorophyll alb binding protein (LHC II),plastocyanin, and the small subunit of ribulose-1,5-bisphosphate carboxylasehad maxima between 8 and 12 Pm (12-16 h after the last heat-shock treatment),the mRNA levels for thionin oscillated with a phase opposed to that of LHC II.Etiolated barley, the circadian oscillator of which was synchronized by cyclicheat-shock treatments, was illuminated for a constant interval at differenttimes of the day; this led to the finding that greening was fastest at thetime when the maximal levels of mRNA for LHC II were also observed. Whereasaccumulation of chlorophyll a during a 4-h period of illumination oscillatedby a factor of 3, chlorophyll b accumulation changed 10- to 15-fold.Similarly, accumulation of LHC II was highest when pigments accumulatedmaximally. Hence, greening or, in other words, thylakoid membrane assembly isunder control of the circadian oscillator. expression and morphogenesis ofetiolated barley (Hordeum vulgare) was investigated. Heat-shock treatments inthe dark induced shortening of the primary leaves and the coleoptiles to thelength of those in light-grown plantlets. In addition, the mRNA levels of thelight-induced genes that were investigated were raised under these conditionsand showed distinct oscillations over a period of at least 3 d. While the mRNAlevels for chlorophyll alb binding protein (LHC II), plastocyanin, and thesmall subunit of ribulose-1,5-bisphosphate carboxylase had maxima between 8and 12 PM (12-16 h after the last heat-shock treatment), the mRNA levels forthionin oscillated with a phase opposed to that of LHC II. Etiolated barley,the circadian oscillator of which was synchronized by cyclic heat-shocktreatments, was illuminated for a constant interval at different times of theday; this led to the finding that greening was fastest at the time when themaximal levels of mRNA for LHC II were also observed. Whereas accumulation ofchlorophyll a during a 4-h period of illumination oscillated by a factor of 3,chlorophyll b accumulation changed 10- to 15-fold. Similarly, accumulation ofLHC II was highest when pigments accumulated maximally. Hence, greening or, inother words, thylakoid membrane assembly is under control of the circadianoscillator.
83                                                     NAL Call. No.: QK745.J6Effects of abscisic acid analogues on abscisic acid-induced gene expression inbarley aleurone protoplasts: relationship between structure and function ofthe abscisic acid molecule.Meulen, R.M. van der; Heidekamp, F.; Jastorff, B.; Horgan, R.; Wang, M.New York : Springer-Verlag New York, c1982-; 1993.Journal of plant growth regulation v. 12 (1): p. 13-19; 1993.  Includesreferences.
Language:  English
Descriptors: Hordeum vulgare; Protoplasts; Gene expression; Induction;Abscisic acid; Analogs; Molecular conformation; Binding site; Chemicalreactions
Abstract:  A 520 The plant hormone abscisic acid (ABA) mediates geneexpression in barley aleurone protoplasts. In order to elucidate the essentialfunctional groups of the ABA molecule, the specificity of a number of ABAanalogues for inducing ABA-regulated gene (e.g., RAB, BASI) expression inbarley aleurone protoplasts was studied. These analogues have modifications atthree different positions of the ABA molecule: (a) the 1'-hydroxyl group(1'-deoxy ABA), (b) the carboxyl group (ABA-methyl ester or ABA-glucoseester), and (c) both the 1'-hydroxyl and 4'-carbonyl groups (alpha-ionylideneacetic acid). The importance of the different putative functional groups wasanalyzed. The dose-response analysis of ABA analogues upon the induction geneexpression showed the following order: ABA > ABA methyl ester > 1'-deoxy ABA >ABA glucose ester > alpha-ionylidene acetic acid > alpha-beta-ionone.
84                                               NAL Call. No.: S494.5.B563C87Effects of abscisic acid and abscisic acid analogues on intracellular calciumlevel and gene expression in barley aleurone protoplasts.Wang, M.; Duijn, B. van; Meulen, R.M. van der; Heidekamp, F.Dordrecht : Kluwer Academic Publishers; 1992.Current plant science and biotechnology in agriculture v. 13: p. 635-642;1992.  In the series analytic: Progress in plant growth regulation / edited byC.M. Karssen, L.C. Van Loon and D. Vreugdenhil.  Proceedings of the 14thInternational Conference on Plant Growth Substances held July 21-26, 1991,Amsterdam, Netherlands.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Abscisic acid; Analogs; Ketones; Calcium ions;Aleurone layer; Protoplasts; Gene expression; Messenger  RNA; Structuralgenes; Plant proteins
85                                                     NAL Call. No.: 450 P699Elevated levels of tubulin transcripts accompany the GA3-induced elongation ofoat internode segments.Mendu, N.; Siflow, C.D.Kyoto, Japan : Japanese Society of Plant Physiologists; 1993 Oct.Plant and cell physiology v. 34 (7): p. 973-983; 1993 Oct.  Includesreferences.
Language:  English
Descriptors: Avena sativa; Cell growth; Gene expression; Gibberellic acid;Internodes; Transcription
Abstract:  Plant cell elongation involves the deposition of nascent cellulosemicrofibrils, the orientation of which is regulated in part by the corticalmicrotubule array. To determine whether changes in tubulin gene expression areassociated with cell elongation, we examined GA3-elicited growth of excisedinternode segments of Avena sativa. Internode elongation was barely detectableafter 6 h of GA3 treatment, when levels of beta-tubulin transcripts hadincreased 5-6 fold over levels found in untreated controls. Elongationcontinued for 48 h, whereas tubulin transcript levels reached a peak at 24 hand then declined. The extent of internode elongation and the level of tubulintranscript accumulation were dependent upon both concentration and duration ofGA3 treatment. Although a 1 h pulse of GA3 treatment was sufficient to induceelongation and enhance tubulin transcript levels, constant GA3 application wasnecessary to elicit the maximum growth and transcript accumulation responses.Inhibition of internode elongation by abscisic acid and2,6,dichlorobenzonitrile (an inhibitor of cellulose biosynthesis) orcycloheximide inhibited the GA3-mediated growth response and the accompanyingelevation of tubulin transcript levels. The strong correlation we observedbetween internode elongation and tubulin transcript level suggests thattubulin gene expression is regulated in close association with cellelongation.
86                                               NAL Call. No.: S494.5.B563C87The endosperm-specific activity of a rice prolamin promoter in transgenictobacco.Fan, Y.L.; Zhou, X.J.Dordrecht : Kluwer Academic Publishers; 1993.Current plant science and biotechnology in agriculture v. 15: p. 169-173;1993.  In the series analytic: Biotechnology in Agriculture / edited by C.You, Z. Chen, Y. Ding.  Proceedings of the First Asia-Pacific Conference onAgricultural Biotechnology held August 20-24, 1992, Beijing, China.  Includesreferences.
Language:  English
Descriptors: Oryza sativa; Nicotiana tabacum; Promoters; Prolamins;Recombinant  DNA; Reporter genes; Beta-glucuronidase; Gene expression;Histoenzymology; Endosperm
87                                                    NAL Call. No.: QK725.P54Enhanced GUS gene expression in cereal/grass cell suspensions and immatureembryos using the maize ubiquitin-based plasmid pAHC25.Taylor, M.G.; Vasil, V.; Vasil, I.K.Berlin, W. Ger. : Springer International; 1993.Plant cell reports v. 12 (9): p. 491-495; 1993.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Zea mays; Pennisetum Americanum; Saccharumofficinarum; Pennisetum purpureum; Panicum maximum; Genetic transformation;Transgenic plants; Plasmid vectors; Direct  DNAuptake; Ubiquitin; Promoters;Recombinant  DNA; Reporter genes; Beta-glucuronidase; Gene expression; Cellsuspensions
Abstract:  Transient GUS (beta-glucuronidase) expression was visualized incell suspensions of Triticum aestivum, Zea mays, Pennisetum glaucum, Saccharumofficinarum, Pennisetum purpureum and Panicum maximum after microprojectilebombardment with pBARGUS and pAHC25 plasmid DNAs. pBARGUS contains the GUS(UidA) gene coding region driven by the Adh1 promoter and the Adh1 intron 1,as well as the BAR gene coding region driven by the CaMV 35S promoter and theAdh1 intron 1. pAHC25 contains the GUS and BAR gene coding regions driven bythe maize ubiquitin promoter, first exon and first intron (Ubi1). Theeffectiveness of the constructs was first compared in cell suspension culturesby counting blue expression units (b.e.u.). The expression of construct pAHC25ranged from 3 to 50 fold greater than pBARGUS in different species. Inaddition, the two plasmids were quantitatively compared in Triticum aestivumand Zea mays by using the more sensitive GUS fluorometric assay to determinethe amount of methylumbellyferride (MU) produced. There was more than a 30fold increase in MU production with pAHC25 than with pBARGUS in the wheatsuspension, while the maize suspension showed only a 2.5 fold increase withthe pAHC25 construct. Transient GUS expression was also visualized in immatureembryos of Pennisetum glaucum following bombardment with pBARGUS and pAHC25DNA. Expression of plasmid pAHC25 was twice as high as pBARGUS. A comparisonof two DNA/gold preparation methods, as well as repeated sonications of theDNA/gold mixture, had no effect on the number of b.e.u.
88                                                     NAL Call. No.: 381 J824Evidence for the translational control of storage protein gene expression inoat seeds.Boyer, S.K.; Shotwell, M.A.; Larkins, B.A.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1992Aug25.The Journal of biological chemistry v. 267 (24): p. 17449-17457; 1992 Aug25.Includes references.
Language:  English
Descriptors: Avena sativa; Seeds; Plant proteins; Genes; Gene expression;Translation; Protein synthesis; Genetic regulation; Avenin; Globulins
Abstract:  We employed a rapid fractionation method coupled with a sensitiveenzyme-linked immunosorbent assay to quantify the globulins and avenins indeveloping and mature oat seeds. On a molar basis, there is approximately10-11 times as much globulin as avenin. Pulse labeling of endosperm proteinsindicated that the rate of globulin synthesis is approximately nine times thatof avenin. In addition, neither protein class showed any signs of degradationduring this experiment. Analysis of the storage protein mRNAs indicates thatboth globulin and avenin transcripts are associated with membrane-boundpolysomes and are found in similar concentrations within the membrane-boundpolysome fraction. We found that avenin and globulin mRNAs are fully loadedwith ribosomes, suggesting that initiation is not rate-limiting fortranslation of either protein. Rates of globulin and avenin synthesis weresimilar when synthetic storage protein mRNAs were translated in vitro.Translation of equimolar amounts of globulin and avenin mRNAs in the samereaction showed equivalent amounts of protein synthesized when compared withglobulin and avenin mRNAs translated in separate reaction mixes. We proposethat translation elongation or termination reactions are likely regulatorysteps for controlling storage protein synthesis in oat endosperm.
89                                                     NAL Call. No.: 450 P692Expression in Escherichia coli of cytochrome c reductase activity from a maizeNADH:nitrate reductase complementary DNA.Campbell, W.H.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.Plant physiology v. 99 (2): p. 693-699; 1992 Jun.  Includes references.
Language:  English
Descriptors: Zea mays; Nadh; Nitrate reductase; Dna; Gene expression;Escherichia coli; Nadh dehydrogenase; Enzyme activity; Clones; Amino acidsequences
Abstract:  A cDNA clone was isolated from a maize (Zea mays L. cv W64A XWL83E) scutellum lambda gt11 library using maize leaf NADH:nitrate reductaseZmnr1 cDNA clone as a hybridization probe; it was designated Zmnr1S. Zmnr1Swas shown to be an NADH:nitrate reductase clone by nucleotide sequencing andcomparison of its deduced amino acid sequence to Zmnr1. Zmnr1S, which is 1.8kilobases in length and contains the code for both the cytochrome b and flavinadenine dinucleotide domains of nitrate reductase, was cloned into the EcoRIsite of the Escherichia coli expression vector pET5b and expressed. The celllysate contained NADH:cytochrome c reductase activity, which is acharacteristic partial activity of NADH:nitrate reductase dependent on thecytochrome b and flavin adenine dinucleotide domains. Recombinant cytochrome creductase was purified by immunoaffinity chromatography on monoclonal antibodyZm2(69) Sepharose. The purified cytochrome c reductase, which had a major sizeof 43 kilodaltons, was inhibited by polyclonal antibodies for maize leafNADH:nitrate reductase and bound these antibodies when blotted tonitrocellulose. Ultraviolet and visible spectra of oxidized and NADH-reducedrecombinant cytochrome c reductase were nearly identical with those of maizeleaf NADH:nitrate reductase. These two enzyme forms also had very similarkinetic properties with respect to NADH-dependent cytochrome c andferricyanide reduction.
90                                                    NAL Call. No.: QK710.P62Expression of a cystein proteinase inhibitor (oryzacystatin-I) in transgenictobacco plants.Masoud, S.A.; Johnson, L.B.; White, F.F.; Reeck, G.R.Dordrecht : Kluwer Academic Publishers; 1993 Feb.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (4): p. 655-663; 1993 Feb.Includes references.
Language:  English
Descriptors: Oryza sativa; Nicotiana tabacum; Complementary  DNA; Proteinaseinhibitors; Cysteine proteinases; Recombinant  DNA; Transgenics; Genetictransformation; Gene expression; Genetic resistance; Pest resistance; Leaves;Roots; Seeds
Abstract:  Expression of cysteine proteinase inhibitors (cystatins) in tobaccoor other plants has the potential for improving resistance against pathogensand insects that possess cysteine proteinases. A chimeric gene containing acDNA clone of rice cystatin (oryzacystatin-I; OC-I), the caulifower mosaicvirus 35S promoter, and the nopaline synthase 3' region was introduced intotobacco plants by Agrobacterium tumefaciens. The presence of the chimeric genein transgenic plants was detected by a polymerase chain reaction-amplifiedassay, and transcriptional activity was shown by RNA blot analysis. Heatedextracts from transgenic tobacco plants, as well as from progeny which wereobtained by selfing a primary transformant, contained protein bands thatcorresponded in molecular mass to OC-I and reacted with antibodies raisedagainst rOC, a recombinant OC-I protein produced by Escherichia coli. Similarbands were absent in extracts from untransformed control plants. OC-I levelsreached 0.5% and 0.6% of the total soluble proteins in leaves and roots,respectively, of some progeny. On a fresh weight basis, the OC-I content washigher in leaves (50 micrograms/g) than in roots (30 micrograms/g). OC-I waspartially purified from protein extracts of rice seeds and from transgenictobacco leaves by affinity to anti-rOC antibodies. OC-I from both sources wasactive against papain.
91                                                     NAL Call. No.: 450 P699Expression of a gene specific for iron deficiency (Ids3) in the roots ofHordeum vulgare.Nakanishi, H.; Okumura, N.; Umehara, Y.; Nishizawa, N.; Chino, M.; Mori, S.Kyoto : Japanese Society of Plant Physiologists; 1993 Apr.Plant and cell physiology v. 34 (3): p. 401-410; 1993 Apr.  Includesreferences.
Language:  English
Descriptors: Hordeum vulgare; Roots; Iron; Nutrient deficiencies; Geneticregulation; Gene expression; Chelating agents; Biosynthesis; Metabolism; Iontransport; Siderophores; Genetic code; Biochemical pathways; Nucleotidesequences; Amino acid sequences
Abstract:  To clone genes required for the synthesis of mugineic acid (MA) orfor the transport of Fe(III)-MA, a lambda ZAPII cDNA library was constructedfrom poly(A)+-RNA isolated from Fe-deficient barley roots. The cDNA librarywas then used for differential screening of barley roots that had been grownin the presence and absence of iron. Seven clones that hybridized specificallyto the probe for Fe deficiency were selected. One clone, presumably encoding afull-length mRNA, as deduced from Northern hybridization, was sequenced. Theclone consisting of 1685 nucleotides encoded a putative protein of 169 aminoacids and an Mr of 18704. The gene was specifically expressed in the roots ofiron-deficient barley. A search for homologies in a protein database (NBRF)revealed that the predicted protein product has a functional peptide domainthat resembles that of 2-oxoglutarate-dependent dioxygenases.
92                                                     NAL Call. No.: 450 P692Expression of a maize ubiquitin gene promoter-bar chimeric gene in transgenicrice plants.Toki, S.; Takamatsu, S.; Nojiri, C.; Ooba, S.; Anzai, H.; Iwata, M.;Christensen, A.H.; Quail, P.H.; Uchimiya, H.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.Plant physiology v. 100 (3): p. 1503-1507; 1992 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Promoters; Introns; Exons; Structural genes;Ubiquitin; Recombinant  DNA; Reporter genes; Marker genes; Acyltransferases;Genetic transformation; Direct  DNAuptake; Electroporation; Transgenic plants;Bilanafos; Herbicide resistance; Streptomyces; Gene expression; Callus;Regenerative ability
Abstract:  We have constructed a chimeric gene consisting of the promoter,first exon, and first intron of a maize ubiquitin gene (Ubi-1) and the codingsequence of the bar gene from Streptomyces hygroscopicus. This construct wastransferred into rice (Oryza sativa L.) protoplasts via electroporation, and10 plants were regenerated from calli that had been selected for resistance toexogenously supplied bialaphos. Transgenic plants grown in a greenhouse wereresistant to both bialaphos and phosphinothricine at a dosage lethal tountransformed control plants. Evidence of stable integration of thetransferred gene into the genome of the regenerated primary transformantplants was obtained from Southern blot analysis. In addition, northern blotanalysis indicated expression and proper splicing of the maize ubiquitin genefirst intron from the primary chimeric transcript in these transgenic riceplants, and western blot analysis and enzymic assays verified expression ofthe active bar gene product. Apparent mendelian segregation for bialaphosresistance in T1 progeny of primary transformants was confirmed.
93                                                   NAL Call. No.: QK725.P532Expression of a rice homeobox gene causes altered morphology of transgenicplants.Matsuoka, M.; Ichikawa, H.; Saito, A.; Tada, Y.; Fujimura, T.; Kano-Murakami,Y.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Sep.The Plant cell v. 5 (9): p. 1039-1048; 1993 Sep.  Includes references.
Language:  English
Descriptors: Oryza sativa; Arabidopsis thaliana; Dna binding proteins;Structural genes; Genetic transformation; Transgenic plants; ComplementaryDNA; Exons; Nucleotide sequences; Amino acid sequences; Molecular mapping;Restriction fragment length polymorphism; Introns; Leaves; Morphogenesis;Plant morphology; Gene expression; Messenger  RNA; Shoot meristems; Leafprimordia; Abnormal development
Abstract:  We have isolated a cDNA clone encoding a homeobox sequence fromrice. DNA sequence analysis of this clone, which was designated as Oryzasativa homeobox 1 (OSH1), and a genomic clone encoding the OSH1 sequence haveshown that the OSH1 gene consists of five exons and encodes a polypeptide of361 amino acid residues. Restriction fragment length polymorphism analysis hasshown that OSH1 is a single-copy gene located near the phytochrome gene onchromosome 3. Introduction of the cloned OSH1 gene into rice resulted inaltered leaf morphology, which was similar to that of the maize morphologicalmutant Knotted-1 (Kn1), indicating that OSH1 is a rice gene homologous to themaize Kn1 gene. RNA gel blot analysis has shown that the gene is primarilyexpressed in the shoot apices of young rice seedlings. This finding issupported by results of transformation experiments in which the 5' flankingregion of the gene directed expression of a reporter gene in the shoot apex,particularly in stipules, of transgenic Arabidopsis. To elucidate thebiological function of the OSH1 gene product, the coding region was introducedinto Arabidopsis under the control of the cauliflower mosaic virus 35Spromoter. Almost all transformants showed abnormal morphology. The typicalphenotype was the formation of clumps of abundant vegetative and reproductiveshoot apices containing meristems and leaf primordia, which did not formelongated shoots. Some transformants with a less severe phenotype formedelongated shoots but had abnormally shaped leaves and flowers with stuntedsepals, petals, and stamens. The abnormal phenotypes were inherited, and thelevel of expression of the introduced OSH1 correlates with the severity of thephenotype. These findings indicate that the abnormal morphologies of thetransgenic plants are caused by the expression of the OSH1 gene product and,therefore, that OSH1 is related to the plant development process.
94                                               NAL Call. No.: S494.5.B563C87Expression of a rice sulfur-rich 10kDa prolamin gene in E. coli.Xu, X.M.; Fan, Y.; Yu, M.M.Dordrecht : Kluwer Academic Publishers; 1993.Current plant science and biotechnology in agriculture v. 15: p. 245-249;1993.  In the series analytic: Biotechnology in Agriculture / edited by C.You, Z. Chen, Y. Ding.  Proceedings of the First Asia-Pacific Conference onAgricultural Biotechnology held August 20-24, 1992, Beijing, China.  Includesreferences.
Language:  English
Descriptors: Oryza sativa; Escherichia coli; Structural genes; Lamins; Genetransfer; Genetic transformation; Gene expression; Nucleotide sequences;Recombinant  DNA; Promoters; Reporter genes; Beta-galactosidase
95                                                     NAL Call. No.: 442.8 Z8Expression of A/B zeins in single and double maize endosperm mutants.Paulis, J.W.; Bietz, J.A.; Bogyo, T.P.; Nelsen, T.C.; Darrah, L.L.; Zuber,M.S.Berlin, W. Ger. : Springer International; 1992 Dec.Theoretical and applied genetics v. 85 (4): p. 407-414; 1992 Dec.  Includesreferences.
Language:  English
Descriptors: Zea mays; Mutants; Epistasis; Structural genes; Zein; Prolamins;Endosperm; Opaque-2 maize; Gene expression; Hplc
Abstract:  Zeins, the major endosperm proteins in maize (Zea mays L.), aredeficient in the essential amino acids lysine and tryptophan. Some mutantgenes, like opaque-2 (o2) and floury-2 (fl2), reduce the levels of A- andB-zeins, thereby improving maize's nutritional value. Other mutants, such asamylose-extender (ae), floury-1 (fl1), soft starch (h), dull-1 (du),shrunken-1 (sh1), sugary-1 (su1), sugary-2 (su2), and waxy (wx), primarilyaffect starch composition, but also alter zein composition. We undertook thisstudy to examine the effects of some of these mutant genes on A/B-zeincomposition and to study the interactions of these genes in double-mutantcombinations. Endosperm prolamins were extracted from inbred B37, tennear-isogenic single mutants (ae, du, fl1, fl2, h, o2, sh1, su1, su2, and wx),and most double-mutant combinations. Zeins in these extracts were fractionatedby reversed-phase high-performance liquid chromatography (RP-HPLC) into 22-24peaks. Of the resulting 22 major peaks the areas of 16 (per milligramendosperm) were significantly affected by individual mutant genes relative tothe zein composition of the normal inbred. In combination these genesexhibited significant epistatic interactions in regulating the expression ofindividual A/B zeins. Epistatic interactions were judged to be significantwhen the amount of a peak in a double mutant differed from the averages forthe peak in the two respective single mutants. The o2 gene, alone and incombination with other mutant genes, significantly decreased the amounts ofmany individual zeins. The effect of the o2 gene was the greatest of all thegenes examined. Various clustering techniques were used to see if mutanteffects could be grouped; among these was principal component analysis, amultivariate statistical technique that analyzes all peak sizessimultaneously. Three-dimensional scatter graphs were constructed based on thefirst three principal components. For the single mutants, these showed norelations to gene actions; for the double mutants, however, this techniqueshowed that four single mutants, o2, sh1, su1 and su2, had the greatesteffects on sein composition when combined with each other and with theremaining six single mutants.
96                                                     NAL Call. No.: 442.8 Z8Expression of chalcone synthase, dihydroflavonol reductase, andflavanone-3-hydroxylase in mutants of barley deficient in anthocyanin andproanthocyanidin biosynthesis.Meldgaard, M.Berlin, W. Ger. : Springer International; 1992.Theoretical and applied genetics v. 83 (6/7): p. 695-706; 1992.  Includesreferences.
Language:  English
Descriptors: Hordeum vulgare; Mutants; Mutations; Structural genes;Controlling elements; Naringenin-chalcone synthase; Oxygenases;Oxidoreductases; Gene expression; Transcription; Messenger  RNA; Dna; Dnaprobes; Dna binding proteins; Anthocyanins; Biosynthesis; Nucleotidesequences; Amino acid sequences; Restriction mapping
Abstract:  A barley (cv Triumph) cDNA library was screened with a cDNA probeencoding flavanone-3-hydroxylase of Antirrhinum majus. A full-length clonecoding for a protein of 377 amino acids (42 kDa), with an overall homology of71% and a central domain homology of 85% to the Antirrhinum protein, wasisolated. This novel barley cDNA and two previously isolated cDNAs encodingchalcone synthase and dihydroquercetin reductase, respectively, were used tostudy the transcription of the corresponding genes in testa pericarp tissuefrom ant 13 mutants of barley. No or very low levels of transcripts are foundin mutants ant 13-152, ant 13-351, and ant 13-353. It is concluded that thegene Ant 13 encodes a transcription factor operating in the flavonoidbiosynthesis of barley. Transcription of the gene for theflavanone-3-hydroxylase (subunit) was also studied in an ant 17 mutant ofbarley. Mutant ant 17-352 transcribes the gene at normal or elevated levels.The mutant is blocked in the synthesis of dihydroquercetin and accumulatesderivatives of eriodictyol, the precursor of dihydroquercetin. The combinedobservations suggest that Ant 17 is the structural gene for a barleyflavanone-3-hydroxylase subunit, and that the mutant allele is a mutation inthe structural domain of the gene.
97                                                     NAL Call. No.: 450 P692Expression of chloroplast and mitochondrial genes during microsporogenesis inmaize.Moneger, F.; Mandaron, P.; Niogret, M.F.; Freyssinet, G.; Mache, R.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.Plant physiology v. 99 (2): p. 396-400; 1992 Jun.  Includes references.
Language:  English
Descriptors: Zea mays; Mitochondria; Chloroplasts; Gene expression; Pollen;Ontogeny; Developmental stages; Transcription; Mitosis; Plastids
Abstract:  Mitochondrial and plastid gene expression has been examined duringmaize (Zea mays) microsporogenesis. Accumulation of transcripts was found forthree mitochondrial genes studied (cob, atp6, and atp9) at the mid-term ofpollen development. In contrast, these mitochondrial transcripts wereundetectable in mature pollen. Southern and DNA gel blot experiments showedthat the copy number of mitochondrial genes was amplified in microspores atstages preceding the accumulation of these transcripts. Plastid transcripts ofthe photosynthetic psbA and rbcL genes could not be detected after the twomitoses, whereas precursors of the 16S rRNA are detected at low levels.
98                                                    NAL Call. No.: QK710.P62Expression of heat shock proteins during development of barley.Kruse, E.; Liu, Z.; Kloppstech, K.Dordrecht : Kluwer Academic Publishers; 1993 Oct.Plant molecular biology v. 23 (1): p. 111-122; 1993 Oct.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Heat shock proteins; Precursors; Multigenefamilies; Gene expression; Messenger  RNA; Seedlings; Seedling stage; Leaves;Genetic regulation; Heat shock; Plastids; Crop growth stage; Amino acidsequences
Abstract:  Barley heat shock proteins have been cloned, characterized byhybrid release translation Clones coding for proteins of 17, 18, 30, 32 and 70kDa have been obtained. Out of these the 32 and 30 kDa proteins have beencharacterized as precursors to plastidic proteins of 26 kDa byposttranslational transport and by cDNA sequencing. The coding regions ofthese two transcribed genes are highly homologous. Accumulation of the plastidHSP as well as of HSP 70 as well as their corresponding mRNAs has been studiedin 2- to 6-day old seedlings and in the 7-day old barley leaf. The mRNA forall investigated proteins were only found after a heat shock; the mRNA levelsincrease towards the tip of the leaf and with development. Furthermore, underthe conditions used the mRNAs for all investigated heat shock proteinsaccumulate in parallel. Unexpectedly, both proteins, HSP 70 and HSP 26, arefound by western blotting in the 2-day old control plants in the absence ofany inducing heat shock. At later stages of development and in the leafgradient only immunoreactivity with HSP 70 was observed. In contrast to thelevels of their mRNAs the highest levels of HSP 30-26 and 70 have beenobserved in the basal segments indicating that translational control plays arole during HSP expression. Under severe heat shock a protein of 30 kDa isinduced whose identity is not known but which reacts with the antibody to HSP30-26 and might represent the accumulating precursors of the plastidicproteins.
99                                                     NAL Call. No.: 442.8 Z8Expression of individual HMW glutenin subunit genes of wheat (Triticumaestivum L.) in relation to differences in the number and type of homoeologoussubunits and differences in genetic background.Kolster, P.; Krechting, C.F.; Gelder, W.M.J. vanBerlin, W. Ger. : Springer International; 1993 Oct.Theoretical and applied genetics v. 87 (1/2): p. 209-216; 1993 Oct.  Includesreferences.
Language:  English
Descriptors: Triticum aestivum; Complex loci; Structural genes; Glutenins;Molecular weight; Gene expression; Lines; Alleles
Abstract:  The amount of individual high-molecular-weight (HMW) gluteninsubunits of bread-wheat has been studied in relation to variation athomoeologous loci and in the general genetic background. The relationshipsbetween Glu-1 loci have been studied using near-isogenic lines (NILs) of thevariety Sicco and in the progenies of two crosses. Substitution of the SiccoGlu-D1 allele by a null-allele resulted in higher amounts of the homoeologoussubunits. The presence of a Glu-A1 null-allele did not have a noticeableeffect on the amounts of homoeologous subunits. In three out of four NILs andin the sister-lines of two crosses, the amounts of HMW-subunits did not dependon the allele make-up at homoeologous loci. Only in the NIL which contains theGlu-D1 allele, encoding subunits 1Dx2.2 and 1Dy12, was the amount ofhomoeologous subunits lower than the amount of these subunits in Sicco. Thisstudy suggests a relation between the amount of HMW-subunits encoded by anallele and its contribution to bread-making quality. The effect of geneticbackground has been studied using F4 and F5 lines of two crosses. The totalamounts of subunits, relative to the total amount of kernel proteins, showed aconsiderable variation between lines. The ratio between individual subunitsdid not differ between genetic backgrounds. Because this ratio is also largelyindependent of differences in environmental conditions, it is concluded thatthe relative amount of a subunit is a valuable measure for the detection ofgenetically-determined differences in the expression of HMW-subunit genes.
100                                                   NAL Call. No.: QK710.P68Expression of maize Adh1 intron mutants in tobacco nuclei.Lou, H.; McCullough, A.J.; Schuler, M.A.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Mar.The plant journal v. 3 (3): p. 393-403; 1993 Mar.  Includes references.
Language:  English
Descriptors: Nicotiana; Zea mays; Gene transfer; Mutants; Transgenics; Nuclei;Gene expression; Nucleotide sequences
101                                                     NAL Call. No.: 382 P56Expression of oat phyA cDNA in the moss Ceratodon purpureus.Thummler, F.; Schuster, H.; Bonenberger, J.Augusta, GA : American Society for Photobiology; 1992 Nov.Photochemistry and photobiology v. 56 (5): p. 771-776; 1992 Nov.  Includesreferences.
Language:  English
Descriptors: Mosses; Bryophyta; Genetic transformation; Avena sativa;Protoplast fusion; Gene expression
Abstract:  The possibility of transforming Ceratodon purpureus protoplasts byPEG-mediated direct DNA uptake was tested. Transformation with a plasmidcarrying a kanamycin-resistance gene resulted in kanamycin-resistant coloniesof C. purpureus protonemata. A full-length cDNA clone coding for oat phyAphytochrome was isolated. The clone HM4.1 which is, 3.7-kb long exhibits about99% nucleotide sequence identity to the known phytochrome clone AP3. Theexpression of HM4.1 in C. purpureus protonemata was tested. A construct withthe 35S-promotor and the structural gene of HM4.1 was cotransformed with theplasmid containing the kanamycin-resistance. Kanamycin-resistant colonies weretested for the presence of HM4.1 sequences in a genomic Southern experiment.Two out of 19 kanamycin-resistant colonies reacted positively with a HM4.1specific probe. The expression of phyA in the positive colonies was examinedwith monoclonal antibodies specific for oat phytochrome. The Western blotexperiment with protein extracts of the two positive colonies grown in thedark revealed clear signals at 124-kDa which were not detected in controlplants. These data demonstrate the possibility of expressing oatphyA-apoprotein in C. purpureus protonemata. The transgenic moss protonematadid not show phenotypical alterations in response to the foreign phytochromepolypeptide; it is not known at the moment if the tetrapyrole chromophore isattached to the oat polypeptide in the protonemata or not.
102                                                   NAL Call. No.: 450 J8224Expression of oat-phyA-cDNA in a suspension cell culture of transgenictobacco: a single-cell system for the study of phytochrome function.McCormac, A.C.; Smith, H.; Whitelam, G.C.Oxford : Oxford University Press; 1993 Jul.Journal of experimental botany v. 264 (44): p. 1095-1103; 1993 Jul.  Includesreferences.
Language:  English
Descriptors: Nicotiana tabacum; Avena sativa; Complementary  DNA; Phytochrome;Transgenic plants; Genetic transformation; Callus; Cell culture; Cellsuspensions; Gene expression; Red light; Far red light; Molecularconformation; Genetic regulation; Proteolysis
Abstract:  A culture of callus cells has been developed from a transgenic lineof tobacco which contains an introduced phyA-cDNA encoding phytochrome A.Suspension cultures of the cells were shown to accumulate a significantimmunodetectable level of the heterologous phytochrome, but not of the nativephyA-gene product. The red-irradiated form (P(fr)) of the heterologousphytochrome was specifically degraded in vivo, and the red-irradiated (P(fr))and far-red-irradiated (P(r)) forms demonstrated different patterns of invitro proteolytic cleavage. These results strongly suggested that thephytochrome apoprotein was associated with a chromophore moiety which mediatedred/far-red sensitive conformational changes of the molecule. Exogenousapplication of 4-amino-5-hexynoic acid (AHA) to the transgenic suspensioncultures resulted in the accumulation of a population of phytochrome which wasstable under red light and gave identical patterns of in vitro digestion inthe red and far-red irradiated forms, i.e. the spectral activity ofphytochrome was inhibited. Application of exogenous 5-aminolevulinic acid(ALA) or biliverdin overcame the inhibitory effects of AHA to restore spectralsensitivity of the phytochrome pool. These results are consistent with theproposed pathway of phytochrome chromophore biosynthesis in intact plantsystems. Thus, the transgenic suspension cultures provided a single-cellsystem in which spectrally-active phytochrome, apparently indistinguishablefrom the native phytochrome synthesized in etiolated seedlings, wasaccumulated. Photoregulation of expression of the genes encoding the smallsubunit of ribulose-1,5-bisphosphate carboxylase and chlorophyll a/b bindingproteins demonstrated that the heterosystem for the study of phytochromepopulation mediated rapid changes in gene expression in the de-differentiatedcells. It is therefore proposed that such a suspension culture of transgeniccells offers a model system for the study of phytochrome function.
103                                                    NAL Call. No.: 450 P699Expression of storage protein multigene families in developing rice endosperm.Kim, W.T.; Li, X.X.; Okita, T.W.Kyoto, Japanese Society of Plant Physiologists; 1993 Jun.Plant and cell physiology v. 34 (4): p. 595-603; 1993 Jun.  Includesreferences.
Language:  English
Descriptors: Oryza sativa; Multigene families; Structural genes; Glutelins;Prolamins; Gene expression; Transcription; Messenger  RNA; Endosperm; Seeddevelopment
Abstract:  Rice seeds accumulate both glutelins and prolamines as storageproteins with the former polypeptides being the predominant reserve. Toevaluate the expression of the genes that encode for these proteins duringseed development, the transcription activities and mRNA levels of several geneclasses that comprise these multigene families were assessed. Results fromnuclear run-on transcription assays and RNA blot studies showed that theexpression of these gene classes for each multigene family was not coordinatebut instead differentially regulated at both the transcriptional andpost-transcriptional levels. Quantification of their total mRNA levelsrevealed equimolar amounts of their mRNAs in 5 and 10 day old seeds and a 40%excess of prolamine transcripts, relative to glutelin transcripts, in seeds of15 days and older. In spite of the significant steady state levels ofprolamine transcripts, glutelin mRNAs were detected at two-fold greater excessin membrane bound polysomes throughout seed development, thereby accountingfor, at least in part, the greater accumulation of this storage protein inrice endosperm. These results suggest that, in addition to regulation at thetranscriptional/post-transcriptional levels, ER membrane-associatedtranslational control is also involved in the expression of rice seed storageprotein multigene families.
104                                                    NAL Call. No.: 450 P692Expression of the Acc1 gene-encoded acetyl-coenzyme A carboxylase indeveloping maize (Zea mays L.) kernels.Somers, D.A.; Keith, R.A.; Egli, M.A.; Marshall, L.C.; Gengenbach, B.G.;Gronwald, J.W.; Wyse, D.L.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Mar.Plant physiology v. 101 (3): p. 1097-1101; 1993 Mar.  Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Acetyl-coa carboxylase; Geneexpression; Seed development; Kernels; Enzyme activity; Endosperm; Plantembryos; Sethoxydim
Abstract:  A mutation (Acc1-S2) in the structural gene for maize (Zea mays L.)acetyl-coenzyme A carboxylase (ACCase) that significantly reduces sethoxydiminhibition of leaf ACCase activity was used to investigate the gene-enzymerelationship regulating ACCase activity during oil deposition in developingkernels. Mutant embryo and endosperm ACCase activities were more than 600-foldless sensitive to sethoxydim inhibition than ACCase in wild-type kerneltissues. Moreover, in vitro cultured mutant kernels developed normally in thepresence of sethoxydim concentrations that inhibited wild-type kerneldevelopment. The results indicate that the Acc1-encoded ACCase accounts forthe majority of ACCase activity in developing maize kernels, suggesting thatAcc1-encoded ACCase functions not only during membrane biogenesis in leavesbut is also the predominant form of ACCase involved in storage lipidbiosynthesis in maize embryos.
105                                                   NAL Call. No.: QK710.P68Expression of the alpha-thionin gene from barley in tobacco confers enhancedresistance to bacterial pathogens.Carmona, M.J.; Molina, A.; Fernandez, J.A.; Lopez-Fando, J.J.; Garcia-Olmedo,F.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Mar.The plant journal v. 3 (3): p. 457-462; 1993 Mar.  Includes references.
Language:  English
Descriptors: Nicotiana tabacum; Hordeum vulgare; Agrobacterium tumefaciens;Gene transfer; Transgenics; Gene expression; Thioneins; Protein synthesis;Pathogenesis-related proteins; Disease resistance; Pseudomonas syringae pv.tabaci
106                                                   NAL Call. No.: 442.8 Z34Expression of the gene encoding the PR-like protein PRms in germinating maizeembryos.Casacuberta, J.M.; Raventos, D.; Puigdomenech, P.; San Segundo, B.Berlin, W. Ger. : Springer International; 1992 Jul.M G G : Molecular and general genetics v. 234 (1): p. 97-104; 1992 Jul.Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Pathogenesis-related proteins; Geneexpression; Plant embryos; Seed germination; Genetic regulation; Defensemechanisms; Scutellum; Gibberella fujikuroi; Fungal diseases; Cell wallcomponents; Gibberellic acid
Abstract:  The PRms protein is a pathogenesis-related (PR)-like protein whosemRNA accumulates during germination of maize seeds. Expression of the PRmsgene is induced after infection of maize seeds with the fungus Fusariummoniliforme. To further our investigations on the expression of the PRms genewe examined the accumulation of PRms mRNA in different tissues of maizeseedlings infected with F. moniliforme and studied the effect of fungalelicitors, the mycotoxin moniliformin, the hormone gibberellic acid, andspecific chemical agents. Our results indicate that fungal infection, andtreatment either with fungal elicitors or with moniliformin, a mycotoxinproduced by F. moniliforme, increase the steady-state level of PRms mRNA. PRmsmRNA accumulation is also stimulated by the application of the hormonegibberellic acid or by treatment with silver nitrate, whereas acetylsalicylicacid has no effect. In situ RNA hybridization in isolated germinating embryosections demonstrates that the PRms gene is expressed in the scutellum,particularly in a group of inner cells, and in the epithelium lying at theinterface of the scutellum and the endosperm. The pattern of expression of thePRms gene closely resembles that found for hydrolytic enzymes, being confinedto the scutellum and the aleurone layer of the germinating maize seed. Ourresults suggest that the PRms protein has a function during the normal processof seed germination that has become adapted to serve among the defencemechanisms induced in response to pathogens during maize seed germination.
107                                                  NAL Call. No.: QK725.P532Expression of the two maize TATA binding protein genes and function of theencoded TBP proteins by complementation in yeast.Vogel, J.M.; Roth, B.; Cigan, M.; Freeling, M.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Nov.The Plant cell v. 5 (11): p. 1627-1638; 1993 Nov.  Includes references.
Language:  English
Descriptors: Zea mays; Saccharomyces cerevisiae; Structural genes; Multiplegenes; Dna binding proteins; Gene expression; Messenger  RNA; Genetictransformation; Complementation; Mutations; Mutants; Molecular mapping;Linkage; Nucleotide sequences; Amino acid sequences; Complementary  DNA
Abstract:  A single gene encodes the TATA binding protein (TBP) in yeasts andanimals. Although two TBP-encoding genes (Tbp) previously were isolated fromboth Arabidopsis and maize, the expression and in vivo function of the encodedplant TBPs were not investigated. Here, we report that the two highlyconserved maize Tbp genes are unlinked and reside within larger, ancestrallyduplicated segments in the genome. We find quantitative differences in Tbp1versus Tbp2 transcript accumulation in some maize tissues. These nonidenticalexpression patterns may indicate differences in the tissue-specific regulationof these genes, which might allow the two encoded maize TBP isoforms toperform nonoverlapping functions in the plant. In addition, we show that themaize TBP products, unlike animal TBPs, are functionally interchangeable withyeast TBP for conferring yeast cell viability. This is a conclusivedemonstration of in vivo activity for a nonyeast TBP protein, and thesecomplementation results point to particular amino acids in TBP that are likelyto influence species-specific protein interactions.
108                                                   NAL Call. No.: QK710.P62Expression, organisation and structure of the genes encoding the waxy protein(granule-bound starch synthase) in wheat.Ainsworth, C.; Clark, J.; Balsdon, J.Dordrecht : Kluwer Academic Publishers; 1993 Apr.Plant molecular biology v. 22 (1): p. 67-82; 1993 Apr.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Complementary  DNA; Structural genes;Hexosyltransferases; Loci; Gene expression; Messenger  RNA; Filling period;Seeds; Starch granules; Amino acid sequences
Abstract:  A full-length cDNA clone representing the waxy protein (GBSSI)isolated from a hexaploid wheat developing grain cDNA library has been used tocharacterise the organization and expression of the waxy genes in wheat. Thegenes are organised as a triplicate set of single copy homeoloci on chromosomearms 4AL, 7AS and 7DS. The genes are active throughout grain filling where themain 2.3 kb transcript accumulates to high levels. The 2.3 kb transcript isnot expressed in leaves where the presence of a related, but less homologous,transcript of 1.6 kb suggests that a different set of genes operates. Gelanalysis and purification of the waxy protein isolated from starch granules,followed by N-terminal amino acid sequencing in conjunction with data fromhybrid select translation experiments and sequence analysis of the cDNA, showsthat the mature protein has a molecular weight of 6OkDa (615 amino acids) andthat the preprotein includes a chloroplast/amyloplast transit peptide of 7kDa(75 amino acids). Analysis of the derived amino acid sequence and alignmentwith five other plant waxy proteins shows that they exhibit substantialhomology. The wheat protein differs from all others in that it contains an 11amino acid insertion towards the N-terminus.The protein contains the conservedmotif KTGGL found in other waxy proteins and which has been implicated as theactive site in glycogen synthase.
109                                                    NAL Call. No.: 442.8 Z8Factors affecting transient gene expression in protoplasts isolated from veryslowly growing embryogenic callus cultures of wheat (Triticum aestivum L.).Zaghmout, O.M.F.; Trolinder, N.L.Berlin, W. Ger. : Springer International; 1993 Jul.Theoretical and applied genetics v. 86 (6): p. 721-730; 1993 Jul.  Includesreferences.
Language:  English
Descriptors: Triticum aestivum; Vitis vinifera; Gene expression; Reportergenes; Beta-glucuronidase; Recombinant  DNA; Cauliflower mosaic caulimovirus;Alcohol dehydrogenase; Promoters; Protoplasts; Electroporation; Genetictransformation; Transgenic plants; Callus; Embryogenesis; Enzyme activity;Histoenzymology; Tobacco mosaic tobamovirus; Nucleotide sequences; Plasmidvectors; Regenerative ability
Abstract:  Protoplasts isolated from embryogenic ('Mustang' and 'ChineseSpring') and non-embryogenic ('Mit') calli of wheat (Triticum aestivum L.)genotypes transiently expressed beta-glucuronidase (GUS) activity whenelectroporated with a plasmid containing the GUS gene and driven by anenhanced 35S promoter and a TMV leader sequence. Conditions for the maximumexpression of GUS activity were: electroporation of the freshly isolatedprotoplasts at 250 Vcm- and 250 microF for 2 s using 50 microgram/ml ofplasmid DNA; incubation of the protoplasts with the plasmid before the pulsefor 2 h; and a 15-min recovery period on ice after the pulse. In general, ahigher GUS activity was obtained in protoplasts of non-embryogenic (NE) callusorigin than in those of embryogenic (E) callus origin. Only GUS constructscontaining a duplicate 35S promoter derivative resulted in a significant levelof GUS expression. The presence of the TMV viral leader sequence in thepAGUS1-TN2 plasmid construct resulted in a significant increase of GUSactivity in the electroporated protoplasts of both callus types. On the otherhand, protoplasts electroporated with the Adh1 promoter and intron showed athreefold less GUS activity than those electroporated with pAGUS1-TN2.Optimized conditions for DNA uptake and expression were very similar forprotoplasts of both callus types. The importance of these findings for thesuccessful regeneration of transgenic and fertile wheat plants is discussed.
110                                                   NAL Call. No.: QK710.P62Factors influencing Agrobacterium-mediated transient expression of gusA inrice.Li, X.Q.; Liu, C.N.; Ritchie, S.W.; Peng, J.Y.; Gelvin, S.B.; Hodges, T.K.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (6): p. 1032-1048; 1992 Dec.Includes references.
Language:  English
Descriptors: Oryza sativa; Agrobacterium tumefaciens; Genetic transformation;Gene expression; Reporter genes; Beta-glucuronidase; Gene transfer; Plasmids;Transgenics; Genetic regulation; 2,4-d; Culture; Explants; Leaves; Roots;Seeds; Shoots; Amino acid derivatives
Abstract:  Transient expression of GUS in rice (Oryza sativa L.) mediated byAgrobacterium tumefaciens was characterized using binary vectors containinggusA genes that express minimal (pKIWI105 and pCNL1) or no (p35S-GUS-INT andpCNL56) GUS activity in bacteria. Four-day old seedlings obtained from seedsor immature embryos of rice were cut into shoot, root, and seed remnants andinoculated with various strains of A. tumefaciens. Transient GUS expressionevents were quantitated histochemically by determining the frequency ofexplants exhibiting blue spots indicative of GUS at four to six days aftercocultivation with A. tumefaciens. A. tumefaciens strains that did not containthe gusA gene (At643) or a Ti-plasmid (At563 and At657) did not elicit anyblue staining characteristic of GUS activity. Several parameters wereimportant in obtaining efficient transient expression of GUS in rice mediatedby A. tumefaciens. The growth regulator 2,4-D inhibited GUS expression ifpresent during the seed germination period, but the presence of 6 mg/l 2,4-Dduring cocultivation of the explants with A. tumefaciens slightly enhanced GUSexpression efficiency. All 21 rice cultivars tested expressed GUS afterco-cultivation with A. tumefaciens. The GUS expression frequency was highestamongst the indica cultivars. The frequencies of GUS expression in japonicacultivars and in Oryza glaberrima cultivars (grown primarily in Africa) weregenerally one-half to one-third the level found for indica varieties. Leafexplants were more susceptible to A. tumefaciens-facilitated GUS expressionthan were roots or seed remnants. The vir genes of an agropine-type Ti-plasmidof A. tumefaciens were most effective in directing transient GUS expression inrice, whereas those of a nopaline-type and an octopine-type plasmid were lesseffective. We have also found that the frequency of transient expression ofGUS was higher with pBIN19 as the precursor cloning vector than with pEND4K asthe precursor cloning vector.  Reasons for differences in effectiveness ofthese binary vectors are discussed.  Using the conditions described here, A.tumefaciens-mediated frequencies of transient GUS expression in four-day oldshoot of several rice cultivars were routinely in excess of 50%.
111                                                    NAL Call. No.: 450 P692Five genes induced by aluminum in wheat (Triticum aestivum L.) roots.Snowden, K.C.; Gardner, R.C.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Nov.Plant physiology v. 103 (3): p. 855-861; 1993 Nov.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Root tips; Aluminum; Treatment; Dna; Geneexpression; Nucleotide sequences; Clones; Tolerance; Phytotoxicity
Abstract:  Five different cDNAs (termed wali1 to wali5 for wheat aluminuminduced) whose expression was induced by Al stress have been isolated from theroot tips of Al-treated wheat (Triticum aestivum L.) plants. Four of thesegenes were induced 24 to 96 h after Al treatment, and their expression isreduced when the Al is removed. Each of these four genes was induced byinhibitory levels of Al in two wheat cultivar's--Warigal, an Al-sensitivecultivar, and Waalt, an Al-tolerant cultivar. The fifth gene (wali2) showed acomplex bimodal pattern of induction and was induced by Al only in thesensitive cultivar. Comparison of the nucleotide sequences of these clones tothose in the sequence data bases showed that wali4 is homologous tophenylalanine ammonia-lyase and wali1 is homologous to a group of plantproteins that are cysteine-rich and have homology to metallothioneins. wali2encodes a novel protein with a repeating motif of cysteine amino acids. Theremaining two wali clones (wali3 and wali5) encode related, cysteine-richproteins that show no significant homology to any known sequences.
112                                                   NAL Call. No.: QP601.M49Foreign gene expression in chloroplasts of higher plants mediated by Tungstenparticle bombardment.Daniell, H.New York : Academic Press, 1955-; 1993.Methods in enzymology v. 217: p. 536-556; 1993.  In the series analytic:Recombinant DNA (Part H) / edited by R. Wu.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Nicotiana tabacum; Beta vulgaris;Chloroplasts; Genetic transformation; Recombinant  DNA; Gene expression
113                                                   NAL Call. No.: QK710.P68Four members of the maize beta-tubulin gene family are expressed in the malegametophyte.Rogers, H.J.; Greenland, A.J.; Hussey, P.J.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Nov.The Plant journal : for cell and molecular biology v. 4 (5): p. 875-882; 1993Nov.  Includes references.
Language:  English
Descriptors: Zea mays; Amino acid sequences; Clones; Dna; Tubulin; Gametes;Gene expression; Males; Nucleotide sequences
114                                                  NAL Call. No.: QH442.A1G4The gene encoding a calcium-dependent protein kinase located near the sbe1gene encoding starch branching enzyme I is specifically expressed indeveloping rice seeds.Kawasaki, T.; Hayashida, N.; Baba, T.; Shinozaki, K.; Shimada, H.Amsterdam : Elsevier Science Publishers; 1993.Gene v. 129 (2): p. 183-189; 1993.  Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Complementary  DNA; Proteinkinase; Calcium ions; Binding site; Nucleotide sequences; Amino acidsequences; Gene mapping; Gene expression; Seed development; Calmodulin
Abstract:  A gene (spk) encoding a Ca(2+)-dependent protein kinase (SPK) islocated in the region immediately upstream of the sbe1 gene encoding a starchbranching enzyme. The spk gene is specifically expressed in developing seedsand its expression pattern is very similar to those of genes encodingstarch-synthesizing enzymes such as sbel and waxy, seed lipid-synthesizingenzymes, as well as genes encoding seed storage proteins. A full-length spkcDNA was isolated from a cDNA library constructed from developing seeds. Thededuced amino acid sequence showed that SPK has a high degree of homology tosoybean and carrot Ca(2+)-dependent protein kinase, both of which containcalmodulin domains. The calmodulin domain, as well as the catalytic subdomainconsensus regions of protein kinases are highly conserved in SPK. Theseresults suggest that a tissue- and stage-specific protein kinase, SPK, isinvolved in the synthesis of seed storage compounds during seed development.They also strongly suggest that Ca(2+) is required for seed development.
115                                                   NAL Call. No.: QK710.P62Gene structure and expression of rice seed allergenic proteins belonging tothe alpha-amylase/trypsin inhibitor family.Adachi, T.; Izumi, H.; Yamada, T.; Tanaka, K.; Takeuchi, S.; Nakamura, R.;Matsuda, T.Dordrecht : Kluwer Academic Publishers; 1993 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (2): p. 239-248; 1993 Jan.Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Dna; Seeds; Enzyme inhibitors;Alpha-amylase; Trypsin inhibitors; Nucleotide sequences; Promoters; Amino acidsequences; Prediction; Multigene families; Gene expression; Seed development;Messenger  RNA; Allergens; Complementary  DNA
Abstract:  Genomic and two novel cDNA clones for rice seed allergenic protein(RA) belonging to the alpha-amylase/trypsin inhibitor family were isolated andtheir nucleotide sequences determined. Ten cysteine residues deduced fromnucleotide sequences were completely conserved among three cDNA clonesincluding a clone, RA17, reported previously. One genomic clone, lambda 4,contained two RA genes, RAG1 and RAG2. Although RAG1 was cloned at the 5'portion only, two RA genes were arranged divergently. Nucleotide sequencingand DNA blotting analyses showed that RA are encoded by a multigene familyconsisting of at least four members. The transcriptional initiation site ofRAG1 was localized at A, 26 bp upstream of the putative translationalinitiation codon, ATG, by the primer extension assay. The putative TATA boxand CAAT box existed about 45 bp and 147 bp upstream of the transcriptioninitiation site, respectively. A conserved sequence (ATGCAAAA) which wassimilar to the sequence (TGCAAAA) identified in rice glutelin promoters wasobserved in the 5' region of the two genes. In addition, RNA blotting analysesprovided that RA genes specifically expressed in ripening seed and theirtranscripts accumulated maximally between 15 and 20 days after flowering.
116                                              NAL Call. No.: QK728.P52 1992Gene transfer to barley.Mendel, R.R.; Clauss, E.; Schulze, J.; Steinbiss, H.H.; Nerlich, A.Boca Raton : CRC Press; 1992.Plant biotechnology and development / editor, Peter M. Gresshoff. p. 117-121;1992. (A CRC series of current topics in plant molecular biology).  Includesreferences.
Language:  English
Descriptors: Hordeum vulgare; Gene transfer; Direct  DNAuptake;Inflorescences; Genetic transformation; Protoplasts; Pollen tubes; Geneexpression
117                                                   NAL Call. No.: QK725.P54Gene transfer to maize male reproductive structure by particle bombardment oftassel primordia.Dupuis, I.; Pace, G.M.Berlin, W. Ger. : Springer International; 1993.Plant cell reports v. 12 (11): p. 607-611; 1993.  Includes references.
Language:  English
Descriptors: Zea mays; Pollen; Gene transfer; Dna; Tassels; Anther culture;Gene expression; Beta-glucuronidase; Anthocyanins; Marker genes; Culturetechniques
Abstract:  Maize (Zea mays L.) tassel primordia were used as a target forparticle bombardment, to assess the possibility of introducing foreign DNAinto male reproductive structures. Transient expression of thebeta-glucuronidase gene (GUS) or anthocyanin marker genes (C1 and B-Peru)driven by the CaMV 35S promoter was obtained in tassel primordia 24h afterbombardment. Gold particles coated with DNA reached stamen primordia tissues,which eventually form the anthers and pollen. Bombarded tassels were alsocultured in vitro and GUS activity was detected in the vascular tissue ofmature anthers that developed within 4 weeks. This new approach represents apreliminary step toward pollen mediated transformation.
118                                                   NAL Call. No.: QH301.A76Genetic control of frost tolerance.Hughes, M.A.; Dunn, M.A.; Zhang, L.; Pearce, R.S.; Goddard, N.J.; White, A.J.Wellesbourne, Warwick : The Association of Applied Biologists; 1993.Aspects of applied biology / (34): p. 163-171; 1993.  In the series analytic:Physiology of varieties / edited by E. White, P.S. Kettlewell, M.A. Parry, andR.P. Ellis.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Cloning; Frost resistance; Gene expression;Genetic regulation; Inheritance; Temperature; Acclimatization; Biochemistry
119                                                   NAL Call. No.: 59.8 C333Genetic engineering and hybridization of wheat.Kureczka, J.E.St. Paul, Minn. : American Association of Cereal Chemists; 1992 Aug.Cereal foods world v. 37 (8): p. 640-642; 1992 Aug.  Includes references.
Language:  English
Descriptors: Wheat; Hybridization; Genetic engineering; Genetictransformation; Gene expression; Food quality
Abstract:  Experts say the creation of useful-new varieties of wheat throughgenetic engineering requires success in three discrete areas. First, genetictransformation technologies must be perfected for use in wheat. Second,commercially useful genes and expression systems must be isolated and madeavailable. Finally, and perhaps most importantly from a business standpoint,new hybridization technologies must be developed that work efficiently withthis normally self-pollinating grain.
120                                                  NAL Call. No.: QK725.P532Genetic isolation, cloning, and analysis of a Mutator-induced, dominantantimorph of the maize amylose extender1 locus.Stinard, P.S.; Robertson, D.S.; Schnable, P.S.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Nov.The Plant cell v. 5 (11): p. 1555-1566; 1993 Nov.  Includes references.
Language:  English
Descriptors: Antirrhinum majus; Loci; Induced mutations; Structural genes;Kinases; Dominance; Genetic polymorphism; Repetitive  DNA; Transposableelements; Gene expression; Transcription; Messenger  RNA; Endosperm;Restriction mapping
Abstract:  We report the genetic identification, molecular cloning, andcharacterization of a dominant mutant at the amylose extender1 locus,Ae1-5180. The identities of our clones are corraborated by their ability toreveal DNA polymorphisms between seven wild-type revertants from Ae1-5180relative to the Ae1-5180 mutant allele and between four of five independentlyderived, Mutator (Mu)-induced recessive ae1 alleles relative to theirrespective wild-type progenitor alleles. The Ae1-5180 mutation is associatedwith two Mu1 insertions flanked by complex rearrangements of ae1-relatedsequences. One of the Mu1 elements is flanked by inverted repeats ofae1-related DNA of at least 5.0 kb in length. This Mu1 element and at leastsome of this flanking inverted repeat DNA are absent or hypermethylated in sixof seven wild-type revertants of Ae1-5180 that were analyzed. The second Mu1element is flanked on one side by the 5.0-kb ae1-specific repeat and on theother side by a sequence that does not hybridize to the ae1-related repeatsequence. This second Mu1 element is present in revertants to the wild typeand does not, therefore, appear to affect ae1 gene function. A 2.7-kb ae1transcript can be detected in wild-type and homozygous ae1-Ref endosperms 20days after pollination. This transcript is absent in endosperms containingone, two, or three doses of Ae1-5180. This result is consistent with asuppression model to explain the dominant gene action of Ae1-5180 andestablishes Ae1-5180 as an antimorphic allele. Homozygous wild-type seedlingsproduce no detectable transcript, indicating some degree of tissue specificityfor ae1 expression. Sequence analyses establish that ae1 encodes starchbranching enzyme II.
121                                              NAL Call. No.: S494.5.B563C87Genetic variation in ABA production in maize determines the extent ofdrought-induced gene transcription.Quarrie, S.A.; Steed, A.; Lazic-Jancic, V.; Kovacevic, D.Dordrecht : Kluwer Academic Publishers; 1992.Current plant science and biotechnology in agriculture v. 13: p. 770-777;1992.  In the series analytic: Progress in plant growth regulation / edited byC.M. Karssen, L.C. Van Loon and D. Vreugdenhil.  Proceedings of the 14thInternational Conference on Plant Growth Substances held July 21-26, 1991,Amsterdam, Netherlands.  Includes references.
Language:  English
Descriptors: Zea mays; Transcription; Gene expression; Water stress; Drought;Abscisic acid; Biosynthesis; Genetic variation; Protein synthesis; Plantproteins
122                                                   NAL Call. No.: QK710.P68A gibberelin-regulated gene from wheat with sequence homology to cathepsin Bof mammalian cells.Cejudo, F.J.; Murphy, G.; Chinoy, C.; Baulcombe, D.C.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Nov.The plant journal v. 2 (6): p. 937-948; 1992 Nov.  Includes references.
Language:  English
Descriptors: Triticum; Amino acid sequences; Cathepsins; Dna; Gene expression;Genetic code; Genetic regulation; Gibberellins; Messenger  RNA; Nucleotidesequences; Transcription
123                                              NAL Call. No.: S494.5.B563C87The gibberellin response element: a DNA sequence in cereal alpha-amylase genepromoters that mediates GA and ABA effects.Rogers, J.C.; Lanahan, M.B.; Rogers, S.W.; Mundy, J.Dordrecht : Kluwer Academic Publishers; 1992.Current plant science and biotechnology in agriculture v. 13: p. 136-146;1992.  In the series analytic: Progress in plant growth regulation / edited byC.M. Karssen, L.C. Van Loon and D. Vreugdenhil.  Proceedings of the 14thInternational Conference on Plant Growth Substances held July 21-26, 1991,Amsterdam, Netherlands.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Triticum aestivum; Avena sativa; Promoters;Binding site; Dna binding proteins; Alpha-amylase; Structural genes; Geneexpression; Transcription; Messenger  RNA; Genetic regulation; Gibberellicacid; Abscisic acid; Aleurone layer; Literature reviews
124                                                  NAL Call. No.: QK725.P532Gibberellin-responsive elements in the promoter of a barley high-plalpha-amylase gene.Gubler, F.; Jacobensen, J.V.Rockville, Md. : American Society of Plant Physiologists; 1992 Nov.The Plant cell v. 4 (11): p. 1435-1441; 1992 Nov.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Promoters; Alpha-amylase; Controlling elements;Gibberellic acid; Abscisic acid; Genetic regulation; Gene expression;Beta-glucuronidase; Reporter genes; Targeted mutagenesis; Recombinant  DNA;Transcription
Abstract:  Deletion analysis has previously shown that the major gibberellicacid (GA)- and abscisic acid (ABA)-responsive elements in the promoter of ahigh-pI alpha-amylase gene of barley are located downstream of -174 (Jacobsenand Close, 1991). We have used transient expression assays in barley aleuroneprotoplasts to identity sequences between -174 and +53 that confer GA and ABAresponsiveness on expression of a beta-glucuronidase reporter gene. Usingalpha-amylase promoter fragments and synthetic oligonucleotides fused tominimal promoters, we have shown that the hormone-responsive region is locatedbetween -174 and -108. A single copy of this region fused to a minimalalpha-amylase promoter (-41) conferred both GA- and ABA-responsive expressionon the reporter gene comparable to the positive control, Am(-174)IGN. Multiplecopies of this region were able to activate even greater levels of expression.Site-directed mutagenesis was used to determine the functional importance ofthe conserved motifs ((-169)pyrimidine box, (-143)TAACAAA box, and(-124)TATCCAC box) and nonconserved intervening sequences within the regionbetween -174 and -108. Our results showed that both the TAACAAA and TATCCACboxes play an important role in GA-regulated expression. We propose that theTAACAAA box is a gibberellin response element, that the TATCCAC box actscooperatively with the TAACAAA box to give a high level of GA-regulatedexpression, and that together these motifs form important components of agibberellin response complex in high-pI alpha-amylase genes. The TAACAAA boxalso appears to be the site of action of ABA. In addition, we have identifieda sequence that acts as a repressor of GA action and that resembles a cAMPresponse element.
125                                                    NAL Call. No.: 450 P692Glutamine induces the N-dependent accumulation of mRNAs encodingphosphoenolpyruvate carboxylase and carbonic anhydrase in detached maize leaftissue.Sugiharto, B.; Suzuki, I.; Burnell, J.N.; Sugiyama, T.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Dec.Plant physiology v. 100 (4): p. 2066-2070; 1992 Dec.  Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Messenger  RNA; Phosphoenolpyruvatecarboxylase; Carbonate dehydratase; Gene expression; Genetic regulation;Glutamine; Leaves; Nitrate; Glutamic acid; Alanine; Serine; Glycine; Enzymeactivity; Glutamate-ammonia ligase
Abstract:  We have used detached leaves to study the N-dependent control ofexpression of phosphoenolpyruvate carboxylase (PEPC) and carbonic anhydrase(CA) genes in maize (Zea mays L. cv Golden Cross Bantam T51). Followingsupplementation with an N-source and zeatin, PEPC and CA mRNA levels increasedin leaves detached from N-deficient maize plants. Addition of methioninesulfoximine (MSX), a specific inhibitor of glutamine synthetase, inhibited thenitrate-dependent increase of PEPC and CA mRNA but did not affect theglutamine-dependent increase of PEPC and CA mRNA levels. Glutamine levels indetached maize leaves treated with various N sources in the presence orabsence of MSX correlated with the levels of PEPC and CA mRNA. We concludethat glutamine is the most likely effector for controlling the N-dependentexpression of PEPC and CA in maize plants.
126                                                    NAL Call. No.: 450 P692Glutamine synthetase and ferredoxin-dependent glutamate synthase expression inthe maize (Zea mays) root primary response to nitrate. Evidence for anorgan-specific response.Redinbaugh, M.G.; Campbell, W.H.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Apr.Plant physiology v. 101 (4): p. 1249-1255; 1993 Apr.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Messenger  RNA; Glutamate-ammonialigase; Glutamate synthase; Ferredoxin; Genetic regulation; Nitrate; Roots;Leaves; Nitrate reductase
Abstract:  To define further the early, or primary, events that occur in maize(Zea mays) seedlings exposed to NO3(-)1 accumulation of chloroplast glutaminesynthetase (GS2; EC 6.3.1.2) and ferredoxin-dependent glutamate synthase(Fd-GOGAT; EC 1.4.7.1), transcripts were examined in roots and leaves. Inroots, NO3(-) treatment caused a rapid (within 30 min), transient, andcycloheximide-independent accumulation of GS2 and Fd-GOGAT transcripts. Inaddition, 10 micromolar external NO3(-) was sufficient to cause transcriptaccumulation. The induction was NO3(-) specific, since NH4Cl treatment did notaffect mRNA levels. GS2 and Fd-GOGAT mRNA accumulation in roots was similar tothat observed for nitrate reductase (NR) mRNA. Therefore, the four genesinvolved in NO3- assimilation (NR, nitrite reductase, GS2, and Fd-GOGAT) areexpressed in the root primary response to NO3(-), suggesting that all fourgenes can respond to the same signal transduction system. In contrast,relatively high levels of GS2 and Fd-GOGAT mRNAs were present in untreatedleaf tissue, and NO3(-) treatment had little or no influence on transcriptaccumulation. Rapid, transient, and cycloheximide-independent NR mRNAexpression was seen in the NO3(-)-treated leaves, demonstrating that NO3(-)was not limiting. The NO3(-) -independent constitutive expression of GS2 andFd-GOGAT is likely due to the requirement for reassimilation ofphotorespiratory NH4+ in these young leaves.
127                                                    NAL Call. No.: 450 P692Group 3 late embryogenesis abundant proteins in desiccation-tolerant seedlingsof wheat (Triticum aestivum L.).Ried, J.L.; Walker-Simmons, M.K.Rockville, Md. : American Society of Plant Physiologists; 1993 May.Plant physiology v. 102 (1): p. 125-131; 1993 May.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Seedlings; Plant embryos; Embryogenesis;Protein content; Desiccation; Tolerance; Antibodies; Genetic regulation; Geneexpression; Dormancy
Abstract:  Dormant seeds and young seedlings of wheat (Triticum aestivum L.)tolerate desiccation. A transcript expressed in this desiccation-toleranttissue has been cloned and sequenced (J. Curry, C.F. Morris, M.K.Walker-Simmons [1991] Plant Mol Biol 16: 1073-1076). This wheat cDNA cloneencodes a protein that is homologous to other group 3 late embryogenesisabundant (LEA) proteins. In this report, we describe the production ofpolyclonal antibodies to the protein product of the cDNA clone and assessgroup 3 LEA protein levels in desiccation-tolerant tissue. The group 3 LEAantibodies detected four major proteins in wheat with molecular masses from 27to 30.5 kD. The genes for these proteins mapped to wheat chromosomes 1A, 1B,and 1D. The group 3 LEA proteins were present in mature seed embryos and weremaintained when growth-arrested, dormant seeds were hydrated for 111 h.However, in germinating seeds the group 3 LEA proteins declined and were nolonger detectable by 111 h. We severely dehydrated seedlings (more than 90%water loss) to assess group 3 LEA transcript and protein accumulation intissues of these desiccation-tolerant plants. In response to dehydration,abscisic acid (ABA) levels increased dramatically and group 3 LEA mRNAs wereinduced in root, shoot, and scutellar tissue. However, group 3 LEA proteinswere detected only in shoot and scutellar tissue and not in root tissue.Treatment of nonstressed seedlings with 20 micromolar ABA resulted in lowlevels of group 3 LEA proteins in the roots, whereas higher levels were foundin the shoot and scutellar tissue. When dehydrated seedlings were rehydrated,shoot and scutellar tissue resumed growth. The roots did not resume growth andsubsequently died. New roots developed later from the scutellar tissue. Thus,in severely dehydrated wheat seedlings, the accumulation of high levels ofgroup 3 LEA proteins is correlated with tissue dehydration tolerance.
128                                                NAL Call. No.: SB113.2.S442Heat shock and recovery in aged wheat aleurone layers.Livesley, M.A.; Bray, C.M.Wallingford, Oxon, UK : C.A.B. International, c1991-; 1993 Sep.Seed science research v. 3 (3): p. 179-186; 1993 Sep.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Seed aging; Heat stress; Heat shock; Seedgermination; Aleurone layer; Alpha-amylase; Polypeptides; Heat shock proteins;Gene expression; Protein synthesis
129                                                   NAL Call. No.: QK710.P62The heat shock response of pollen and other tissues of maize.Hopf, N.; Plesofsky-Vig, N.; Brambl, R.Dordrecht : Kluwer Academic Publishers; 1992 Jul.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (4): p. 623-630; 1992 Jul.Includes references.
Language:  English
Descriptors: Zea mays; Multigene families; Structural genes; Heat shockproteins; Gene expression; Transcription; Messenger  RNA; Genetic regulation;Heat shock; Introns; Rna editing; Pollen; Pollen germination; Shoots; Tassels
Abstract:  While a heat shock treatment of 40 degrees C or 45 degrees Cinduced the vegetative tissues of maize to produce the typical heat shockproteins (HSPs), germinating maize pollen exposed to the same temperatures didnot synthesize these characteristic HSPs. Comparison of RNA accumulation inshoot and tassel tissue showed that mRNAs for HSP70 and HSP18 increasedseveral-fold, reaching high levels within 1 or 2 hours. At the highertemperature of 45 degrees C these vegetative tissues were blocked in removalof an intron from the HSP70 mRNA precursor, which accumulated to a high levelin tassel tissue. In germinating pollen exposed to heat shock, mRNAs for theseHSPs were induced but accumulated only to low levels. The stressed pollenmaintained high levels of RNA for alpha-tubulin, a representative normaltranscript. It is likely that the defective heat shock response of maizepollen is due to inefficient induction of heat shock gene transcription.
130                                                   NAL Call. No.: QH301.N32Heat-induced "photo"morphogenesis in dark grown plants and circadianrhythmicity: is there a connection?.Kloppstech, K.; Otto, B.; Beator, J.New York, N.Y. : Plenum Press; 1992.NATO ASI series : Series A : Life sciences v. 226: p. 91-99. ill; 1992.  Inthe series analytic: Regulation of chloroplast biogenesis / edited by J.H.Argyroudi-Akoyunoglou. Proceedings of a NATO Advanced Research Workshop, July28-August 3, 1991, Crete, Greece.  Includes references.
Language:  English
Descriptors: Pisum sativum; Chloroplasts; Plant extracts; Seeds; Heat shockproteins; Morphogenesis; Plant development; Seedlings; Zea mays; Circadianrhythm; Greening; Gene expression
131                                                    NAL Call. No.: 450 P699The heat-shock response in rice seedlings: isolation and expression of cDNAsthat encode class I low-molecular-weight heat-shock proteins.Tseng, T.S.; Tzeng, S.S.; Yeh, K.W.; Yeh, C.H.; Chang, F.C.; Chen, Y.M.; Lin,C.Y.Kyoto : Japanese Society of Plant Physiologists; 1993 Jan.Plant and cell physiology v. 34 (1): p. 165-168; 1993 Jan.  Includesreferences.
Language:  English
Descriptors: Oryza sativa; Seedlings; Stress response; Heat stress; Heat shockproteins; Protein synthesis; Genetic regulation; Genetic code; Dna; Clones;Gene expression
Abstract:  Two full-length cDNA clones, pTS1 and pTS3, specific for heat-shockproteins were isolated from a rice cDNA library. Both encoded 16 to 20 kDaclass I heat-shock proteins. Heavy-metal stress, in addition to heat stress,increased the levels of the corresponding mRNAs.
132                                              NAL Call. No.: S494.5.B563C87Hormonal control of gene expression.Jacobsen, J.V.; Gubler, F.Dordrecht : Kluwer Academic Publishers; 1992.Current plant science and biotechnology in agriculture v. 13: p. 116-127;1992.  In the series analytic: Progress in plant growth regulation / edited byC.M. Karssen, L.C. Van Loon and D. Vreugdenhil.  Proceedings of the 14thInternational Conference on Plant Growth Substances held July 21-26, 1991,Amsterdam, Netherlands.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Crops; Gene expression; Messenger  RNA; Plantproteins; Enzymes; Alpha-amylase; Ribosomal  DNA; Ribosomal  RNA; Genes;Genetic regulation; Gibberellic acid; Abscisic acid; Aleurone layer;Protoplasts; Transcription; Promoters; Recombinant  DNA; Reporter genes;Beta-glucuronidase; Histoenzymology; Genetic transformation; Literaturereviews
133                                                    NAL Call. No.: 381 J824Hormone response complex in a novel abscisic acid and cycloheximide-induciblebarley gene.Shen, Q.; Uknes, S.J.; Ho, T.H.D.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993Nov05.The Journal of biological chemistry v. 268 (31): p. 23652-23660; 1993 Nov05.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Plant proteins; Nucleotidesequences; Amino acid sequences; Gene location; Chromosomes; Promoters; Geneexpression; Transcription; Genetic regulation; Abscisic acid; Cycloheximide;Introns; Aleurone layer; Complementary  DNA
Abstract:  The phytohormone, abscisic acid (ABA), plays a variety of rolesduring seed development and in the plant's response to environmental stresses.To study the molecular action of ABA, we have isolated a single copyABA-induced gene, HVA22, which is mapped to barley chromosome 1. The HVA22gene can be induced by either ABA or the protein synthesis inhibitor,cycloheximide, and addition of both inducers to barley aleurone layers has asynergistic effect on the expression of this gene. Sequence comparisonindicates that the HVA22 gene product is highly homologous to the product ofhuman DP1 gene, which is likely to contribute to colorectal tumorigenesis. Thehormonal regulation of HVA22 expression has been studied, and there appear tobe at least three elements, two located in the promoter and one in the firstintron, which are essential for the high level of ABA induction of HVA22expression. Among the promoter elements is a homolog of ABA response element,which has been shown to be important in the expression of other ABA-inducedgenes in plants. We suggest that the barley HVA22 gene product is likely aregulatory protein, and the ABA induction of this gene requires the action ofa complex set of hormone response elements.
134                                                  NAL Call. No.: QK725.P532Identification and molecular characterization of ZAG1, the maize homolog ofthe Arabidopsis floral homeotic gene AGAMOUS.Schmidt, R.J.; Veit, B.; Mandel, M.A.; Mena, M.; Hake, S.; Yanofsky, M.F.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Jul.The Plant cell v. 5 (7): p. 729-737; 1993 Jul.  Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Structural genes; Nucleotidesequences; Amino acid sequences; Plant proteins; Gene expression; MessengerRNA; Gynoecium; Stamens; Maize ears; Multigene families; Gene mapping; Loci;Endosperm; Inflorescences
Abstract:  Recent genetic and molecular studies in Arabidopsis and Antirrhinumsuggest that mechanisms controlling floral development are well conservedamong dicotyledonous species. To assess whether similar mechanisms alsooperate in more distantly related monocotyledonous species, we have begun toclone homologs of Arabidopsis floral genes from maize. Here we report thecharacterization of two genes, designated ZAG1 and ZAG2 (for Zea AG), thatwere cloned from a maize inflorescence cDNA library by low stringencyhybridization with the AGAMOUS (AG) cDNA from Arabidopsis. ZAG1 encodes aputative polypeptide of 286 amino acids having 61% identity with the AGAMOUS(AG) protein. Through a stretch of 56 amino acids, constituting the MADSdomain, the two proteins are identical except for two conservative amino acidsubstitutions. The ZAG2 protein is less similar to AG, with 49% identityoverall and substantially less similarity than ZAG1 outside the well-conservedMADS domain. Like AG, ZAG1 RNA accumulates early in stamen and carpelprimordia. In contrast, ZAG2 expression begins later and is restricted todeveloping carpels. Hybridization to genomic DNA with the full-length ZAG1cDNA under moderately stringent conditions indicated the presence of a largefamily of related genes. Mapping data using maize recombinant inbreds placedZAG1 and ZAG2 near two loci that are known to affect maize flower development,Polytypic ear (Pt) and Tassel seed4 (Ts4), respectively. The ZAG1 protein fromin vitro translations binds to a consensus target site that is recognized bythe AG protein. These data suggest that maize contains a homolog of theArabidopsis floral identity gene AG and that this gene is conserved insequence and function.
135                                                    NAL Call. No.: 450 P692Identification, cDNA cloning, and gene expression of soluble starch synthasein rice (Oryza sativa L.) immature seeds.Baba, T.; Nishihara, M.; Mizuno, K.; Kawasaki, T.; Shimada, H.; Kobayashi, E.;Ohnishi, S.; Tanaka, K.I.; Arai, Y.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Oct.Plant physiology v. 103 (2): p. 565-573; 1993 Oct.  Includes references.
Language:  English
Descriptors: Oryza sativa; Seeds; Plant composition; Isoenzymes; Starch;Purification; Protein composition; Developmental stages; Biosynthesis; Clones;Dna; Genetic code; Gene expression; Seed development
Abstract:  Three forms of soluble starch synthase were resolved byanion-exchange chromatography of soluble extracts from immature rice (Oryzasativa L.) seeds, and each of these forms was further purified by affinitychromatography. The 55-, 57-, and 57-kD proteins in the three preparationswere identified as candidates for soluble starch synthase by western blotanalysis using an antiserum against rice granule-bound starch synthase. It isinteresting that the amino-terminal amino acid sequence was identical amongthe three proteins, except that the 55-kD protein lacked eight amino acids atthe amino terminus. Thus, these three proteins are products of the same gene.The cDNA clones coding for this protein have been isolated from an immaturerice seed library in lambda gt11 using synthetic oligonucleotides as probes.The deduced amino acid sequence of this protein contains alysine-X-glycine-glycine consensus sequence for the ADP-glucose-binding siteof starch and glycogen synthases. Therefore, we conclude that this proteincorresponds to a form of soluble starch synthase in immature rice seeds. Theprecursor of the enzyme contains 626 amino acids, including a 113-residuetransit peptide at the amino terminus. The mature form of soluble starchsynthase shares a significant but low sequence identity with ricegranule-bound starch synthase and Escherichia coli glycogen synthase. However,several regions, including the substrate-binding site, are highly conservedamong these three enzymes. Blot hybridization analysis demonstrates that thegene encoding soluble starch synthase is a single-copy gene in the rice genomeand is expressed in both leaves and immature seeds. These results suggest thatsoluble and granule-bound starch synthases play distinct roles in starchbiosynthesis of plant.
136                                                    NAL Call. No.: 450 P692Identification of embryoid-abundant genes that are temporally expressed duringpollen embryogenesis in wheat anther cultures.Reynolds, T.L.; Kitto, S.L.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Dec.Plant physiology v. 100 (4): p. 1744-1750; 1992 Dec.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Complementary  DNA; Genes; Gene expression;Messenger  RNA; Pollen; Gametogenesis; Anther culture; Embryogenesis
Abstract:  Uninucleate microspores in anther cultures of bread wheat (Triticumaestivum cv Pavon) are capable of producing haploid pollen embryoids andplants. To gain an understanding of this alternate pathway of pollendevelopment, we constructed a cDNA library to young pollen embryoids, isolatedembryoid-specific genes, and analyzed their expression patterns duringmorphogenesis. Two embryoid-abundant clones, pEMB4 and 94, were expressed veryearly during culture, suggesting that these genes are associated withdevelopment and are not simply expressed as a consequence of differentiation.The accumulation patterns of five cloned mRNAs may indicate the activation ofspecific genes associated with the major morphological and physiologicalactivities connected with the differentiation of embryoids in vitro. Theseresults suggest that embryoid-abundant gene expression is causally related tothis pathway because gene expression is spatially and temporally specific andis not observed when microspores are cultured under noninductive conditions.
137                                              NAL Call. No.: QK725.P56 1993In vitro analysis of plant mitochondrial transcription.Stern, D.B.; Rapp, W.D.Weinheim ; New York : VCH; 1993.Plant mitochondria : with emphasis on RNA editing and cytoplasmic malesterility /. p. 181-192; 1993.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Zea mays; Mitochondrial  DNA; Transcription;Gene expression; Literature reviews; Genetic regulation; Promoters
Abstract:  Plant mitochondria possess a sophisticated gene expressionapparatus that includes a variable and fluid genome structure, complextranscription units, extensive post-transcriptional processing including cisand trans-splicing and RNA editing, and its own translational apparatus.Insight into mechanistic aspects of plant mitochondrial gene expression hasbeen limited by the lack of suitable in vitro models. Recently, however, thedevelopment of in vitro RNA editing, tRNA processing and transcription systemshas been reported. This review will consider both the newly developed de novotranscription initiation system and previously developed run-on transcriptionsystems. Together with RNA filter hybridizations, these methods provide a wayto analyze plant mitochondrial transcriptional regulation comprehensively.
138                                                   NAL Call. No.: QH426.D32The independent stage-specific expression of the 18-kDa heat shock proteingenes during microsporogenesis in Zea mays L.Atkinson, B.G.; Raizada, M.; Bouchard, R.A.; Frappier, J.R.H.; Walden, D.B.New York, N.Y. : Wiley-Liss, Inc; 1993.Developmental genetics v. 14 (1): p. 15-26; 1993.  In the special issue: Focuson heat shock genes (part 1) / edited by J.J. Heikkila.  Includes references.
Language:  English
Descriptors: Zea mays; Multigene families; Heat shock proteins; Geneexpression; Gametogenesis; Pollen; Messenger  RNA; Genetic regulation;Nucleotide sequences; Complementary  DNA; Amino acid sequences
Abstract:  The small (18-kDa) heat shock proteins (hsps) of maize are encodedby a complex multigene family. In a previous report, we described the geneticinformation from cDNAs encoding two different members of the family. In thiscommunication, we report the isolation and characterization of cDNA andgenomic clones encoding information for a third member of this hsp family(c/gMHSP18-1). DNA fragments containing nucleotide sequences common to, orspecific for, each of these characterized 18-kDa genes were prepared and usedas probes to assess the expression of these genes during microsporogenesis anddevelopment of the gametophyte in an inbred line of maize (Oh43). Our resultsdemonstrate (1) that mRNA transcripts encoding the 18-kDa hsps are expressedand/or accumulate during microsporogenesis, and (2) that genes encoding two ofthe characterized 18-kDa hsps are expressed and/or accumulate independently,in a stage-specific manner during microsporogenesis. These observations implythat the stage-specific expression of particular 18-kDa hsp genes results fromgene-specific regulation during microsporogenesis and gametophyte developmentrather than from an overall activation of the heat shock or stress response.
139                                                    NAL Call. No.: 442.8 Z8The influence of the rye genome on expression of heat shock proteins intriticale.Somers, D.J.; Gustafson, J.P.; Filion, W.G.Berlin, W. Ger. : Springer International; 1992.Theoretical and applied genetics v. 83 (8): p. 987-993; 1992.  Includesreferences.
Language:  English
Descriptors: Secale cereale; Triticale; Genome analysis; Genomes; Geneexpression; Heat shock proteins; Heat shock; Addition lines; Seedlings
Abstract:  The heat shock protein profiles from Secale cereale L. cv Imperial,Triticum aestivum L. cv Chinese Spring, S. cereale X T. aestivum amphiploid,and the seven disomic S. cereale addition lines to T. aestivum were used tocompare the wheat, rye, and triticale Heat Shock Protein profiles and to studythe influence of the rye genome on heat shock protein expression in triticale.Three-day-old seedlings were heat shocked for 2 h at 40 degrees C in thepresence of 35S-methionine, and polypeptides from root tissues were subjectedto one- or two-dimensional gel electrophoresis. The wheat and rye heat shockprotein profiles each consisted of > 150 heat shock proteins, of which 94 weresufficiently reproducible to construct a standard map. There were 11 uniquerye heat shock proteins compared to 22 unique wheat heat shock proteins. Thetriticale heat shock protein profile resembled the rye parent more than thewheat parent. There were 22 heat shock proteins expressed uniquely by wheatthat were not expressed in triticale. Rye chromosomes 1 and 3 exhibited asubstantial repressive influence on the expression of 95% of the unique wheatheat shock proteins in triticale, while rye chromosome 4 appeared to have theleast repressive influence on expression of the unique wheat heat shockproteins in triticale.
140                                                    NAL Call. No.: QH442.B5Insect resistant rice generated by introduction of a modified delta-endotoxingene of Bacillus thuringiensis.Fujimoto, H.; Itoh, K.; Yamamoto, M.; Kyozuka, J.; Shimamoto, K.New York, N.Y. : Nature Publishing,; 1993 Oct.Bio/technology v. 11 (10): p. 1151-1155; 1993 Oct.  Includes references.
Language:  English
Descriptors: Oryza sativa; Transgenic plants; Gene transfer; Genetictransformation; Bacillus thuringiensis; Structural genes; Bacterial toxins;Endotoxins; Gene expression; Genetic resistance; Pest resistance; Chilosuppressalis; Cnaphalocrocis medinalis; Messenger  RNA; Inheritance
141                                                  NAL Call. No.: QD341.A2N8Insertion of non-intron sequence into maize introns interferes with splicing.Luehrsen, K.R.; Walbot, V.Oxford : IRL Press; 1992 Oct11.Nucleic acids research v. 20 (19): p. 5181-5187; 1992 Oct11.  Includesreferences.
Language:  English
Descriptors: Zea mays; Transposable elements; Introns; Insertionalmutagenesis; Alternative splicing; Rna editing; Alcohol dehydrogenase; Actin;Structural genes; Gene expression; Reporter genes; Luciferase; Messenger  RNA
Abstract:  Transposable element (TE) insertion into or near plant introns cancause intron skipping and alternative splicing events, resulting in reducedexpression. To explore the impact of inserted sequences on splicing, we addednon-intron sequence to two maize introns and tested these chimeric introns ina maize transient expression assay. Non-intron sequence inserted into Adh1-Sintron 1 and actin intron 3 decreased expression from the luciferase reportergene; the insertion sites tested were not in intron regions thought to beessential for splicing. Alternatively spliced mRNAs were not observed intranscripts derived from the insertion variants. In contrast, addition of aninternal segment of an intron to Adh1-S intron 1 resulted in normal splicesite selection and efficient processing. Because the normal intron sequence(including the conserved splice junctions) was retained in all constructs, wehypothesize that added non-intron sequence can interfere with intronrecognition and/or splicing.
142                                                    NAL Call. No.: 386 D282Intron splicing and intron-mediated enhanced expression in monocots.Sinibaldi, R.M.; Mettler, I.J.San Diego, Calif. : Academic Press; 1992.Progress in nucleic acid research and molecular biology v. 42: p. 229-257;1992.  Literature review.  Includes references.
Language:  English
Descriptors: Zea mays; Introns; Gene expression; Genetic regulation; Rna;Monocotyledons; Literature reviews
143                                                   NAL Call. No.: QK710.P62Iron induces ferritin synthesis in maize plantlets.Lobreaux, S.; Massenet, O.; Briat, J.F.Dordrecht : Kluwer Academic Publishers; 1992 Jul.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (4): p. 563-575; 1992 Jul.Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Dna; Ferritin; Messenger  RNA; Geneexpression; Genetic regulation; Iron; Nutrient availability; Roots; Leaves;Nucleotide sequences; Amino acid sequences; Hydroponics; Nutrient deficiencies
Abstract:  The iron-storage protein ferritin has been purified to homogeneityfrom maize seeds, allowing to determine the sequence of the first 29NH2-terminal amino acids of its subunit and to raise specific rabbitpolyclonal antibodies. Addition of 500 micromolar Fe-EDTA/75 micromolarFe-citrate to hydroponic culture solutions of maize plantlets, previouslystarved for iron, led to a significant increase of the iron concentration ofroots and leaves, albeit root iron was mainly found associated with theapoplast. Immunodetection of ferritin by western blots indicated that thisiron treatment induced ferritin protein accumulation in roots and leaves overa period of 3 days. In order to investigate this induction at the ferritinmRNA level, various ferritin cDNA clones were isolated from a cDNA libraryprepared from poly(A)+ mRNA isolated from roots 48 h after iron treatment.These cDNAs were classified into two groups called FM1 and FM2. Upstream ofthe sequence encoding the mature ferritin subunit, both of these cDNAscontained an in-frame coding sequence with the characteristics of a transitpeptide for plastid targeting. Two members of the FM1 subfamily, both partialat their 5' extremity, were characterized. They are identical, except in their3' untranslated region: FM1A extends 162 nucleotides beyond the 3' terminus ofFM1B. These two mRNAs could arise from the use of two differentpolyadenylation signals. FM2 is 96% identical to FM1 and contains 45nucleotides of 5' untranslated region. Northern analyses of root and leafRNAs, at different times after iron treatment, revealed ferritin mRNAaccumulation in response to iron. Ferritin mRNA accumulation was transient andparticularly abundant in leaves, reaching a maximum at 24 h. The level offerritin mRNA in roots was affected to a lesser extent than in leaves.
144                                                   NAL Call. No.: QK710.P62Isolation and analysis of a cDNA clone encoding the small subunit ofADP-glucose pyrophosphorylase from wheat.Ainsworth, C.; Tarvis, M.; Clark, J.Dordrecht : Kluwer Academic Publishers; 1993 Oct.Plant molecular biology v. 23 (1): p. 23-33; 1993 Oct.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Complementary  DNA; Kinases; Nucleotidesequences; Amino acid sequences; Gene location; Chromosomes; Gene expression;Messenger  RNA; Leaves; Roots; Seeds; Seed development
Abstract:  A full-length cDNA clone from hexaploid bread wheat, encoding thesmall subunit of ADP-glucose pyrophosphorylase, has been isolated from anendosperm cDNA library. The cDNA insert has an open reading frame whichencodes a protein of 473 amino acids (52.1 kDa). The presence of achloroplast/amyloplast transit peptide of 22 amino acids is proposed. Thededuced amino acid sequence exhibits a high degree of homology with the smallsubunit ADP-glucose pyrophosphorylase proteins from rice (with 90% ofidentical amino acids) and potato (with 86% of identical amino acids) andcontains conserved sequence elements which are thought to represent thesubstrate binding and allosteric activator sites. The genes are organised assingle-copy loci on chromosomes 7A, 7B and 7D in the wheat genome and arehighly expressed during grain development. Homologous transcripts areexpressed in leaves and roots.
145                                                   NAL Call. No.: QK710.P62Isolation and characterization of a cDNA clone encoding the TATA box-bindingprotein (TFIID) from wheat.Kawata, T.; Minami, M.; Tamura, T.; Sumita, K.; Iwabuchi, M.Dordrecht : Kluwer Academic Publishers; 1992 Aug.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (5): p. 867-872; 1992 Aug.Includes references.
Language:  English
Descriptors: Triticum aestivum; Dna; Structural genes; Dna binding proteins;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Seed germination; Seedling growth; Binding site; Cauliflower mosaiccaulimovirus; Histones; Adenoviridae; Promoters
Abstract:  We isolated a complementary DNA (cDNA) encoding the TATA-bindingfactor 'TFIID' from a wheat seedling cDNA library. The wheat TFIID transcriptof 1.2 kb poly(A)+ RNA was expressed at a low level early in germination, butgradually increased as the seedlings developed. In vitro binding experimentsshowed that the bacterially expressed wheat TFIID protein could specificallybind to the TATA boxes of the cauliflower mosaic virus (CaMV) 35S, wheathistone H3 and adenovirus major late genes with different affinity. Acomparison with Arabidopsis TFIID showed the presence of a plant-specificregion consisting of 13 amino acids at the divergent amino terminus and aconserved region (182 amino acids) at the carboxy terminus longer than thatobserved in yeasts (180 amino acids) and animals (181 amino acids).
146                                                   NAL Call. No.: QK710.P62Isolation and characterization of a rice cDNA clone encoding ATP/ADPtranslocator.Hashimoto, H.; Nishi, R.; Umeda, M.; Uchimiya, H.; Kato, A.Dordrecht : Kluwer Academic Publishers; 1993 Apr.Plant molecular biology v. 22 (1): p. 163-164; 1993 Apr.  Includes references.
Language:  English
Descriptors: Oryza sativa; Complementary  DNA; Binding proteins; Atp; Adp;Mitochondria; Active transport; Nucleotide sequences; Amino acid sequences;Gene expression; Messenger  RNA; Genetic regulation; Salinity; Temperature
Abstract:  We isolated a rice cDNA clone which encodes an open reading frameof 382 amino acids. Its deduced amino acid sequence corresponds to an ATP/ADPtranslocator protein. Its homology with a maize ATP/ADP translocator was 83.9%in nucleotide sequence, and 90.2% of the amino acid level. Expression of thisgene is regulated by such external stresses as salinity and low temperature.
147                                                   NAL Call. No.: QK710.P62Isolation and characterization of a rice cDNA similar to the bovinebrain-specific 14-3-3 protein gene.Kidou, S.I.; Umeda, M.; Kato, A.; Uchimiya, H.Dordrecht : Kluwer Academic Publishers; 1993 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (1): p. 191-194; 1993 Jan.Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Dna; Plant proteins; Nucleotidesequences; Amino acid sequences; Comparisons; Cattle; Brain; Animal proteins;Tyrosine 3-monooxygenase; Enzyme inhibitors; Protein kinase; Gene expression
Abstract:  We isolated a rice cDNA clone which is similar to the bovinebrain-specific 14-3-3 protein (an activator protein of tyrosine and tryptophanhydroxylase involved in the synthetic pathway of monoamine) gene. The deducedamino acid sequence of the cDNA indicated a surprising similarity to a potentinhibitor of Ca2+-phospholipid-dependent protein kinase C. DNA blot analysisindicated that this gene is located at more than a single locus in rice genomeDNA. Expression of this gene is regulated by external stresses.
148                                                    NAL Call. No.: 450 P692Isolation and characterization of cDNAs encoding wheat3-hydroxy-3-methylglutaryl coenzyme A reductase.Aoyagi, K.; Beyou, A.; Moon, K.; Fang, L.; Ulrich, T.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jun.Plant physiology v. 102 (2): p. 623-628; 1993 Jun.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Complementary  DNA; Hydroxymethylglutaryl-coareductase; Multigene families; Nucleotide sequences; Amino acid sequences;Gene expression; Messenger  RNA; Seedlings
Abstract:  The enzyme 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR,EC 1.1.1.34) is a key enzyme in the isoprenoid biosynthetic pathway. We haveisolated partial cDNAs from wheat (Triticum aestivum) using the polymerasechain reaction. Comparison of deduced amino acid sequences of these cDNAsshows that they represent a small family of genes that share a high degree ofsequence homology among themselves as well as among genes from other organismsincluding tomato, Arabidopsis, hamster, human, Drosophila, and yeast. Southernblot analysis reveals the presence of at least four genes. Our resultsconcerning the tissue-specific expression as well as developmental regulationof these HMGR cDNAs highlight the important role of this enzyme in the growthand development of wheat.
149                                                   NAL Call. No.: QK710.P68Isolation and characterization of male flower cDNAs from maize.Wright, S.Y.; Suner, M.M.; Bell, P.J.; Vaudin, M.; Greenland, A.J.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Jan.The plant journal v. 3 (1): p. 41-49. ill; 1993 Jan.  Includes references.
Language:  English
Descriptors: Zea mays; Stamens; Tassels; Clones; Dna libraries; Amino acidsequences; Gene expression; Genetic code; Molecular biology; Nucleotidesequences
150                                                   NAL Call. No.: QK710.P62Isolation and characterization of wheat triticin cDNA revealing a uniquelysine-rich repetitive domain.Singh, N.K.; Donovan, G.R.; Carpenter, H.C.; Skerritt, J.H.; Langridge, P.Dordrecht : Kluwer Academic Publishers; 1993 May.Plant molecular biology v. 22 (2): p. 227-237; 1993 May.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Complementary  DNA; Structural genes;Globulins; Nucleotide sequences; Amino acid sequences; Lysine; Geneexpression; Messenger  RNA; Plant proteins; Seeds; Gene location; Chromosomes;Seed development; Legumin
Abstract:  Polyclonal antibodies were raised against a purified 22 kDatriticin polypeptide (delta) and were used to screen a wheat seed cDNA libraryin the Escherichia coli expression vector lamda gt11. The isolated cDNA cloneswere grouped into three families based on their cross-hybridization reactionsin DNA dot-blot studies. Southern blots of genomic DNAs extracted fromditelocentric and nullisomic-tetrasomic lines of Chinese Spring wheat, probedwith the excised cDNA inserts, indicated that one of the three fami- lies (9clones) had triticin clones. This was finally confirmed by comparing thepredicted amino acid sequences of two of these clones (lamdaTri-l2,lamdaTri-25) with the published tryptic peptide sequences of triticin. TheSouthern blots also showed that there is at least one triticin gene located onthe short arm of each of the homoeologous group I chromosomes (1A, 1B, 1D),although till now no triticin protein product has been identified for thechromosome 1B. The nucleotide sequence of the largest triticin cDNA clonelamdaTri-25 (1567 bp) is presented here, and its predicted amino acid sequenceshows strong homology with the legumin-like proteins of oats (12S globulin),rice (glutelin) and legume seeds. A unique feature of the triticin sequence isthat it contains a lysine-rich repetitive domain, inserted in thehypervariable region of the typical legumin-like genes. Northern blotting oftotal RNA extracted from different stages of the developing wheat seedrevealed that the triticin gene expression is switched on 5-10 days afteranthesis (DAA). There was a steady increase in the level of triticin mRNAuntil 20 DAA, after which it started decreasing. The maximum mRNA accumulationoccurred between 17 and 20 DAA. These observations conform closely with thepublished data on triticin protein accumulation during grain development.
151                                                   NAL Call. No.: QK710.P62Isolation of genes abundantly expressed in rice anthers at the microsporestage.Tsuchiya, T.; Toriyama, K.; Nasrallah, M.E.; Ejiri, S.I.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (6): p. 1189-1193; 1992 Dec.Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Plant proteins; Dna; Nucleotidesequences; Amino acid sequences; Gene expression; Anthers; Pollen
Abstract:  A cDNA library of rice (Oryza sativa L.) has been constructed fromanthers at an early stage of pollen development. By differential screening ofthe library, we have isolated cDNAs of two genes, designated as Osc4 and Osc6,that are abundantly expressed in anthers containing tetrads and uninucleatemicrospores, but are not expressed in leaves or roots. Expression of Osc4 isabsent in mature anthers, while Osc6 is present although the expression decaysduring pollen maturation. A comparison of the nucleotide and deduced aminoacid sequences with those in data banks has not shown significant homology toknown molecules.
152                                                   NAL Call. No.: QK725.P54Isolation of protoplasts from developing barley endosperm: a tool fortransient expression studies.Diaz, I.; Carbonero, P.Berlin, W. Ger. : Springer International; 1992.Plant cell reports v. 10 (12): p. 595-598; 1992.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Endosperm; Protoplasts; Isolation techniques;Gene expression; Transgenics
Abstract:  We have developed a method for the routine isolation of protoplastsfrom developing starchy endosperm of barley (Hordeum vulgare L.).Preplasmolysis of the intact endosperms, a low concentration of hydrolyticenzymes and gravity sedimentation before any centrifugation step, were crucialfactors for a good preparation. Best yields were obtained early afterpollination (8-13 days) or with mutants with low starch content. Transientexpression of a reporter gene under the control of the 35S promoter, afterpolyethyleneglycol transfection of endosperm protoplasts, was of the sameorder as that found in coleoptile derived protoplasts. No significantdifference in expression was found for a given tissue between cv. Bomi and itsmutant Riso 1508.
153                                                   NAL Call. No.: QK710.P62Kinetic induction of oat shoot pulvinus invertase mRNA by gravistimulation andpartial cDNA cloning by the polymerase chain reaction.Wu, L.L.; Song, I.; Karuppiah, N.; Kaufman, P.B.Dordrecht : Kluwer Academic Publishers; 1993 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (6): p. 1175-1179; 1993 Mar.Includes references.
Language:  English
Descriptors: Avena sativa; Gene expression; Transcription; Messenger  RNA;Beta-fructofuranosidase; Pulvini; Gravity; Complementary  DNA; Cloning;Polymerase chain reaction; Nucleotide sequences; Amino acid sequences
Abstract:  An asymmetric (top vs. bottom halves of pulvini) induction ofinvertase mRNA by gravistimulation was analyzed in oat shoot pulvini. TotalRNA and poly(A)+ RNA, isolated from oat pulvini, and two oligonucleotideprimers, corresponding to two conserved amino acid sequences (NDPNG and WECPD)found in invertase from other species, were used for the polymerase chainreaction (PCR). A partial length cDNA (550 bp) was obtained and characterized.A 62% nucleotide sequence homology and 58% deduced amino acid sequencehomology, as compared to beta-fructosidase of carrot cell wall, was found.Northern blot analysis showed that there was an obviously transient inductionof invertase mRNA by gravistimulation in the oat pulvinus system. The mRNA wasrapidly induced to a maximum level at 1 h after gravistimulation treatment andgradually decreased afterwards. The mRNA level in the bottom half of the oatpulvinus was significantly higher than that in the top half of the pulvinustissue. The kinetic induction of invertase mRNA was consistent with thetransient accumulation of invertase activity during the graviresponse of thepulvinus. This indicates that the expression of the invertase gene(s) could beregulated by gravistimulation at the transcriptional level. Southern blotanalysis showed that there were two to three genomic DNA fragments whichhybridized with the partial-length invertase cDNA.
154                                                    NAL Call. No.: TX393.J6Lack of expression of the gamma-45 gliadin gene in a durum wheat genotype.D'Ovidio, R.; Margiotta, B.; Porceddu, E.; Lafiandra, D.London : Academic Press; 1992 Sep.Journal of cereal science v. 16 (2): p. 173-181; 1992 Sep.  Includesreferences.
Language:  English
Descriptors: Triticum durum; Genotypes; Gliadin; Genes; Gene expression
Abstract:  Electrophoretic analysis of seed proteins of a durum wheataccession (MG 41392) showed the absence of gamma-45 gliadin, whereas theomega-gliadin and low molecular weight glutenin subunits usually associatedwith it were present. Polymerase chain reaction (PCR) analysis of genomic DNAfrom this genotype showed the presence of the amplification band typicallyfound in type-45 durum wheat cultivars. This observation was confirmed bySouthern blot analysis, which showed the presence of all gamma-gliadinhybridizing bands usually found in type-45 durum wheat cultivars. The gene forgamma-45 gliadin is present, therefore, but not expressed.
155                                                   NAL Call. No.: QK710.P62A leaf-specific gene stimulated by light during wheat accumulation to lowtemperature.Chauvin, L.P.; Houde, M.; Sarhan, F.Dordrecht : Kluwer Academic Publishers; 1994 Oct.Plant molecular biology v. 23 (2): p. 255-265; 1994 Oct.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Complementary  DNA; Structural genes; Plantproteins; Leaves; Acclimatization; Cold; Nucleotide sequences; Amino acidsequences; Gene expression; Messenger  RNA; Genetic regulation; Light;Multigene families
Abstract:  We report here the identification and characterization of a newleaf-specific light-stimulated gene induced during cold acclimation of wheat.Sequence analysis revealed that the gene encodes a protein of 19 kDa with a pIof 8.8. This is a novel protein with a particular charge distribution. TheC-terminal half has a high propensity to form an alpha-helix and contains allthe acidic amino acids with a net negative charge of -7. On the other hand,the N-terminal half is rich in proline, lysine and arginine with a netpositive charge of +10. These properties are commonly found in severaltranscription factors. The protein is also rich in alanine (21%),ishydrophilic but not boiling soluble in contrast to other alanine-richproteins. During low temperature exposure, the corresponding mRNA accumulatesrapidly in the leaf and remains at a constant level in two tolerant cultivarsused. However, in a less tolerant cultivar, the mRNA level declines despitemaintaining the plants at 4 degrees C. Southern blot analysis indicates thatthe differential expression in the less tolerant genotype is not due to adifferent genomic organization or gene copy number. The mRNA was specificallylocalized in leaf tissues and increased several-fold during the greening at 4degrees C. Furthermore, this gene is not induced in callus cultures acclimatedin the absence or presence of light. This suggests that the full expression ofthis gene is dependent on organized leaf tissue. The expression of this genewas not affected by ABA, drought, heat shock, salinity, wounding oranaerobiosis, demonstrating that it is specifically induced by lowtemperature. The Wcs19 mRNA is preferentially expressed in tolerant Gramineaespecies.
156                                                    NAL Call. No.: 450 P692Light-regulated and cell-specific expression of tomato rbcS-gusA and ricerbcS-gusA fusion genes in transgenic rice.Kyozuka, J.; McElroy, D.; Hayakawa, T.; Xie, Y.; Wu, R.; Shimamoto, K.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul.Plant physiology v. 102(3): p. 991-1000; 1993 Jul.  Includes references.
Language:  English
Descriptors: Lycopersicon esculentum; Oryza sativa; Structural genes;Ribulose-bisphosphate carboxylase; Recombinant  DNA; Reporter genes;Beta-glucuronidase; Transgenic plants; Genetic transformation; Geneexpression; Genetic regulation; Promoters; Light; Mesophyll; Nucleotidesequences; Amino acid sequences; Histoenzymology
Abstract:  A previously isolated rice (Oryza sativa) rbcS gene was furthercharacterized. This analysis revealed specific sequences in the 5' regulatoryregion of the rice rbcS gene that are conserved in rbcS genes of othermonocotyledonous species. In transgenic rice plants, we examined theexpression of the beta-glucuronidase (gusA) reporter gene directed by the2.8-kb promoter region of the rice rbcS gene. To examine differences in theregulation of monocotyledonous and dicotyledonous rbcS promoters, the activityof a tomato rbcS promoter was also investigated in transgenic rice plants. Ourresults indicated that both rice and tomato rbcS promoters confermesophyll-specific expression of the gusA reporter gene in transgenic riceplants and that this expression is induced by light. However, the expressionlevel of the rice rbcS-gusA gene was higher than that of the tomato rbcS-gusAgene, suggesting the presence of quantitative differences in the activity ofthese particular monocotyledonous and dicotyledonous rbcS promoters intransgenic rice. Histochemical analysis of rbcS-gusA gene expression showedthat the observed light induction was only found in mesophyll cells.Furthermore, it was demonstrated that the light regulation of rice rbcS-gusAgene expression was primarily at the level of mRNA accumulation. We show thatthe rice rbcS gene promoter should be useful for expression of agronomicallyimportant genes for genetic engineering of monocotyledonous species.
157                                                   NAL Call. No.: QK710.P62Localisation of cis elements in the promoter of a wheat alpha-Amy2 gene.Huttly, A.K.; Phillips, A.L.; Tregear, J.W.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 903-911; 1992 Sep.Includes references.
Language:  English
Descriptors: Triticum aestivum; Avena sativa; Cauliflower mosaic caulimovirus;Promoters; Controlling elements; Alpha-amylase; Structural genes; Inducedmutations; Deletions; Recombinant  DNA; Gene expression; Reporter genes;Beta-glucuronidase; Transcription; Genetic regulation; Gibberellins; Aleuronecells; Protoplasts; Genetic transformation
Abstract:  A functional analysis of the promoter from the wheat alpha-amylasegene alpha-Amy2/54 is described. Mutant alpha-Amy2/54 promoters containingreplacements or deletions were constructed and their ability to directexpression of the reporter gene beta-glucuronidase (GUS) ingibberellin-responsive oat aleurone protoplasts analysed. Chimaeric promotersusing regions of the cauliflower mosaic virus (CaMV) 35S and alpha-Amy2/54promoters were also analysed. The results suggest that at least three regionswithin the alpha-Amy2/54 promoter contain cis elements that are necessary forhigh-level gibberellin-regulated transcription. Fusion of 1.8 kb of promotersequence upstream from -117 bp to a minimal (-55 CaMV 35S) promoter gave riseto hormone-independent expression implying that the region 3' to -117 bpcontains an element which represses transcription in the absence ofgibberellin or presence of abscisic acid.
158                                                  NAL Call. No.: QK725.P532Maize anthocyanin regulatory gene pl is a duplicate of c1 that functions inthe plant.Cone, K.C.; Cocciolone, S.M.; Burr, F.A.; Burr, B.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Dec.The Plant cell v. 5 (12): p. 1795-1805; 1993 Dec.  Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Complementary  DNA; Alleles; Dnabinding proteins; Molecular mapping; Restriction fragment length polymorphism;Restriction mapping; Genetic regulation; Anthocyanins; Biosynthesis;Pigmentation; Aleurone layer; Transcription; Gene expression; Messenger  RNA;Nucleotide sequences; Amino acid sequences; Chromosome maps
Abstract:  Genetic studies in maize have identified several regulatory genesthat control the tissue-specific synthesis of purple anthocyanin pigments inthe plant. c1 regulates pigmentation in the aleurone layer of the kernel,whereas pigmentation in the vegetative and floral tissues of the plant bodydepends on pl. c1 encodes a protein with the structural features of eukaryotictranscription factors and functions to control the accumulation of transcriptsfor the anthocyanin biosynthetic genes. Previous genetic and molecularobservations have prompted the hypothesis that c1 and pl are functionallyduplicate, in that they control the same set of anthocyanin structural genesbut in distinct parts of the plant. Here, we show that this proposedfunctional similarity is reflected by DNA sequence homology between c1 and plUsing a c1 DNA fragment as a hybridization probe, genomic and cDNA clones forpl were isolated. Comparison of pl and c1 cDNA sequences revealed that thegenes encode proteins with 90% or more amino acid identity in the amino- andcarboxyterminal domains that are known to be important for the regulatoryfunction of the C1 protein. Consistent with the idea that the pi gene productalso acts as a transcriptional activator is our finding that a functional plallele is required for the transcription of at least three structural genes inthe anthocyanin biosynthetic pathway.
159                                                  NAL Call. No.: QK725.P532The maize auxotrophic mutant orange pericarp is defective in duplicate genesfor tryptophan synthase beta.Wright, A.D.; Moehlenkamp, C.A.; Perrot, G.H.; Neuffer, M.G.; Cone, K.C.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.The Plant cell v. 4 (6): p. 711-719; 1992 Jun.  Includes references.
Language:  English
Descriptors: Zea mays; Multiple genes; Structural genes; Hydro-lyases;Nucleotide sequences; Amino acid sequences; Gene mapping; Restriction fragmentlength polymorphism; Gene expression; Messenger  RNA; Recessive lethals;Mutants; Mutations; Tryptophan; Amino acid metabolism; Chromosome maps
Abstract:  orange pericarp (orp) is a seedling lethal mutant of maize causedby mutations in the duplicate unlinked recessive loci orp1 and orp2. Mutantseedlings accumulate two tryptophan precursors, anthranilate and indole,suggesting a block in tryptophan biosynthesis. Results from feeding studiesand enzyme assays indicate that the orp mutant is defective in tryptophansynthase beta activity. Thus, orp is one of only a few amino acid auxotrophicmutants to be characterized in plants. Two genes encoding tryptophan synthasebeta were isolated from maize and sequenced. Both genes encode polypeptideswith high homology to tryptophan synthase beta enzymes from other organisms.The cloned genes were mapped by restriction fragment length polymorphismanalysis to approximately the same chromosomal locations as the geneticallymapped factors orp1 and orp2. RNA analysis indicates that both genes areexpressed in all tissues examined from normal plants. Together, thebiochemical, genetic, and molecular data verify the identity of orp1 and orp2as duplicate structural genes for the beta subunit of tryptophan synthase.
160                                                   NAL Call. No.: 442.8 G28Maize bronze 1:dSpm insertion mutations that are not fully suppressed by anactive Spm.Bunkers, G.; Nelson, O.E. Jr; Raboy, V.Baltimore, Md. : Genetics Society of America; 1993 Aug.Genetics v. 134 (4): p. 1211-1220; 1993 Aug.  Includes references.
Language:  English
Descriptors: Zea mays; Transposable elements; Insertional mutagenesis;Structural genes; Induced mutations; Loci; Repetitive  DNA; Binding site; Dnabinding proteins; Alleles; Genetic regulation; Gene expression; Deletions;Gene interaction
Abstract:  The Suppressor-mutator (Spm) family of maize transposable elementsconsists of autonomous Spm elements and nonautonomous defective Spm (dSpm)elements. One characteristic of this family is that the insertion of dSpmelements into a structural gene often permits some level of structural geneexpression in the absence of Spm activity, and this structural gene expressionis suppressed in trans by Spm activity. The Spm's subterminal repetitiveregions (SRRs) contain several iterations of a 12-bp repeat motif. It had beenproposed that binding of an Spm-encoded protein to these repeat motifs blocksstructural gene transcriptional readthrough, thus suppressing gene expression.The bz-m13 allele of the bronze 1 locus contains a 2.24-kb dSpm insertion inthe second exon of a Bz allele. In the absence of Spm activity, bz-m13displays substantial Bz expression, and this expression is fully suppressed bySpm. Four intra-dSpm deletion derivatives are described in which this Bzexpression is only partially suppressed by Spm. Each of these derivativesretains at least 12 SRR repeat motifs. Thus the presence of these repeatmotifs is not sufficient to guarantee complete suppression by Spm. Some otherproperty such as secondary structure or element size must play a role.
161                                                    NAL Call. No.: 450 P692A maize cDNA encoding a type II chlorophyll a/b-binding protein of photosystemII.Viret, J.F.; Schantz, M.L.; Schantz, R.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug.Plant physiology v. 102 (4): p. 1361-1362; 1993 Aug.  Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Chlorophyll a/b binding protein;Nucleotide sequences; Amino acid sequences; Photosystem ii; Apoproteins; Lightharvesting complexes; Messenger  RNA; Gene expression; Genetic regulation;Light; Greening
162                                                  NAL Call. No.: QK725.P532Maize floral development: new genes and old mutants.Veit, B.; Schmidt, R.J.; Hake, S.; Yanofsky, M.F.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Oct.The Plant cell v. 5 (10): p. 1205-1215; 1993 Oct.  In the special issue:Special review issue on plant reproduction.  Includes references.
Language:  English
Descriptors: Zea mays; Genes; Gene expression; Inflorescences; Celldifferentiation; Flowering; Mutants; Organogenesis; Gene interaction
163                                                    NAL Call. No.: 500 N21PMaize mitochondrial manganese superoxide dismutases are encoded by adifferently expressed multigene family.Zhu, D.; Scandalios, J.G.Washington, D.C. : National Academy of Sciences,; 1993 Oct15.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (20): p. 9310-9314; 1993 Oct15.  Includes references.
Language:  English
Descriptors: Zea mays; Amino acid sequences; Clones; Dna; Gene expression;Genetic code; Nucleotide sequences; Superoxide dismutase; Transcription
Abstract:  We have isolated maize cDNAs encoding three manganese-containingsuperoxide dismutases (MnSODs) distinct from the one previously reported.Molecular analyses indicate that multiple MnSOD transcripts are encoded bydifferent, though similar, genes in the maize genome. A single MnSOD gene hasbeen reported in all other organisms examined to date. The deduced amino acidsequences show that these maize MnSOD proteins have a mitochondrial transitpeptide and that the first 9 amino acids (matrix-targeting sequence) in thetransit peptide are conserved. This suggests that all the maize MnSOD proteinsare mitochondria-associated isozymes. RNA blot analysis demonstrated that eachmember of the maize MnSOD multigene family is both spatially anddevelopmentally regulated. One gene, Sod3.3, was predominantly expressed inthe embryo late in embryogenesis. Patterns of increased Mn-SOD transcriptaccumulation are shown to be associated with increased mitochondrial activityduring plant growth and development. The influence of mitochondrial metabolismon the expression of the nuclear MnSOD genes is discussed.
164                                                   NAL Call. No.: QK710.P62Metabolic regulation of alpha-amylase gene expression in transgenic cellcultures of rice (Oryza sativa L.).Huang, N.; Chandler, J.; Thomas, B.R.; Koizumi, N.; Rodriguez, R.L.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 737-747; 1993 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Multigene families; Geneexpression; Transcription; Messenger  RNA; Transgenic plants; Genetictransformation; Recombinant  DNA; Reporter genes; Beta-glucuronidase; Geneticregulation; Sucrose; Cell suspensions
Abstract:  Expression of two genes in the alpha-amylase gene family iscontrolled by metabolic regulation in rice cultured cells. The levels ofRAmy3D and RAmy3E mRNAs in rice cultured cells are inversely related to theconcentration of sugar in the culture medium. Other genes in the ricealpha-amylase gene family have little or no expression in cultured cells;these expression levels are not controlled by metabolic regulation. A RAmy3Dpromoter/GUS gene fusion was metabolically regulated in the transgenic ricecell line 3DG, just as the endogenous RAmy3D gene is regulated. An assay ofGUS enzyme activity in 3DG cells demonstrated that RAmy3D/GUS expression isrepressed when sugar is present in the culture medium and induced when sugaris removed from the medium. The 942 bp fragment of the RAmy3D promoter thatwas linked to the coding region of the GUS reporter gene thus contains all ofthe regulatory sequences necessary for metabolic regulation of the gene.
165                                                   NAL Call. No.: QK710.P68Metabolic regulation of rice alpha-amylase and sucrose synthase genes inplants.Karrer, E.E.; Rodriguez, R.L.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Jul.The plant journal v. 2 (4): p. 517-523. ill; 1992 Jul.  Includes references.
Language:  English
Descriptors: Oryza sativa; Plant embryos; Sucrose synthase; Alpha-amylase;Gene expression; Genetic regulation; Metabolism
166                                                    NAL Call. No.: 381 J824Methyl jasmonate-regulated translation of nuclear-encoded chloroplast proteinsin barley (Hordeum vulgare L. cv. Salome).Reinbothe, S.; Reinbothe, C.; Parthier, B.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993May15.The Journal of biological chemistry v. 268 (14): p. 10606-10611; 1993 May15.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Leaves; Nuclei; Chloroplasts; Plant growthregulators; Jasmonic acid; Derivatives; Esters; Translation; Gene expression;Plastids
Abstract:  The naturally occurring plant growth regulator (-)-jasmonic acidmethyl ester (JaMe) induces the formation of novel abundant proteins inexcised barley leaf segments. Concomitantly, this substance depresses thetranslation of most preexisting ('control') leaf mRNAs, including those fornuclear-encoded chloroplast proteins such as the small subunit ofribulose-1,5-bisphosphate carboxylase/oxygenase (SSU, rbcS gene product) andseveral light harvesting chlorophyll protein complex apoproteins (LHCPs, cabgene products). The changes in protein synthesis observed for SSU and LHCPsdid not correspond to equivalent alterations in the rbcS and cab transcriptlevels. Analysis of polysome-associated in vitro translatable and hybridizablemRNAs, however, demonstrated a restriction of rbcS and cab transcripts tosmaller polysomes in JaMe-exposed leaf tissues, in comparison to water-treatedtissues. Since treatment of JaMe-incubated leaf segments with cycloheximideprior to harvest led to a shift of both transcripts toward larger polysomes, ahormone-induced impairment of chain initiation is assumed to lower translationof SSU and LHCP in situ. In contrast, the mRNA for plastid leucyl-tRNAsynthetase (LRS1, lrs1 gene product) neither changed its abundance nor itsassociation with polysomes in JaMe-treated leaves and was translated into thecorresponding polypeptide. Together, our results highlight a remarkablevariability of nuclear gene expression in response to plant growth regulatorsof the methyl jasmonate type.
167                                          NAL Call. No.: SB123.57.T732 1993Microprojectile bombardment: a method for the production of transgenic cerealcrop plants and the functional analysis of genes.Morrish, F.; Songstad, D.D.; Armstrong, C.L.; Fromm, M.New York : M. Dekker; 1993.Transgenic plants : fundamentals and applications /. p. 133-171; 1993.Includes references.
Language:  English
Descriptors: Grain crops; Gramineae; Genetic transformation; Transgenicplants; Gene transfer; Gene expression; Literature reviews; Genetic vectors;Reporter genes
168                                                   NAL Call. No.: QK710.P62MNF1, a leaf tissue-specific DNA-binding protein of maize, interacts with thecauliflower mosaic virus 35S promoter as well as the C4 photosyntheticphosphoenolpyruvate carboxylase gene promoter.Yanagisawa, S.; Izui, K.Dordrecht : Kluwer Academic Publishers; 1992 Jul.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (4): p. 545-553; 1992 Jul.Includes references.
Language:  English
Descriptors: Zea mays; Cauliflower mosaic caulimovirus; Dna binding proteins;Binding site; Promoters; Phosphoenolpyruvate carboxylase; Nucleotidesequences; Leaves; Gene expression
Abstract:  When gel shift assays were performed with maize nuclear extract anda DNA fragment containing the cauliflower mosaic virus (CaMV) 35S promoter,three DNA-protein complexes were observed. Analyses with nuclear extractsprepared from green leaves, etiolated leaves, stems and roots showed that thecomplexes resulted from the existence of at least two nuclear factors. One ofthem is presumably a constitutive nuclear factor found in all tissues tested,and another is a leaf-specific factor present both in green and etiolatedleaves. This leaf-specific nuclear factor seemed to be identical to MNF1,previously identified as a factor interacting with the promoter of the maizegene for phosphoenolpyruvate carboxylase involved in the C4 photosynthesis.Deletion analysis revealed that MNF1 binds to the sequence from -281 to -235relative to the transcription start site of the CaMV 35S promoter. MNF1-likenuclear protein was also found in tobacco nuclear extracts. The possibilitythat MNF1 participates as a positive trans-acting factor in the expression ofgenes in maize leaves is discussed.
169                                                   NAL Call. No.: QK710.P68Molecular analyses of a barley multigene family homologous to the yeastprotein kinase gene SNF1.Halford, H.G.; Vicente-Carbajosa, J.; Sabelli, P.A.; Shewry, P.R.; Hannappel,U.; Kreis, M.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Sep.The plant journal v. 2 (5): p. 791-797; 1992 Sep.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Protein kinase; Multigenefamilies; Introns; Exons; Nucleotide sequences; Amino acid sequences;Messenger  RNA; Gene expression; Plant; Complementary  DNA
170                                                   NAL Call. No.: QK710.P62Molecular analysis and spatial expression pattern of alow-temperature-specific barley gene, blt101.Goddard, N.J.; Dunn, M.A.; Zhang, L.; White, A.J.; Jack, P.L.; Hughes, M.A.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 871-879; 1993 Nov.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Complementary  DNA; Plantproteins; Nucleotide sequences; Amino acid sequences; Shoots; Meristems; Geneexpression; Messenger  RNA; Cold; Leaves; Roots; Gene location; Chromosomes
Abstract:  A cDNA clone of the previously unreported low-temperature-inducedgene blt101 was isolated after a differential screen of a cDNA libraryprepared from low-temperature (6 degrees C day/2 degrees C night) grown barleyshoot meristems. Southern blot analysis of barley ditelosomic addition lineswas used to assign this single-copy gene to the long arm of chromosome 4.Analysis of steady-state levels of blt101 mRNA showed the induction of thistranscript in shoot meristems upon transfer of barley (cv. Igri) plants fromcontrol (20 degrees C/15 degrees C) to low (6 degrees C/2 degrees C)temperature treatment. Further, the high level of this transcript ismaintained at low temperatures but is reduced on transfer from low to controltemperatures. The gene is not induced by drought or by foliar application ofABA. Analysis of segregating doubled haploid lines shows that there is nospecific association of this gene with either spring/winter growth habit orfrost hardiness. Examination of the spatial expression pattern revealedubiquitous expression of blt101in low-temperature (6 degrees C/2 degrees C)grown barley shoot meristems, mature leaves and roots.
171                                             NAL Call. No.: S494.5.B563B554The molecular analysis of barley resistance to powdery mildew.Scott, K.J.Wallingford, Oxford, UK : CAB International; 1992.Biotechnology in agriculture (5): p. 481-495; 1992.  In the series analytic:Barley : genetics, biochemistry, molecular biology and biotechnology / editedby P.R. Shewry.  Includes references.
Language:  English
Descriptors: Hordeum; Lines; Erysiphe graminis; Mildews; Genetic resistance;Varietal reactions; Host specificity; Genetic regulation; Gene expression;Induction; Messenger  RNA; Genes; Nucleotide sequences; Protein synthesis
172                                                   NAL Call. No.: 442.8 Z34Molecular analysis of the gene encoding a rice starch branching enzyme.Kawasaki, T.; Mizuno, K.; Baba, T.; Shimada, H.Berlin, W. Ger. : Springer International; 1993 Feb.M G G : Molecular and general genetics v. 237 (1/2): p. 10-16; 1993 Feb.Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Hexosyltransferases; Starch;Nucleotide sequences; Promoters; Amino acid sequences; Exons; Introns; Geneexpression; Messenger  RNA; Seed development
Abstract:  The sequence of a rice gene encoding a starch branching enzyme(sbe1) shows extreme divergence from that of the rice gene, that is homologousto bacterial glycogen branching enzyme (sbe2). sbe1 is expressed abundantlyand specifically in developing seeds and maximally in the middle stages ofseed development. This expression pattern completely coincides with that ofthe waxy gene, which encodes a granule-bound starch synthase. Three G-boxmotifs and consensus promoter sequences are present in the 5' flanking regionof sbe1. It encodes a putative transit peptide, which is required fortransport into the amyloplast. A 2.2 kb intron (intron 2) precedes the borderbetween the regions encoding the transit peptide and the mature protein, andcontains a high G/C content with several repeated sequences in its 5' half.Although only a single copy of sbe1 is present in the rice genome, Southernanalysis using intron 2 as a probe indicates the presence of severalhomologous sequences in the rice genome, suggesting that this large intron andalso the transit peptide coding region may be acquired from another portion ofthe genome by duplication and insertion of the sequence into the gene.
173                                                   NAL Call. No.: QK710.P68Molecular analysis of three maize 22 kDa auxin-binding proteingenes--transient promoter expression and regulatory regions.Schwob, E.; Choi, S.Y.; Simmons, C.; Migliaccio, F.; Ilag, L.; Hesse, T.;Palme, K.; Soll, D.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Sep.The Plant journal : for cell and molecular biology v. 4 (3): p. 423-432; 1993Sep.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Amino acid sequences; Auxins; Bindingproteins; Genetic analysis; Genetic code; Genetic regulation; Moleculargenetics; Nucleotide sequences; Promoters; Protoplasts
174                                                   NAL Call. No.: QK710.P68Molecular characterization of cDNA encoding for adenylate kinase of rice(Oryza sativa L.).Kawai, M.; Kidou, S.I.; Kato, A.; Uchimiya, H.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Nov.The plant journal v. 2 (6): p. 845-854; 1992 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Adenylate kinase; Amino acid sequences; Dnalibraries; Enzyme activity; Gene expression; Genetic code; Genetic regulation;Messenger  RNA; Nucleotide sequences; Transcription
175                                                   NAL Call. No.: QK710.P62Molecular characterization of maize extensin expression.Hood, E.E.; Murphy, J.M.; Pendleton, R.C.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 685-695; 1993 Nov.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Multigene families; Structural genes;Plant proteins; Cell wall components; Hydroxyproline; Messenger  RNA;Histochemistry; Seedlings; Pericarp; Tassels
Abstract:  This study concerned the developmental regulation ofwall-localized, hydroxyproline-containing proteins in maize tissues andorgans. Silk and pericarp cell walls contained more peptidyl hydroxyprolinethan did walls of any vegetative tissue, although all tissues and organsaccumulated these proteins as they matured. In many tissues,hydroxyproline-rich proteins are first associated with the wall in a solubleform before being insolubilized through covalent attachment to the matrix.Because hydroxyproline was more soluble earlier than later in development, itappears that insolubilization was occurring in maize tissues and organs aswell. Tissue prints reacted with an anti-extensin antibody gave positiveresults, indicating the presence of a soluble form of this commonhydroxyproline-rich glycoprotein (HRGP). Silk and pericarp cells activelysynthesized this extensin from abundant transcripts. In vegetative tissues,extensin transcripts were somewhat more abundant in seedlings than inpre-anthesis or mature plants, but levels were much lower than in silk andpericarp. Southern blots of maize genomic DNA indicated that these extensintranscripts are encoded by a small multigene family. Potential roles forextensin in reproductive/protective tissues versus the embryo or vegetativetissues are suggested.
176                                                   NAL Call. No.: QK710.P68Molecular characterization of one of the maize polygalacturonase gene familymembers which are expressed during late pollen development.Allen, R.L.; Lonsdale, D.M.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Feb.The plant journal v. 3 (2): p. 261-271; 1993 Feb.  Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Promoters; Polygalacturonase;Nucleotide sequences; Amino acid sequences; Recombinant  DNA; Reporter genes;Beta-glucuronidase; Gene expression; Histoenzymology; Pollen; Anthers;Gametogenesis; Messenger  RNA; Multigene families; Transgenic plants; Genetictransformation; Nicotiana tabacum
177                                                   NAL Call. No.: 442.8 Z34Molecular characterization of rgp2, a gene encoding a small GTP-bindingprotein from rice.Youssefian, S.; Nakamura, M.; Sano, H.Berlin, W. Ger. : Springer International; 1993 Feb.M G G : Molecular and general genetics v. 237 (1/2): p. 187-192; 1993 Feb.Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Multigene families; Complementary DNA; Binding proteins; Guanosine triphosphate; Nucleotide sequences; Aminoacid sequences; Gene expression; Messenger  RNA; Leaves; Stems; Roots;Panicles; Crop growth stage
Abstract:  We previously reported the isolation of rgp1, a gene from rice,which encodes a ras-related GTP-binding protein, and subsequently showed thatthe gene induces specific morphological changes in transgenic tobacco plants.Here, we report the isolation and characterization of an rgp1 homologue, rgp2,from rice. The deduced rgp2 protein sequence shows 53% identity with the ricergp1 protein, but 63% identity with both the marine ray ora3 protein, which isclosely associated with synaptic vesicles of neuronal tissue, and themammalian rab11 protein. Conservation of particular amino acid sequence motifsplaces rgp2 in the rab/ypt subfamily, which has been implicated in vesiculartransport. Northern blot analysis of rgp1 and rgp2 suggests that both genesshow relatively high, but differential, levels of expression in leaves, stemsand panicles, but low levels in roots. In addition, whereas rgp1 shows maximalexpression at a particular stage of plantlet growth, rgp2 is constitutivelyexpressed during the same period. Southern blot analysis suggests that, inaddition to rgp1 and rgp2, several other homologues exist in rice and thesemay constitute a small multigene family.
178                                                    NAL Call. No.: 381 J824Molecular cloning of two DNA-binding proteins of maize that are structurallydifferent but interact with the same sequence motif.Yanagisawa, S.; Izui, K.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993Jul25.The Journal of biological chemistry v. 268 (21): p. 16028-16036; 1993 Jul25.Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Dna binding proteins; Nucleotidesequences; Amino acid sequences; Binding site; Dna; Promoters; Multigenefamilies; Gene expression; Messenger  RNA
Abstract:  Nuclear extracts from maize leaves have been shown previously tocontain a factor, MNF1, that interacts with both the cauliflower mosaic virus35S promoter and the promoter of the maize gene for phosphoenol-pyruvatecarboxylase, which is involved in C4 photosynthesis. We have isolated two cDNAclones encoding proteins (MNB1a and MNB1b), that bind to an MNF1-binding sitein a sequence-specific manner, by screening of a maize cDNA expression librarywith synthetic oligonucleotides. Using various mutated oligonucleotides, weshowed that both proteins recognize an AAGG motif at the MNF1-binding site asimportant bases for binding, as does MNF1 in maize nuclear extracts. However,the binding specificities of MNB1a and MNB1b are similar but not identical tothat of MNF1. The deduced amino acid sequences of these proteins arecompletely different from each other. The basic region of MNB1b exhibitshomology to the high mobility group (HMG) box of the vertebrate HMG1 family,whereas MNB1a exhibits no homology to any known proteins. Southern blotanalysis of genomic DNA revealed that the cDNA for MNB1a is derived from amultigene family whose members have highly homologous N-terminal basic domain,whereas the gene for MNB1b exhibits only limited homology to a few othergenes. These results suggest that the MNF1-binding site on the 35S promoter isa target of multiple DNA-binding proteins.
179                                                   NAL Call. No.: QK710.P68Molecular homology among members of the R gene family in maize.Consonni, G.; Geuna, F.; Gavazzi, G.; Tonelli, C.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Feb.The plant journal v. 3 (2): p. 335-346; 1993 Feb.  Paper presented at the"Symposium on the use of Mutants to Study Plant Metabolism and Development,"Annual Meeting of the Society of Experimental Biology, April, 1992.  Includesreferences.
Language:  English
Descriptors: Zea mays; Multigene families; Structural genes; Dna bindingproteins; Nucleotide sequences; Amino acid sequences; Loci; Messenger  RNA;Molecular conformation; Promoters; Genetic regulation; Gene expression;Anthocyanins; Biosynthesis; Pigmentation
180                                                   NAL Call. No.: 442.8 Z34A molecular marker to select for freezing tolerance in Gramineae.Houde, M.; Dhindsa, R.S.; Sarhan, F.Berlin, W. Ger. : Springer International; 1992 Jul.M G G : Molecular and general genetics v. 234 (1): p. 43-48; 1992 Jul.Includes references.
Language:  English
Descriptors: Triticum aestivum; Gramineae; Structural genes; Plant proteins;Freezing; Cold tolerance; Acclimatization; Antibodies; Immunoblotting; Genetransfer; Gene expression; Escherichia coli; Leaves
Abstract:  We isolated, and expressed in Escherichia coli, a gene (Wcs120)that is strongly induced during cold acclimation of wheat. The gene productwas purified and used to produce antibodies. Immunoblotting experiments withthe anti-WCS120 antibody identified several cold-induced proteins named FTMsfor Freezing Tolerance Markers since they are associated with the developmentof freezing tolerance. This protein family was found to be coordinatelyregulated specifically by low temperature, highly hydrophilic, stable toboiling, and to have a pI above 6.5. The accumulation kinetics during theacclimation period indicated a positive correlation with the capacity of eachgenotype to develop freezing tolerance. Accumulation of the proteins washigher in the freezing-tolerant genotype than in the less tolerant one. Inaddition, their accumulation was more pronounced in the crown and leaf tissuescompared with roots, confirming a relationship to the capacity of thedifferent tissues to develop freezing tolerance. Analysis of different species(eight monocots and four dicots) indicated that this protein family isspecific for freezing-tolerant cereals. The antibody did not cross-react withany of the non-cereal species examined. The anti-FTMs antibody represents apotential tool for breeders to select for freezing tolerance traits in theGramineae.
181                                                    NAL Call. No.: 450 P692An mRNA putatively coding for an O-methyltransferase accumulatespreferentially in maize roots and is located predominantly in the region ofthe endodermis.Held, B.M.; Wang, H.Q.; John, I.; Wurtele, E.S.; Colbert, J.T.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul.Plant physiology v. 102(3): p. 1001-1008; 1993 Jul.  Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Structural genes; Transferases;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Roots; Plant tissues
Abstract:  ZRP4, a 1.4-kb mRNA that preferentially accumulates in roots ofyoung Zea mays L. plants, was identified by isolation of the correspondingcDNA clone. Genomic Southern analysis indicates that the zrp4 gene isrepresented once in the corn genome. The deduced ZRP4 polypeptide of 39,558 Dis rich in leucine, serine, and alanine. Comparison of the deduced ZRP4polypeptide sequence to polypeptide sequences of previously cloned plant andanimal genes indicates that ZRP4 may be an O-methyltransferase. The ZRP4 mRNApreferentially accumulates in young roots and can be detected only at lowlevels in leaf, stem, and other shoot organs. ZRP4 mRNA accumulation isdevelopmentally regulated within the root, with very low levels ofaccumulation in the meristematic region, higher levels in the regions of cellelongation, highest levels in the region of cell maturation, and low levels inthe mature regions of the root. ZRP4 mRNA is predominantly located in theendodermis, with lower levels in the exodermis. An intriguing possibility isthat the ZRP4 mRNA may code for an O-methyltransferase involved in suberinbiosynthesis.
182                                                   NAL Call. No.: QK710.P62An mRNA that specifically accumulates in maize roots delineates a novel subsetof developing cortical cells.John, I.; Wang, H.; Held, B.M.; Wurtele, E.S.; Colbert, J.T.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (5): p. 821-831; 1992 Dec.Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Plant proteins; Messenger  RNA; Aminoacid sequences; Nucleotide sequences; Gene expression; Roots; Cortex; Rootmeristems; Cell differentiation; Dna
Abstract:  A near full-length cDNA clone (pZRP3) corresponding to an mRNA thataccumulates specifically in roots of maize was isolated. The ZRP3 mRNA is ca.600 nucleotides in length. The amino acid sequence of the predictedpolypeptide is rich in leucine (16%), proline (11%), and cysteine (8.5%). Thezrp3 gene appears to be expressed exclusively in roots, whereas otherZrp3-related genes are expressed in additional organs of the maize plant. Insitu hybridization shows that ZRP3 mRNA accumulation is largely confined tothe cells of the cortical ground meristem. Furthermore, accumulation of thismRNA occurs within a distinct subset of cortical cells, the inner three tofour cell layers.
183                                                   NAL Call. No.: 442.8 Z34Multiple pyruvate decarboxylase genes in maize are induced by hypoxia.Peschke, V.M.; Sachs, M.M.Berlin, W. Ger. : Springer International; 1993 Aug.Molecular & general genetics : MGG v. 240 (2): p. 206-212; 1993 Aug.  Includesreferences.
Language:  English
Descriptors: Zea mays; Structural genes; Multigene families; ComplementaryDNA; Pyruvate decarboxylase; Nucleotide sequences; Amino acid sequences; Geneexpression; Genetic regulation; Anaerobiosis; Anaerobic conditions;Restriction fragment length polymorphism; Gene mapping
Abstract:  Two cDNA clones corresponding to anaerobically induced maize mRNAswere found to have homology to a previously identified maize pyruvatedecarboxylase gene. DNA sequencing and RFLP mapping indicate that these cDNAsrepresent two additional maize pdc genes. Each of the clones is approximately85% identical in predicted amino acid sequence to the other two. All threeclones are induced by hypoxic stress, but with different levels and kineticsof induction.
184                                                  NAL Call. No.: QK725.P532Mutations of the 22- and 27-kD zein promoters affect transactivation by theopaque-2 protein.Ueda, T.; Piscataway, NJ; Waverczak, W.; Ward, K.; Sher, N.; Ketudat, M.;Schmidt, R.J.; Messing, J.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.The Plant cell v. 4 (6): p. 701-709; 1992 Jun.  Includes references.
Language:  English
Descriptors: Zea mays; Dna binding proteins; Opaque-2 maize; Loci; Inducedmutations; Promoters; Zein; Multigene families; Gene expression; Geneticregulation; Binding site; Nucleotide sequences; Controlling elements; Targetedmutagenesis
Abstract:  By utilizing a homologous transient expression system, we havedemonstrated that the Opaque-2 (O2) gene product O2 confers positivetrans-regulation on a 22-kD zein promoter. This trans-acting function of theO2 protein is mediated by its sequence-specific binding to a cis element (theO2 target site) present in the 22-kD zein promoter. A multimer of a 32-bppromoter fragment containing this O2 target site confers transactivation byO2. A single nucleotide substitution in the O2 target sequence not onlyabolishes O2 binding in vitro, but also its response to transactivation by O2in vivo. We have also demonstrated that an amino acid domain including thecontiguous basic region and the heptameric leucine repeat is essential for thetrans-acting function of the O2 protein. Similar but not identical O2 targetsequence motifs can be found in the promoters of zein genes of differentmolecular weight classes. Conversion of such a motif in the 27-kD zeinpromoter to an exact O2 target sequence by site-directed mutagenesis wassufficient to increase the binding affinity of the O2 protein in vitro and toconfer transactivation by O2 in vivo.
185                                                   NAL Call. No.: QK710.P68Myb genes from Hordeum vulgare: tissue-specific expression of chimeric Mybpromoter/Gus genes in transgenic tobacco.Wissenbach, M.; Uberlacker, B.; Vogt, F.; Becker, D.; Salamini, F.; Rohde, W.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Sep.The Plant journal : for cell and molecular biology v. 4 (3): p. 411-422; 1993Sep.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Nicotiana; Transgenics; Transcription;Beta-glucuronidase; Dna binding proteins; Enzyme activity; Gene expression;Nucleotide sequences; Promoters
186                                                   NAL Call. No.: QK710.P68The nitrogen response of a barley C-hordein promoter is controlled by positiveand negative regulation of the GCN4 and endosperm box.Muller, M.; Knudsen, S.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Aug.The Plant journal : for cell and molecular biology v. 4 (2): p. 343-355; 1993Aug.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Gene expression; Genetic variation; Endosperm;Hordein; Promoters; Responses; Amino acids; Ammonium nitrate
187                                                   NAL Call. No.: QK710.P68A novel fingerprint method for analyzing the expression of complex multigenefamilies of very low transcript abundance.Bohl, S.; Apel, K.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Jun.The plant journal v. 3 (6): p. 887-893; 1993 Jun.  Includes references.
Language:  English
Descriptors: Hordeum murinum; Multigene families; Structural genes; Plantproteins; Gene expression; Messenger  RNA; Biochemical techniques; Polymerasechain reaction; Complementary  DNA; Restriction fragment length polymorphism
188                                                  NAL Call. No.: QK725.P532A novel light-regulated promoter is conserved in cereal and dicotchloroplasts.Christopher, D.A.; Kim, M.; Mullet, J.E.Rockville, Md. : American Society of Plant Physiologists; 1992 Jul.The Plant cell v. 4 (7): p. 785-798; 1992 Jul.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Triticum aestivum; Oryza sativa; Zea mays;Sorghum bicolor; Nicotiana tabacum; Spinacia oleracea; Pisum sativum;Promoters; Genetic regulation; Light; Gene expression; Messenger  RNA; Plantproteins; Photosystem ii; Binding proteins; Chlorophyll; Heterogeneity;Nucleotide sequences; Chloroplast genetics
Abstract:  The chloroplast psbD-psbC genes encode D2 and cp43, a reactioncenter protein and chlorophyll-binding antenna protein of photosystem II,respectively. We have previously shown that differential accumulation oflight-induced psbD-psbC mRNAs in barley chloroplasts is due to transcriptionfrom a blue light-responsive promoter (LRP). It is hypothesized that thelight-induced mRNAs help to maintain levels of the D2 polypeptide, which isphotodamaged and degraded in illuminated plants. To determine if light-inducedaccumulation of psbD-psbC mRNAs was a conserved phenomenon in chloroplasts,the expression of psbD-psbC operons from five cereals (barley, wheat, rice,maize, and sorghum) and three dicot (tobacco, spinach, and pea) species wasexamined. Cereal and dicot psbD-psbC operons differ due to several DNArearrangements that moved psbK-psbI proximal to psbD-psbC, allowingcotranscription of these genes and production of several unique transcripts incereals. Despite differences in the structure and expression of the cereal anddicot psbD-psbC operons, the accumulation of light-induced psbD-psbC mRNAs wasconserved in all species studied. An unusual feature of the light-inducedmRNAs was the occurrence of 5' end microheterogeneity. The multiple 5' terminiwere mapped to several consecutive nucleotides (8 to 25 bp) within a highlyconserved (61%) DNA region that represents the transcription initiation sitefor the mRNAs in barley and tobacco. The novel LRP differs in sequence fromtypical plastid promoters that have prokaryotic "-10" and "-35" elements andis centered 570 bp (cereals), 900 bp (tobacco, spinach), or 1100 bp (pea)upstream from the psbD translational start codon. We propose thatphysiological and gene regulatory demands of the chloroplast act asconstraints that preserved the linkage of the LRP with psbD despite DNAinversions involving the psbD upstream region.
189                                                    NAL Call. No.: 381 J824A novel lipoxygenase from rice. Primary structure and specific expression uponincompatible infection with rice blast fungus.Peng, Y.L.; Shirano, Y.; Ohta, H.; Hibino, T.; Tanaka, K.; Shibata, D.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1994Feb04.The Journal of biological chemistry v. 269 (5): p. 3755-3761; 1994 Feb04.Includes references.
Language:  English
Descriptors: Oryza sativa; Magnaporthe grisea; Complementary  DNA;Lipoxygenase; Nucleotide sequences; Amino acid sequences; Gene expression;Messenger  RNA; Leaves; Fungal diseases; Defense mechanisms; Enzyme activity
Abstract:  A novel lipoxygenase cDNA (3,007 base pairs) was isolated from riceleaves (Oryza sativa cv. Aichiasahi) which had been infected with anincompatible race of the rice blast fungus, Magnaporthe grisea. A single copyof the gene is present in the rice genome and encodes a protein of 923residues with a molecular weight of 102,714. This gene product shares theleast amino acid sequence homology among plant lipoxygenases identified todate. A novel feature of this gene product is a putative transit peptidesequence at the amino terminus, suggesting the enzyme is localized inchloroplasts. An active lipoxygenase was expressed from the cDNA inEscherichia coli and characterized. The lipoxygenase introduces molecularoxygen exclusively into the C-13 position of linoleic and linolenic acids. Thegene is expressed at high levels 15 h after inoculation with an incompatiblerace of M. grisea, at a low level after inoculation with a compatible race ofthe pathogen, and is not expressed in mock-infected leaves. Gene expressionbegins at the same time that the pathogen begins to penetrate into leaftissue. This novel lipoxygenase gene expression is a part of the earlyresponse of the host to pathogenic attack.
190                                                    NAL Call. No.: 450 P692Nuclear targeting of the maize R protein requires two nuclear localizationsequences.Shieh, M.W.; Wessler, S.R.; Raikhel, N.V.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Feb.Plant physiology v. 101 (2): p. 353-361; 1993 Feb.  Includes references.
Language:  English
Descriptors: Allium cepa; Nuclei; Protein transport; Transgenic plants;Beta-glucuronidase; Genetic regulation; Transcription; Genetic code; Aminoacid sequences; Gene expression; Spatial distribution; Plant anatomy
Abstract:  Previous genetic and structural evidence indicates that the maize Rgene encodes a nuclear transcriptional activating factor. In-frame carboxylandamino-terminal fusions of the R gene to the reporter gene encodingbeta-glucuronidase (GUS) were sufficient to direct GUS to the nucleus of thetransiently transformed onion (Allium cepa) epidermal cells. Further analysisof chimeric constructs containing regions of the R gene fused to the GUS cDNArevealed three specific nuclear localization sequences (NLSs) that werecapable of redirecting the GUS protein to the nucleus. Amino-terminal NLS-A(amino acids 100-109, GDRRAAPARP) contained several arginine residues; asimilar localization signal is found in only a few viral proteins. The medialNLS-M (amino acids 419- 428, MSERKRREKL) is a simian virus 40 large Tantigen-type NLS, and the carboxyl-terminal NLS-C (amino acids 598-610,MISESLRKAIGKR) is a mating type alpha 2 type. NLSs M and C are independentlysufficient to direct the GUS protein to the nucleus when it is fused at theamino terminus of GUS, whereas NLS-A fused to GUS partitioned between thenucleus and cytoplasm. Similar partitioning was observed when localizationsignals NLS-A and NLS-C were independently fused to the carboxy-terminalportion of GUS. A sequential deletion of the localization signals indicatedthat the amino-terminal and carboxyl-terminal fusions of R and GUS wereredirected to the nucleus only when both NLS-A and -M, or NLS-C and -M, werepresent. These results indicate that multiple localization signals arenecessary for nuclear targeting of this protein. The conservation of thelocalization signals within the alleles of R and similar proteins from otherorganisms is also discussed.
191                                              NAL Call. No.: QK725.P56 1993Nuclear-mitochondrial interactions in Triticum and Triticale.Kuck, U.; Mohr, S.; Laser, B.; Schulte-Kappert, E.; Odenbach, W.; Oettler, G.Weinheim ; New York : VCH; 1993.Plant mitochondria : with emphasis on RNA editing and cytoplasmic malesterility /. p. 357-366; 1993.  Includes references.
Language:  English
Descriptors: Triticum; Triticum aestivum; Triticale; Nucleocytoplasmicinteraction; Mitochondrial genetics; Cytoplasmic inheritance; MitochondrialDNA; Gene expression; Amplification; Cytoplasmic male sterility; Plantbreeding
Abstract:  In wheat hybrid breeding, the timopheevi cytoplasm is commonly usedto generate cytoplasmic male sterile lines. A comparative investigation of theorganization and expression of the mitochondrial genome has been performedusing cytoplasmic male sterile (cms) and fertile lines carrying the timopheeviand aestivum cytoplasm, respectively. A major genomic variation has beenobserved in the homologous region of the atp6 and orf25 gene which results indifferent sizes of mRNA transcripts derived from both genes. We conclude fromSouthern hybridization data that a strict maternal inheritance of mtDNA occursin interspecific wheat crosses. In contrast, mtDNA in Triticale, a wheat/ryehybrid, seems to be derived from both parental lines. However, PCRamplification experiments indicate that substoichiometric amounts of mtDNA aremost probably already present in mitochondria from the maternal line. Thus,under the influence of nuclear genes, amplification of specific regions of themitochondrial genome may also occur in Triticale.
192                                                   NAL Call. No.: QK710.P62Nuclease sensitivity and functional analysis of a maize histone H3 genepromoter.Brignon, P.; Lepetit, M.; Gigot, C.; Chaubet, N.Dordrecht : Kluwer Academic Publishers; 1993 Sep.Plant molecular biology v. 22 (6): p. 1007-1015; 1993 Sep.  Includesreferences.
Language:  English
Descriptors: Zea mays; Promoters; Histones; Multigene families; Chromatin;Enzyme activity; Deoxyribonuclease i; Nucleases; Recombinant  DNA; Reportergenes; Beta-glucuronidase; Gene expression; Meristems; Apical meristems;Genetic transformation; Transgenic plants; Nicotiana tabacum
Abstract:  A 1 kb region of a maize H3 histone gene promoter has been analysedat a structural and functional level. Micrococcal nuclease digestion ofisolated nuclei showed that the promoter region is organized into nucleosomesbut a zone extending over approximately one nucleosome (20 to 230 bp upstreamof the TATA box) displays remarkable accessibility to digestion. Three DNaseI-hypersensitive sites were found within this zone at the vicinity ofconsensus sequences, some of which are already known to act as cis elements.This promoter region is able to direct faithful expression of the GUS reportergene in meristematic tissues of transgenic tobacco plants.
193                                                   NAL Call. No.: QK710.P62Nucleotide sequence and expression of two cDNA coding for two histone H2Bvariants of maize.Joanin, P.; Gigot, C.; Philipps, G.Dordrecht : Kluwer Academic Publishers; 1992 Nov.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (4): p. 581-588; 1992 Nov.Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Dna; Histones; Nucleotide sequences;Amino acid sequences; Multigene families; Gene expression; Meristems;Messenger  RNA
Abstract:  The complete amino acid sequences of two variants of histone H2B ofmaize were deduced from the cDNAs isolated from a maize cDNA library. The twoencoded proteins are 150 (H2B(1)) and 149 (H2B(2)) amino acids long and showsthe classical organization of H2B histones. The hydrophobic C-terminal regionis highly conserved as compared to that of the animal counterparts with only21 changes (13 conservative) among the 90 residues. Between the N-terminalpart and the C-terminal region we note the presence of a basic cluster (9residues) characteristic of histones H2B. The N-terminal third is extended ascompared to the animal consensus H2B and has the same size as the H2B histoneof wheat. Up to 9 acidic residues and a five time repeated pentapeptidePA/KXE/KK are present in this region. Southern-blot hybrization showed thatthe H2B histones are encoded by a multigenic family like the other corehistones (H3 and H4) of plants. The general expression pattern of these geneswas significantly different from that of the H3 and H4 genes neither ingerminating seeds nor in different tissues of adult maize.
194                                                  NAL Call. No.: QK725.P532Oapque-2 is a transcriptional activator that recognizes a specific target sitein 22-kD zein genes.Schmidt, R.J.; Ketudat, M.; Aukerman, M.J.; Hoschek, G.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.The Plant cell v. 4 (6): p. 689-700; 1992 Jun.  Includes references.
Language:  English
Descriptors: Zea mays; Dna binding proteins; Opaque-2 maize; Binding site;Nucleotide sequences; Promoters; Zein; Multigene families; Gene expression;Transcription; Loci; Endosperm; Genetic regulation
Abstract:  opaque-2 (o2) is a regulatory locus in maize that plays anessential role in controlling the expression of genes encoding the 22-kD zeinproteins. Through DNase I footprinting and DNA binding analyses, we haveidentified the binding site for the O2 protein (O2) in the promoter of 22-kDzein genes. The sequence in the 22-kD zein gene promoter that is recognized byO2 is similar to the target site recognized by other "basic/leucine zipper"(bZIP) proteins in that it contains an ACGT core that is necessary for DNAbinding. The site is located in the -300 region relative to the translationstart and lies about 20 bp downstream of the highly conserved zein genesequence motif known as the "prolamin box." Employing gel mobility shiftassays, we used O2 antibodies and nuclear extracts from an o2 null mutant todemonstrate that the O2 protein in maize endosperm nuclei recognizes thetarget site in the zein gene promoter. Mobility shift assays using nuclearproteins from an o2 null mutant indicated that other endosperm proteins inaddition to O2 can bind the O2 target site and that O2 may be associated withone of these proteins. We also demonstrated that in yeast cells the O2 proteincan activate expression of a lacZ gene containing a multimer of the O2 targetsequence as part of its promoter, thus confirming its role as atranscriptional activator. A computer-assisted search indicated that the O2target site is not present in the promoters of zein genes other than those ofthe 22-kD class. These data suggest a likely explanation at the molecularlevel for the differential effect of o2 mutations on expression of certainmembers of the zein gene family.
195                                                  NAL Call. No.: QK725.P532Opaque2 modifiers act post-transcriptionally and in a polar manner ongamma-zein gene expression in maize endosperm.Or, E.; Boyer, S.K.; Larkins, B.A.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Nov.The Plant cell v. 5 (11): p. 1599-1609; 1993 Nov.  Includes references.
Language:  English
Descriptors: Zea mays; Opaque-2 maize; Modifiers; Gene interaction; Dnabinding proteins; Genetic regulation; Gene expression; Structural genes; Zein;Endosperm; Messenger  RNA; Transcription; Translation
Abstract:  The opaque2 (o2) modifier genes convert the soft endosperm of an o2mutant to a hard, vitreous phenotype. The primary biochemical changeassociated with the expression of these genes is a two- to threefold increasein synthesis of the 27-kD gamma-zein storage protein. To investigate themechanism of modifier gene activity, we examined the level of gamma-zein mRNAand protein synthesis during the early stages of endosperm development innormal, o2, and modified o2 genotypes. Although the o2 mutation was found toreduce expression of the 27-kD gamma-zein genes, the activity of o2 modifiergenes dramatically increased the level of both gamma-zein protein and mRNAs asearly as 16 days after pollination. At this stage, transcription of gamma-zeingenes is reduced by approximately 50% in both o2 and modified o2 genotypescompared to wild type. Thus, it appearsthat the modifiers regulate gamma-zeinsynthesis through a post-transcriptional mechanism. Analysis of transcriptsfrom the two nearly identical genes (A and B) encoding the 27-kD gamma-zeinprotein showed differences in the mRNA ratios in different genotypes. Inmodified o2 mutants, accumulation of A over B transcript was greatly enhancedduring endosperm development. Somatic recombination at this locus was found toreduce the number of B genes in the endosperm, but this could not account forthe preferential accumulation of the A transcript. Our results suggest that aproduct of the o2 modifier genes increases the translation or stability of theA gene mRNA, leading to enhanced synthesis of 27-kD gamma-zein protein.
196                                                   NAL Call. No.: QK710.P62The origin of lysine-containing proteins in opaque-2 maize endosperm.Habben, J.E.; Kirleis, A.W.; Larkins, B.A.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 825-838; 1993 Nov.  Includes references.
Language:  English
Descriptors: Zea mays; Opaque-2 maize; Messenger  RNA; Complementary  DNA;Plant proteins; Lysine; Endosperm; Zein; Immunoblotting; Gene expression;Structural genes; Dna binding proteins
Abstract:  The reduction of zein synthesis in the maize (Zea mays L.) opaque-2mutant is associated with an increased percentage of lysine in the endospermprotein. When expressed on an endosperm basis, we found that W64A opaque-2contains 490 pg of lysine compared with 350 micrograms in W64A normal.SDS-PAGE analysis of endosperm proteins indicated that several non-zeinproteins are more abundant in the mutant than in normal genotype. To determinethe subcellular origin of these proteins, we separated an endosperm homogenatefrom developing kernels by sucrose density gradient centrifugation and usedmarker enzyme assays and immunoblot analyses to identify cellular components.Amino acid analysis of proteins in the gradient fractions showed that themajority of the lysine occurs in soluble proteins at the top of the gradient.To identify these proteins, we prepared a complex antiserum against the entiresoluble protein fraction and used it to immunoscreen an endosperm cDNAexpression library. Sequence analysis of clones identified mRNAs involved incarbohydrate metabolism, amino acid biosynthesis, and protein synthesis. RNAdot blot hybridization analysis with these clones revealed significantvariation in the levels of transcripts between normal and opaque-2 endosperm,but we identified several mRNAs that are elevated in opaque-2 and that mayencode proteins responsible for the enhanced lysine content.
197                                                   NAL Call. No.: QK710.P62A pathogen-induced gene of barley encodes a HSP90 homologue showing strikingsimilarity to vertebrate forms resident in the endoplasmic reticulum.Walther-Larsen, H.; Brandt, J.; Collinge, D.B.; Thordal-Christensen, H.Dordrecht : Kluwer Academic Publishers; 1993 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (6): p. 1097-1108; 1993 Mar.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Complementary  DNA; Multigene families;Structural genes; Heat shock proteins; Nucleotide sequences; Amino acidsequences; Gene expression; Genetic regulation; Heat shock; Erysiphe graminisf.sp. hordei; Leaves; Messenger  RNA
Abstract:  The full-length nucleotide sequence of a barley (Hordeum vulgareL.) leaf mRNA, found to increase rapidly in amount during infection attemptsby the powdery mildew fungus (Erysiphe graminis DC. ex Merat), is reported.The mRNA encodes a polypeptide of 809 amino acid residues which, by sequencecomparison, was identified as a member of the 90 kDa heat shock protein(HSP90) family. The encoded protein most resembles the endoplasmic reticulum(ER) resident HSP90 protein, the 94 kDa glucose-regulated protein (GRP94) ofvertebrates, as it possesses both the characteristic N-terminal domainincluding a signal peptide sequence and the C-terminal ER retention signal(Lys-Asp-Glu-Leu). A transcript cross-hybridizing at high stringencyaccumulated rapidly in leaves upon heat shock treatment. Genomic DNA blotanalysis indicated the presence of a family of related genes in the barleygenome.
198                                                   NAL Call. No.: QK710.P68A pathogen-induced gene of barley encodes a protein showing high similarity toa protein kinase regulator.Brandt, J.; Thordal-Christensen, H.; Vad, K.; Gregersen, P.L.; Collinge, D.B.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Sep.The plant journal v. 2 (5): p. 815-820; 1992 Sep.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Complementary  DNA; Protein kinase; Nucleotidesequences; Amino acid sequences; Gene expression; Messenger  RNA; Geneticregulation; Infections; Erysiphe graminis f.sp. hordei
199                                                    NAL Call. No.: 450 P693Pattern of expression of meristem-specific cDNA clones of barley (Hordeumvulgare L.).Kohler, S.; Coraggio, I.; Becker, D.; Salamini, F.Secaucus, N.J. : Springer-Verlag; 1992.Planta v. 186 (2): p. 227-235; 1992.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Meristems; Dna; Clones; Gene expression;Hybridization; Transcription; Shoot apices; Plant morphology; Ultrastructure;Nucleotide sequences; Amino acid sequences
Abstract:  Deoxyribonucleic-acid sequences expressed at high levels inmeristematic tissues of barley (Hordeum vulgare L.) have been cloned bydifferential hybridization. Five out of the seven cDNA clones studied showedhomologies to histone genes H2a (two clones), H2b, H3 and H4. Their patternsof expression, as studied by RNA and in-situ hybridization, were typical forgenes transcribed during cell division. A sixth cDNA clone, Sab2, had a 65.7%identity (on a protein basis) to L2-like ribosomal proteins of Escherichiacoli and other lower prokaryotes. In a domain of 50 amino acids, the seventhclone, Sab35, showed 69.0% sequence identity to the ribosomal protein L21 ofRattus norvegicus. The Sab35 mRNA contained in its 5'-untranslated leadersequence small open reading frames, a feature pointing to a possibletranslational control. The Sab35 in-situ hybridization pattern was to acertain degree different from that of the histone-like clone Sab11: itdetected transcripts not only in tissues that are associated with vegetativeand reproductive apices but also in sub-apical regions. The visualization insitu of transcripts coded by Sab11, 35 and 44 is discussed as a possibletechnique for studying differential gene expression in barley meristematictissues.
200                                                   NAL Call. No.: QK710.P62PCR amplification and sequences of cDNA clones for the small and largesubunits of ADP-glucose pyrophosphorylase from barley tissues.Villand, P.; Aalen, R.; Olsen, O.A.; Luthi, E.; Lonneborg, A.; Kleczkowski,L.A.Dordrecht : Kluwer Academic Publishers; 1992 Jun.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (3): p. 381-389; 1992 Jun.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Dna; Structural genes; Nucleotidyltransferases;Polymerase chain reaction; Nucleotide sequences; Endosperm; Roots; Leaves;Restriction mapping; Messenger  RNA; Amino acid sequences; Gene expression;Transcription
Abstract:  Several cDNAs encoding the small and large subunit of ADP-glucosepyrophosphorylase (AGP) were isolated from total RNA of the starchy endosperm,roots and leaves of barley by polymerase chain reaction (PCR). Sets ofdegenerate oligonucleotide primers, based on previously published conservedamino acid sequences of plant AGP, were used for synthesis and amplificationof the cDNAs. For either the endosperm, roots and leaves, the restrictionanalysis of PCR products (ca. 550 nucleotides each) has revealedheterogeneity, suggesting presence of three transcripts for AGP in theendosperm and roots, and up to two AGP transcripts in the leaf tissue. Basedon the derived amino acid sequences, two clones from the endosperm, beps andbepl, were identified as coding for the small and large subunit of AGP,respectively, while a leaf transcript (blpl) encoded the putative largesubunit of AGP. There was about 50% identity between the endosperm clones, andboth of them were about 60% identical to the leaf cDNA. Northern blot analysishas indicated that beps and bepl are expressed in both the endosperm androots, while blpl is detectable only in leaves. Application of the PCRtechnique in studies on gene structure and gene expression of plant AGP isdiscussed.
201                                                   NAL Call. No.: QK710.P62Pea dehydrins: identification, characterisation and expression.Roberton, M.; Chandler, P.M.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 1031-1044; 1992 Sep.Includes references.
Language:  English
Descriptors: Pisum sativum; Structural genes; Dna; Plant proteins; Nucleotidesequences; Amino acid sequences; Water stress; Desiccation; Gene expression;Messenger  RNA; Seedlings; Abscisic acid; Embryogenesis; Cotyledons; Shoots;Roots
Abstract:  An antiserum raised against dehydrin from maize (Zea mays)recognised several polypeptides in extracts of pea (Pisum sativum) cotyledons.A cDNA expression library was prepared from mRNA of developing cotyledons,screened with the antiserum and positive clones were purified andcharacterised. The nucleotide sequence of one such clone, pPsB12, contained anopen reading frame which would encode a polypeptide with regions ofsignificant amino acid sequence similarity to dehydrins from other plantspecies. The deduced amino acid sequence of the pea dehydrin encoded by B12 is197 amino acids in length, has a high glycine content (25.9), lacks tryptophanand is highly hydrophilic. The polypeptide has an estimated molecular mass of20.4 kDa and pI = 6.4. An in vitro synthesised product from the clonecomigrates with one of the in vivo proteins recognised by the antiserum. Acomparison of the pea dehydrin sequence with sequences from other speciesrevealed conserved amino acid regions: an N-terminal DEYGNP and a lysine-richblock (KIKEKLPG), both of which are present in two copies. Unexpectedly, peadehydrin lacks a stretch of serine residues which is conserved in otherdehydrins. B12 mRNA and dehydrin proteins accumulated in dehydration-stressedseedlings, associated with elevated levels of endogenous abscisic acid (ABA).Applied ABA induced expression of dehydrins in unstressed seedlings. Dehydrinexpression was rapidly reversed when seedlings were removed from the stress orfrom treatment with ABA and placed in water. During pea cotyledon development,dehydrin mRNA and proteins accumulated in mid to late embryogenesis. Dehydrinproteins were some of the most actively synthesised at about the time ofmaximum fresh weight and represent about 2% of protein in mature cotyledons.
202                                                   NAL Call. No.: QH301.N32Photoreceptors and their action on chloroplast development photoregulated geneexpression.Richter, G.New York, N.Y. : Plenum Press; 1992.NATO ASI series : Series A : Life sciences v. 226: p. 71-76; 1992.  In theseries analytic: Regulation of chloroplast biogenesis / edited by J.H.Argyroudi-Akoyunoglou. Proceedings of a NATO Advanced Research Workshop, July28-August 3, 1991, Crete, Greece.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Lemna gibba; Chloroplasts; Biologicaldevelopment; Gene expression; Photoreceptors; Phytochrome
203                                                    NAL Call. No.: 450 P692Plastid DNA in developing maize endosperm: Genome structure, methylation, andtranscript accumulation patterns.McCullough, A.J.; Kangasjarvi, J.; Gengenbach, B.G.; Jones, R.J.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Oct.Plant physiology v. 100 (2): p. 958-964; 1992 Oct.  Includes references.
Language:  English
Descriptors: Zea mays; Dna; Plastids; Endosperm; Restriction mapping; Dnamethylation; Gene expression; Messenger  RNA
Abstract:  Amyloplasts in storage organs such as maize (Zea mays L.) endospermare plastid-derived, nonphotosynthetic, starch-accumulating organelles. Thisstudy was initiated to characterize the plastid genome in maize endospermcells containing differentiated amyloplasts and to determine whether plastidgenes are transcribed during the period of amyloplast biogenesis in endospermdevelopment. four cosmid clones representing the total sequence diversity ofthe maize plastid genome were hybridized to restriction digests of totalcellular DNA from isolated 16-day-old endosperms. The hybridization patternsindicated that the plastid DNA present in endosperm tissue wasindistinguishable from that in leaf total DNA. Methylation of maize endospermamyloplast DNA or leaf chloroplast DNA was not detected with themethylation-sensitive enzymes HpaII and EcoRII. Transcripts homologous to the17 specific plastid DNA BamHI fragments tested were detectable in total RNAprepared from 16-day-old endosperm tissue. Compared with leaf transcripts, theabundance of endosperm transcripts was substantially lower for transcriptsdetected by 12 different BamHI fragments and was similar or relatively higherfor some transcripts homologous to five BamHI fragments. Transcriptshomologous to genes for plastid ribosomal small subunit proteins 7 and 12 onfragments 10 and 23 and to an open reading frame on fragment 14 accumulatedprimarily as unprocessed or partially processed species in endosperm RNA. Thedemonstration that maize endosperm cells contain an intact, transcriptionallyactive plastid genome indicates that plastid genes could contribute toamyloplast biogenesis, although no transcripts unique to endosperm wereidentified.
204                                                   NAL Call. No.: QH301.N32Plastid gene expression during chloroplast development by two alternativepathways in barley seedlings.Krupinska, K.; Schmidt, A.; Falk, J.New York, N.Y. : Plenum Press; 1992.NATO ASI series : Series A : Life sciences v. 226: p. 51-56. ill; 1992.  Inthe series analytic: Regulation of chloroplast biogenesis / edited by J.H.Argyroudi-Akoyunoglou. Proceedings of a NATO Advanced Research Workshop, July28-August 3, 1991, Crete, Greece.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Seedlings; Chloroplasts; Biological development;Gene expression; Plastids; Transcription
205                                                    NAL Call. No.: 450 P692Plastid genes encoding the transcription/translation apparatus aredifferentially transcribed early in barley (Hordeum vulgare) chloroplastdevelopment. Evidence for selective stabilization of psbA mRNA.Baumgartner, B.J.; Rapp, J.C.; Mullet, J.E.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Mar.Plant physiology v. 101 (3): p. 781-791; 1993 Mar.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Transcription; Translation; Ribosomal  RNA;Transfer  RNA; Gene expression; Chloroplasts; Chloroplast genetics; MessengerRNA; Structural genes; Rna polymerase; Ribosomes; Proteins; Celldifferentiation; Photosystem ii; Plant proteins
Abstract:  Chloroplast genomes encode rRNAs, tRNAs, and proteins involved intranscription, translation, and photosynthesis. The expression of 15 plastidgenes representing each of these functions was quantitated during chloroplastdevelopment in barley (Hordeum vulgare). The transcription of all plastidgenes increased during the initial phase of chloroplast development and thendeclined during chloroplast maturation. RNAs corresponding to rpoB-rpoC1-rpoC2, which encode subunits of a plastid RNA polymerase, and rpsl6, whichencodes a ribosomal protein, reached maximal abundance early in chloroplastdevelopment prior to genes encoding subunits of the photosynthetic apparatus(rbcL, atpB, psaA, petB). Transcription of rpoB as well as 16S rRNA,trnfM-trnG, and trnk was high early in chloroplast development and declined10-fold relative to rbcL transcription during chloroplast maturation. RNAhybridizing to psbA and psbD, genes encoding reaction center proteins ofphotosystem II, was differentially maintained in mature chloroplasts ofilluminated barley. Differential accumulation of psbD mRNA relative to rbcLmRNA was due to light-stimulated transcription of psbD. In contrast, enhancedlevels of psbA mRNA in mature chloroplasts were due primarily to selectivestabilization of the psbA mRNA. These data document dynamic modulation ofplastid gene transcription and mRNA stability during barley chloroplastdevelopment.
206                                                   NAL Call. No.: 442.8 G28Pl-Bh, an anthocyanin regulatory gene of maize that leads to variegatedpigmentation.Cocciolone, S.M.; Cone, K.C.Baltimore, Md. : Genetics Society of America; 1993 Oct.Genetics v. 135 (2): p. 575-588; 1993 Oct.  Includes references.
Language:  English
Descriptors: Zea mays; Alleles; Dna binding proteins; Structural genes;Nucleotide sequences; Amino acid sequences; Anthocyanins; Biosynthesis;Pigmentation; Variegation; Spatial variation; Plant tissues; Kernels; Dnamethylation; Gene expression; Messenger  RNA; Genetic regulation
Abstract:  Anthocyanins are purple pigments that can be produced in virtuallyall parts of the maize plant. The spatial distribution of anthocyaninsynthesis is dictated by the organ-specific expression of a few regulatorygenes that control the transcription of the structural genes. The regulatorygenes are grouped into families based on functional identity and DNA sequencesimilarity. The C1/Pl gene family consists of C1, which controls pigmentationof the kernel, and Pl, which controls pigmentation of the vegetative andfloral organs. We have determined the relationship of another gene, Blotched(Bh), to the C1 gene family. Bh was originally described as a gene thatconditions blotches of pigmentation in kernels homozygous for recessive c1,suggesting that Bh could functionally replace C1 in the kernel. Our geneticand molecular analyses indicate that Bh is an allele of Pl, that we designatePl-Bh. Pl-Bh differs from wild-type Pl alleles in two respects. In contrast tothe uniform pigmentation observed in plants carrying Pl, the pattern ofpigmentation in plants carrying Pl-Bh is variegated. Pl-Bh leads to variegatedpigmentation in virtually all tissues of the plant, including the kernel, anorgan not pigmented by other Pl alleles. To address the molecular basis forthe unusual pattern of expression of Pl-Bh, we cloned and sequenced the gene.The nucleotide sequence of Pl-Bh showed only a single base-pair differencefrom that of Pl. However, genomic DNA sequences associated with Pl-Bh werefound to be hypermethylated relative to the same sequences around thewild-type Pl allele. The methylation was inversely correlated with Pl mRNAlevels in variegated plant tissues. Thus, we conclude that DNA methylation mayplay a role in regulating Pl-Bh expression.
207                                                   NAL Call. No.: QK710.P68The profilm multigene family of maize, differential expression of threeisoforms.Staiger, C.J.; Goodbody, K.C.; Hussey, P.J.; Valenta, R.; Drobak, B.K.; Lloyd,C.W.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Oct.The Plant journal : for cell and molecular biology v. 4 (4): p. 631-641; 1993Oct.  Includes references.
Language:  English
Descriptors: Zea mays; Amino acid sequences; Binding proteins; Geneexpression; Genetic code; Multigene families; Nucleotide sequences;Polypeptides
208                                                   NAL Call. No.: QK725.P54The promoter of barley trypsin-inhibitor BTI-cMe, discriminates between wheatand barley endosperm protoplasts in transient expression assays.Diaz, I.; Royo, J.; Carbonero, P.Berlin, W. Ger. : Springer International; 1993.Plant cell reports v. 12 (12): p. 698-701; 1993.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Triticum aestivum; Nicotiana tabacum; Endosperm;Protoplasts; Beta-glucuronidase; Enzyme activity; Gene expression; Geneticcode; Promoters; Reporter genes; Transfection; Cauliflower mosaic caulimovirus
Abstract:  Several promoter fragments from the barley gene coding for trypsininhibitor, BTI-CMe, have been fused to the beta-glucuronidase (GUS) reportergene and these chimeric constructs used for transient expression inprotoplasts. Transfection of developing endosperm protoplasts from barley (cvBomi) show a maximum GUS expression of about 50% of that driven by thecauliflower mosaic virus 35S promoter, while in wheat endosperm protoplastsexpression is less than 10%. No significant expression is found in transfectedleaf protoplasts from barley, wheat or tobacco (<2% of the 35S control). Allthe information required for endosperm and barley specificity is presentin the343 bp proximal to the translation initiation site.
209                                                   NAL Call. No.: QK710.P68The promoter of the rice gene GOS2 is active in various different monocottissues and binds rice nuclear factor ASF-1.Pater, B.S. de; Mark, F. van der; Rueb, S.; Katagiri, F.; Chua, N.H.;Schilperoort, R.A.; Hensgens, L.A.M.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Nov.The plant journal v. 2 (6): p. 837-844; 1992 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Amino acid sequences; Dna binding proteins; Geneexpression; Genetic code; Genetic engineering; Histochemistry; Nucleotidesequences; Promoters; Transcription
210                                                   NAL Call. No.: QH506.E46Protein phosphatase activity is required for light-inducible gene expressionin maize.Sheen, J.Oxford, Eng. : IRL Press; 1993 Sep.The EMBO journal v. 12 (9): p. 3497-3505; 1993 Sep.  Includes references.
Language:  English
Descriptors: Zea mays; Phosphoprotein phosphatase; Enzyme activity; Geneticregulation; Gene expression; Promoters; Ribulose-bisphosphate carboxylase;Kinases; Recombinant  DNA; Reporter genes; Chloramphenicol acetyltransferase;Chlorophyll; Biosynthesis; Complementary  DNA; Enzyme inhibitors
Abstract:  Chlorophyll accumulation and photosynthetic gene activation are twohallmarks of greening process in etiolated maize leaves in response to lightsignals. However, very little is known about the relevant signal transductionpathways mediating these essential processes that lead to photosyntheticcompetence. It is shown here that a potent and specific protein phosphatase 1(PP1) and PP2A inhibitor, okadaic acid, efficiently blocks chlorophyllaccumulation induced by light in etiolated maize leaves. In addition, thelight-inducible expression of two photosynthetic fusion genes can bespecifically suppressed by the structurally unrelated PP1 and PP2A inhibitors,okadaic acid and calyculin A, using a sensitive and physiological maizeprotoplast transient assay. The specificity and effective concentration of theinhibitors in vivo and in vitro strongly suggest that PP1 is required fortransmitting light signals. Intriguingly, several partial cDNAs encoding novelas well as conserved PP1 can be identified in maize leaves using thepolymerase chain reaction. Studies of chimeric promoters indicate that PP1activity is essential for the interaction of multiple regulatory elements.Although PP1 and PP2A have been implicated in the suppression of gene activityin yeast and animals, the present data indicate that PP1 appears to beessential for light-dependent gene activation in plants.
211                                                    NAL Call. No.: 450 P692Protein synthesis in maize during anaerobic and heat stress.Russell, D.A.; Sachs, M.M.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.Plant physiology v. 99 (2): p. 615-620; 1992 Jun.  Includes references.
Language:  English
Descriptors: Zea mays; Protein synthesis; Heat stress; Anaerobic conditions;Gene expression; Messenger  RNA; Translation; Heat shock proteins; Alcoholdehydrogenase; Enzyme activity
Abstract:  Protein accumulation and protein synthesis were investigated duringanaerobic stress and heat shock in maize seedlings (Zea mays L.). Antibodiesagainst alcohol dehydrogenase (ADH) and cytosolic glyceraldehyde-3-phosphatedehydrogenase (GAPC) were used to investigate the expression of the genesencoding these proteins during stress treatment. ADH1 protein accumulation isshown to increase about 10-fold in the root after 24 hours of anaerobictreatment. The Gpc gene products are separable into two size classes: the slowmobility GAPC1 and GAPC2 (GAPC1/2), and the faster GAPC3 and GAPC4 (GAPC3/4).The GAPC1/2 antigen did not increase at all, whereas the GAPC3/4 antigenincreased less than fourfold. The proteins synthesized in the root duringaerobic and anaerobic conditions were compared, and GAPC3/4 was identified asan anaerobic polypeptide. In vitro translations were used to estimate thelevels of different mRNAs in roots following anaerobiosis, recovery fromanaerobiosis, and heat shock. This was compared with the in vivo proteinsynthesis rates in roots labeled under identical conditions. In vivo labelingindicates that GAPC and ADH are not heat shock proteins. Although bothGAPC3/4- and ADH1-translatable mRNA levels increase about 10-fold duringanaerobiosis, in vivo labeling of these proteins (relative to total proteinsynthesis) is further enhanced, leading to a selective translation effect forADH1 of threefold, and for GAPC3/4 of sixfold. In contrast, anoxia causes nochange in GAPC1/2-translatable mRNA levels or in vivo labeling. As anadditional comparison, beta-glucosidase mRNA levels are found to be constantduring anoxia, but in vivo synthesis decreases.
212                                                   NAL Call. No.: QK710.P62Proximal promoter region of the wheat histone H3 gene confers S phase-specificgene expression in transformed rice cells.Ohtsubo, N.; Nakayama, T.; Terada, R.; Shimamoto, K.; Iwabuchi, M.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (3): p. 553-565; 1993 Nov.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Oryza sativa; Promoters; Histones; Recombinant DNA; Reporter genes; Beta-glucuronidase; Genetic transformation; Transgenicplants; Mutants; Deletions; Genetic regulation; Gene expression; Celldivision; Relationships; Dna replication; Messenger  RNA; Structural genes
Abstract:  The cis-regulatory elements that confer cell cycle-dependentexpression to the wheat histone H3 gene were investigated in rice cells (Ocstrain) transformed with H3/GUS chimeric genes. 5' deletion mutants of the H3promoter region (from -1711, -908 or -185 to +57 relative to the transcriptionstart site) were joined to the coding sequence of the bacterialbeta-glucuronidase (GUS) gene then introduced stably into rice cells. S1analyses of the RNA from transformed rice cells whose cell cycles had beensynchronized by treatment with aphidicolin showed that the steady-state levelsof the transcripts from chimeric genes were altered with the change in DNAsynthesis and the content of rice H3 mRNA throughout the cell cycle. Eventhough H3 promoter activity decreased as 5' deletion proceeded, transcriptsfrom the chimeric genes showed increases, as much as 10-fold 1 h after releasefrom the aphidicolin block, which were rapidly lost over the next 4 h. Theresults suggest that the 242 bp sequence from -185 to +57, which contains thebasal promoter region, confers the S phase-specific expression of the H3 geneand that the upstream sequence from position -186 is required for the fullactivity of this promoter.
213                                                    NAL Call. No.: 381 J824The PSI-K subunit of photosystem I from barley (Hordeum vulgare L.). Evidencefor a gene duplication of an ancestral PSI-G/K gene.Kjaerulff, S.; Andersen, B.; Nielsen, V.S.; Moller, B.L.; Okkels, J.S.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993Sep05.The Journal of biological chemistry v. 268 (25): p. 18912-18916; 1993 Sep05.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Duplication; ComplementaryDNA; Photosystem i; Light harvesting complexes; Nucleotide sequences; Aminoacid sequences; Gene expression; Messenger  RNA; Genetic regulation; Light
Abstract:  Photosystem I of barley contains a polypeptide with an apparentmolecular mass of 7 kDa when isolated using the detergentn-decyl-beta-D-maltopyranoside. The 7-kDa polypeptide is lost from the PS Icomplex isolated using Triton X-100. The 7-kDa polypeptide and a correspondingfull-length cDNA clone have been isolated. Based on high sequence similarityto an N-terminal sequence of PSI-K from spinach and to the deduced amino acidsequence of Psak from Chlamydomonas reinhardtii the 7-kDa barley polypeptideis identified as PSI-K. The cDNA clone encodes a precursor polypeptide of 131amino acid residues with a calculated molecular mass of 13,726 Da. The transitpeptide shows characteristics of polypeptides imported into the chloroplast.PSI-K has two hydrophobic regions predicted to be membrane-spanningalpha-helices. In vitro expressed orePSI-K polypeptide was imported intointact chloroplasts, whereas an in vitro expressed prePSI-K lacking 7 aminoacid residues (Met-Ala-Ser- Gln-Leu-Ser-Ala) at the N-terminal end of thetransit peptide failed to be imported. The mRNA encoding PSI-K increasesduring illumination. PsaK is located in a single locus in the genome. PSI-Khas significant similarity to PSI-G. When comparing the barley PSI- K andPSI-G with the reported PSI-K sequence from Synechococcus vulcanus, the degreeof similarity is equal, suggesting that an ancestral gene has been duplicatedin a chloroplast progenitor but not in a cyanobacterial.
214                                                    NAL Call. No.: 450 P699Purification, characterization and cDNA cloning of the 200 kDa protein inducedby cold acclimation in wheat.Ouellet, F.; Houde, M.; Sarhan, F.Kyoto : Japanese Society of Plant Physiologists; 1993 Jan.Plant and cell physiology v. 34 (1): p. 59-65; 1993 Jan.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Cold tolerance; Freezing; Acclimatization;Stress response; Protein synthesis; Plant proteins; Purification; Geneticanalysis; Clones; Cultivars; Gene expression; Amino acid sequences; Chemicalcomposition
Abstract:  We have purified to homogeneity the 200 kDa protein inducedspecifically by low temperature in wheat (Triticum aestivum L.). The boilingsolubility of the protein has been used as a main step in the purificationprocedure. Amino acid composition indicates that the 200 kDa has acompositional bias for glycine (11.4%), threonine (13.3%), and alanine(22.0%). Using oligonucleotide probes, we have isolated a clone (pWcs200) froma cold-acclimated winter wheat cDNA library. Northern analysis demonstratedthat the expression of the corresponding gene was specifically upregulated bylow temperature. Southern analysis showed that the gene organization and therelative copy number were identical in two cultivars differing in theircapacity to develop freezing tolerance. Protein sequence and immunologicalanalyses indicate that this protein shares similar features with the 50 kDaprotein induced during cold acclimation of wheat. The two proteins areboiling-soluble, and possess similar repeated elements. These elements may beimportant for the development of freezing tolerance. We have shown that the200 kDa protein is the largest member of a family of immunologically-relatedcold-induced proteins in wheat. Expression of pWcs200 in E. coli yielded aproduct of around 200 kDa, indicating that the clone contains most of thecoding region for this protein.
215                                                    NAL Call. No.: QP501.E8Purification, characterization and gene structure of (1 leads to3)-beta-glucanase isoenzyme GIII from barley (Hordeum vulgare).Wang, J.; Xu, P.; Fincher, G.B.New York, NY : Springer-Verlag New York Inc; 1992 Oct.European journal of biochemistry v. 209 (1): p. 103-109; 1992 Oct.  Includesreferences.
Language:  English
Descriptors: Hordeum vulgare; Seeds; Seedlings; Beta-glucanase; Isoenzymes;Genes; Nucleotide sequences; Amino acid sequences; Gene expression;Purification; Characterization
Abstract:  A new member of the barley (1 leads to 3)-beta-glucanglucanohydrolase family of enzymes has been purified from extracts ofgerminated grain and young seedlings by fractional precipitation with ammoniumsulphate, ion-exchange chromatography, chromatofocussing and gel-filtrationchromatography. The enzyme, which has been designated (1 leads to3)-beta-glucanase isoenzyme GIII, is a basic protein with an apparentmolecular mass of 32000 Da. Oligosaccharide products released by the enzymeduring hydrolysis of the (1 leads to 3)-beta-glucan, laminarin, indicate thatthe enzyme is an endohydrolase. A 2349-bp fragment of barley genomic DNA hasbeen isolated and identified as the gene encoding the (1 leads to3)-beta-glucanase isoenzyme GIII. The open reading frame encoding theisoenzyme is interrupted by a single intron of 180 bp that splits a codon inthe putative signal-peptide region. Northern-blot analyses with gene-specificprobes indicate that the (1 leads to 3)-beta-glucanase isoenzyme GIII mRNAaccumulates in developing leaves; no mRNA transcripts were detected in thealeurone or scutellum of germinated grain, or in mature vegetative tissues.Although plant (1 leads to 3)-beta-glucanases are generally classified as'pathogenesis-related' proteins, the physiological function of the barley (1leads to 3)-beta-glucanase isoenzyme GIII is unclear.
216                                                   NAL Call. No.: QK710.P68Random sequencing of cDNA libraries reveals a variety of expressed genes incultured cells of rice (Oryza sativa L.).Uchimiya, H.; Kidou, S.I.; Shimazaki, T.; Aotsuka, S.; Takamatsu, S.; Nishi,R.; Hashimoto, H.; Matsubayashi, Y.; Kidou, N.; Umeda, M.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Nov.The plant journal v. 2 (6): p. 1005-1009; 1992 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Cell cultures; Dna libraries; Gene expression;Messenger  RNA; Nucleotide sequences; Databases
217                                                   NAL Call. No.: 442.8 Z34Regulated transcription of the maize Bronze-2 promoter in electroporatedprotoplasts requires the C1 and R gene products.Bodeau, J.P.; Walbot, V.Berlin, W. Ger. : Springer International; 1992 Jun.M G G : Molecular and general genetics v. 233 (3): p. 379-387; 1992 Jun.Includes references.
Language:  English
Descriptors: Zea mays; Promoters; Reporter genes; Gene expression; Geneticregulation; Transcription; Messenger  RNA; Dna binding proteins; Genetictransformation; Protoplasts; Electroporation; Structural genes; Controllingelements; Anthocyanins; Biosynthesis
Abstract:  The putative maize transcription factor genes R and C1 are requiredfor expression of reporter genes with promoters from the Bz1 and A1 genes,which encode enzymes required for anthocyanin biosynthesis in maize. Bz2 isanother anthocyanin biosynthetic gene; we show that expression of a reportergene from the Bz2 promoter also requires R and C1 when the fusion construct isintroduced into maize kernels by particle gun bombardment. When electroporatedinto maize protoplasts from a suspension cell line not synthesizinganthocyanins, reporter genes with Bz2, Bz1, and A1 promoters are expressedonly when both R and C1 expression plasmids are co-electroporated.Electroporation of R and C1 expression plasmids also induces the endogenousgenes required for anthocyanin synthesis, resulting in pink protoplasts within24 h. RNase protection analysis demonstrates that accumulation of mRNA fromthe endogenous Bz1 and Bz2 genes absolutely requires introduced R and C1. Intime-course experiments there is a delay of 3-6 h before the Bz2 promoter isactivated, supporting the proposed role for R- and C1-encoded proteins intranscriptional control. An excess of R relative to C1 suppresses expressionof A1, Bz1, and Bz2 promoters, suggesting an interaction between the R and C1proteins.
218                                              NAL Call. No.: S494.5.B563C87The regulation of light and protein synthesis inhibitors on gene expression ofRubisco and Rubisco subunit binding protein.Li, L.R.; Chen, G.Y.; Miao, Y.G.Dordrecht : Kluwer Academic Publishers; 1993.Current plant science and biotechnology in agriculture v. 15: p. 217-220;1993.  In the series analytic: Biotechnology in Agriculture / edited by C.You, Z. Chen, Y. Ding.  Proceedings of the First Asia-Pacific Conference onAgricultural Biotechnology held August 20-24, 1992, Beijing, China.  Includesreferences.
Language:  English
Descriptors: Oryza sativa; Gene expression; Structural genes;Ribulose-bisphosphate carboxylase; Transcription; Genetic regulation; Light;Messenger  RNA; Binding proteins
219                                                   NAL Call. No.: QK710.P62Regulation of the maize HRGP gene expression by ethylene and wounding. mRNAaccumulation and qualitative expression analysis of the promoter bymicroprojectile bombardment.Tagu, D.; Walker, N.; Ruiz-Avila, L.; Burgess, S.; Martinez-Izquierdo, J.A.;Leguay, J.J.; Netter, P.; Puigdomenech, P.Dordrecht : Kluwer Academic Publishers; 1992 Nov.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (3): p. 529-538; 1992 Nov.Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Promoters; Glycoproteins; Plantproteins; Cell wall components; Gene expression; Genetic regulation; Messenger RNA; Ethylene; Abiotic injuries; Genetic transformation; Direct  DNAuptake;Mesocotyls
Abstract:  The expression of the maize gene coding for a hydroxyproline-richglycoprotein (HRGP) has been studied by measuring the mRNA accumulation afterwounding or ethylene treatment. RNA blot and in situ hybridization techniqueshave been used. The temporal and tissue-specific expression has been observed:the cells related to the vascular system show the more intense HRGP mRNAaccumulation. Transcriptional constructions of the maize HRGP promoter havebeen tested on different maize tissues by microbombarding. A 582 bp promoteris able to direct the expression of the gus gene on calli and young leaves.Constructions having shorter promoter sequences lose this ability. The 582 bpconstruction retains the general specificity of expression observed for theHRGP gene.
220                                                     NAL Call. No.: QK1.C83Regulation of wheat histone gene expression.Nakayama, T.; Iwabuchi, M.Boca Raton, Fla. : CRC Press; 1993.Critical reviews in plant sciences v. 12 (1/2): p. 97-110; 1993.  Literaturereview.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Histones; Gene expression; Genetic regulation;Genes; Transcription; Nucleotide sequences; Literature reviews
221                                                     NAL Call. No.: QK1.C83Regulation of wheat histone gene expression.Nakayama, T.; Iwabuchi, M.Boca Raton, Fla. : CRC Press; 1993.Critical reviews in plant sciences v. 12 (1/2): p. 97-110; 1993.  Literaturereview.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Histones; Gene expression; Genetic regulation;Genes; Transcription; Nucleotide sequences; Literature reviews
222                                                   NAL Call. No.: 64.8 C883Regulatory DNA of ribosomal RNA genes and control of nucleolus organizeractivity in wheat.Flavell, R.B.; O'Dell, M.; Sardana, R.; Jackson, S.Madison, Wis. : Crop Science Society of America, 1961-; 1993 Sep.Crop science v. 33 (5): p. 889-894; 1993 Sep.  Paper presented at the "SearsSymposium on Genetic Engin eering in Cereals", April 24, 1992.  Includesreferences.
Language:  English
Descriptors: Triticum aestivum; Nucleolus organizer; Ribosomal  RNA; Geneexpression; Loci; Genetic regulation; Nucleotide sequences; Promoters; Geneticvariation; Models
Abstract:  A molecular genetic analysis of wheat (Triticum aestivum L.)ribosomal RNA (rRNA) gene locus expression is described. Locus activity wasestimated by cytological assays of nucleolus organiser volume. Gene structurewas determined from DNA sequencing and restriction endonuclease mapping ofisolated genes. Relative nucleolus organiser activity is correlated with thenumber of 135 base pair (bp) repeats that lie upstream of the gene promoter. Amodel is proposed in which gene and locus-relative activity is determined bythe ability of the 135 bp and other promoter sequences of the genes in a locusto compete for regulatory proteins in limiting concentration in the nucleus.Active loci are enriched with genes which have unmethylated cytosines atspecific sites in the promoter and the 135 bp repents and in which chromatinstructure is perturbed. It is concluded that the processes that producedifferent numbers of regulatory DNA sequences between rRNA genes areresponsible for the differential expression of nucleolus organisers inhexaploid wheat and in interspecies hybrids.
223                                                   NAL Call. No.: QK710.P68Repression of the high-methionine zein gene in the maize inbred line Mo17.Schickler, H.; Benner, M.S.; Messing, J.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Feb.The plant journal v. 3 (2): p. 221-229; 1993 Feb.  Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Zein; Gene expression; Inbred lines;Messenger  RNA; Amino acids; Protein composition; Loci; Genetic regulation;Seed development
224                                                  NAL Call. No.: QK725.P532A rice cab gene promoter contains separate cis-acting elements that regulateexpression in dicot and monocot plants.Luan, S.; Bogorad, L.Rockville, Md. : American Society of Plant Physiologists; 1992 Aug.The Plant cell v. 4 (8): p. 971-981; 1992 Aug.  Includes references.
Language:  English
Descriptors: Oryza sativa; Nicotiana tabacum; Zea mays; Promoters; Controllingelements; Chlorophyll a/b binding protein; Recombinant  DNA; Reporter genes;Beta-glucuronidase; Genetic transformation; Gene expression; Light; Geneticregulation; Transgenics; Deletions; Repetitive  DNA; Leaves; Agrobacteriumtumefaciens; Direct  DNAuptake; Induced mutations
Abstract:  The major light-harvesting chlorophyll a/b binding proteins of thephotosynthetic apparatus are encoded by families of nuclear cab genes. Theexpression of most cab genes is tissue specific and photoregulated inangiosperms. In transgenic tobacco plants, expression of the reporter genebeta-glucuronidase (GUS) is photoregulated and tissue specific from 5'upstream sequences of the rice cab1R gene; deletion of sequences upstream fromposition -170 with respect to the transcription start site eliminates theenhanced and photoregulated expression in the transgenic plants. Using an insitu transient expression assay, we have determined that the sequence OCT-R,an octamer repeat that lies within the -269 to -170 region of cab1R, isessential for photoregulated expression of the chimeric GUS gene in leaf cellsof maize and rice but is not required for expression in illuminated tobaccoleaves. Conversely, box III - and G-box-like sequences found near OCT-R incab1R are necessary for high-level transient expression of the reporter genein tobacco leaf tissue but are not required for transient expression in maizeor rice leaves.
225                                                   NAL Call. No.: QK710.P68RNA editing in maize chloroplasts is a processing step independent of splicingand cleavage to monocistronic mRNAs.Freyer, R.; Hoch, B.; Neckermann, K.; Maier, R.M.; Kossel, H.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Oct.The Plant journal : for cell and molecular biology v. 4 (4): p. 621-629; 1993Oct.  Includes references.
Language:  English
Descriptors: Zea mays; Amino acid sequences; Chloroplasts; Gene expression;Genetic code; Messenger  RNA; Nucleotide sequences; Rna editing; Transcription
226                                                  NAL Call. No.: QK725.P532Role of the regulatory gene pl in the photocontrol of maize anthocyaninpigmentation.Cone, K.C.; Cocciolone, S.M.; Moehlenkamp, C.A.; Weber, T.; Drummond, B.J.;Tagliani, L.A.; Bowen, B.A.; Perrot, G.H.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Dec.The Plant cell v. 5 (12): p. 1807-1816; 1993 Dec.  Includes references.
Language:  English
Descriptors: Zea mays; Dna binding proteins; Alleles; Dominance; Recessivegenes; Promoters; Genetic regulation; Gene expression; Structural genes;Anthocyanins; Biosynthesis; Pigmentation; Light; Light relations; MessengerRNA; Restriction mapping; Nucleotide sequences; Amino acid sequences
Abstract:  The pl gene encodes a regulatory protein that controls thetranscription of a number of structural genes of the anthocyanin biosyntheticpathway in maize. pl alleles have been classified phenotypically into twocategories: dominant (Pl) alleles lead to intense, light-independentpigmentation in vegetative and floral organs of the plant; recessive "sun-red'alleles (pl) lead to light-dependent red pigmentation in which only tissuesexposed to light become pigmented. Based on these observations, two alternatepathways leading to anthocyanin synthesis in the plant have been proposed: onerequiring light and the other bypassing the light requirement through theaction of Pi. To evaluate this hypothesis, we have analyzed light-independentand light-dependent alleles of pl. Sequence analysis revealed that the twotypes of alleles have very distinct promoters but have the capacity to encodevery similar proteins. The protein encoded by one recessive allele was shownto be functional in transient assays. Measurements of husk mRNA levels byquantitative polymerase chain reaction showed that sun-red pl alleles areexpressed at much lower levels than a Pl allele, but their expression isincreased approximately sixfold by exposure to light. These results lead tothe conclusion that the sun-red pl alleles are not null; instead, theysynthesize functional mRNA and protein. We propose that the light-dependentpigmentation observed in pl plants is the result of a threshold effect inwhich light exposure boosts pl mRNA expression past a crucial level necessaryto generate sufficient PL protein molecules to activate transcription of theanthocyanin structural genes.
227                                                   NAL Call. No.: QK710.P62Sequence analysis of three members of the maize polygalacturonase gene familyexpressed during pollen development.Allen, R.L.; Lonsdale, D.M.Dordrecht : Kluwer Academic Publishers; 1992 Oct.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (2): p. 343-345; 1992 Oct.Includes references.
Language:  English
Descriptors: Zea mays; Multigene families; Structural genes;Polygalacturonase; Nucleotide sequences; Gene expression; Pollen;Gametogenesis; Restriction mapping; Genetic variation
228                                                 NAL Call. No.: SB732.6.M65Sequence and expression of a wheat gene that encodes a novel proteinassociated with pathogen defense.Bull, J.; Mauch, F.; Hertig, C.; Rebmann, G.; Dudler, R.St. Paul, Minn. : APS Press; 1992 Nov.Molecular plant-microbe interactions : MPMI v. 5 (6): p. 516-519; 1992 Nov.Includes references.
Language:  English
Descriptors: Triticum aestivum; Disease resistance; Erysiphe graminis f.sp.tritici; Gene expression; Host parasite relationships; Genes; Erysiphegraminis f.sp. hordei; Nucleotide sequences; Amino acid sequences;Pathogenesis-related proteins
229                                                   NAL Call. No.: QK710.P62Site-specific oligodeoxynucleotide binding to maize Adh1 gene promoterrepresses Adh1-GUS gene expression in vivo.Lu, G.; Feri, R.J.Dordrecht : Kluwer Academic Publishers; 1992 Aug.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (5): p. 715-723; 1992 Aug.Includes references.
Language:  English
Descriptors: Zea mays; Promoters; Alcohol dehydrogenase; Structural genes; Dnaconformation; Nucleotides; Binding site; Genetic regulation; Gene expression;Reporter genes; Beta-glucuronidase; Dna; Nucleotide sequences; Genetictransformation; Controlling elements
Abstract:  There is a 36 bp tract of extreme homopurine/homopyrimidine (PuPy)asymmetry in the maize Adh1 gene promoter (from -44 to -79) that isS1-hypersensitive in plasmids under supercoil tension. Oligodeoxynucleotidescorresponding to the PuPy tract were designed to examine the secondarystructure of the region and address the possible role of the tract in generegulation. On the basis of oligodeoxynucleotide band-shift and DNase Ifootprinting analyses, it was concluded that the homopyrimidineoligodeoxynucleotide can form a triple helix with the duplex PuPy tract invitro. Transient assays in protoplasts, suspension cells, and seedling rootsshow that the homopyrimidine oligodeoxynucleotide is also capable ofrepressing Adh1-GUS gene expression during co-transformation, presumably bythe formation of a triple helix with the PuPy tract in vivo. The complementaryhomopurine oligodeoxynucleotide would not form a triple helix in vitro, norwould it repress Adh1-GUS in vivo. We propose that triple helix formation is apotential regulatory phenomenon in vivo, and that an intraregion triple helixcould occur within the Adh1 promoter via the formation of H-DNA.
230                                                   NAL Call. No.: QK710.P62Sorghum mitochondrial atp6: divergent amino extensions to a conserved corepolypeptide.Mullen, J.A.; Pring, D.R.; Kempken, F.; Ferguson, J.; Chase, C.D.Dordrecht : Kluwer Academic Publishers; 1992 Oct.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (1): p. 71-79; 1992 Oct.  Includesreferences.
Language:  English
Descriptors: Sorghum bicolor; Structural genes; Multiple genes;Adenosinetriphosphatase; Line differences; Mitochondrial  DNA; Mitochondrialgenetics; Nucleotide sequences; Restriction mapping; Cytoplasmic malesterility; Amino acid sequences; Transcription; Messenger  RNA; Geneexpression
Abstract:  Sorghum mitochondrial atp6 occurs as one copy in the line Tx398 andas two copies in IS1112C. In IS1112C a repeated sequence diverged within theatp6 open reading frames. The two open reading frames (1137 bp, atp6-1; 1002bp, atp6-2) share an identical conserved region of 756 bp but are flanked 5'by divergent extensions of 246 (atp6-1) or 381 bp (atp6-2). Tx398 carried onlyatp6-2. The breakpoint of the repeated sequence of the conserved core regioncorresponds to the amino acid sequence Ser-Pro-Leu-Asp, which is the aminoterminus of the proteolytically processed yeast ATP6. The 5' extensions ofatp6-1 and atp6-2 were similar to those of rice and maize, respectively. Eachopen reading is transcribed, however nuclear background influencedtranscriptional patterns of atp6-2 in IS1112C.
231                                                   NAL Call. No.: QH426.D32Spatial regulation in the expression of structural and regulatorystorage-protein genes in Zea mays endosperm.Dolfini, S.F.; Landoni, M.; Tonelli, C.; Bernard, L.; Viotti, A.New York, N.Y. : Wiley-Liss, Inc; 1992.Developmental genetics v. 13 (4): p. 264-276; 1992.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Genetic regulation; Endosperm;Structural genes; Loci; Zein; Multigene families; Glutelins; Messenger  RNA;Spatial distribution; Opaque-2 maize; Modifiers
Abstract:  Endosperm development in maize seed involves the multiplication,enlargement, and differentiation of cells with consequent accumulation ofstorage products. The storage protein genes, encoding zeins, and glutelins(multigene families) are expressed and developmentally regulated by differentloci. Wild-type lines and genotypes carrying mutations at loci affecting zeinsynthesis (o2, o7, fl2, and pro1) were characterized at the molecular leveland investigated by Northern analysis in order to define the expression ofstructural and regulatory genes. In situ hybridization in both wild-type andmutant lines was performed to visualize the spatial distribution oftranscripts representing each gene family, during endosperm development. Thezein and glutelin mRNAs are expressed in all endosperm cells, except for thealeurone layer. However, each mRNA type accumulates at a different level inthe various endosperm regions, thus allowing to recognize specific territoriesof expression for each storage protein mRNA within the tissue. The spatialexpression patterns appear early for each gene type and are maintained duringthe course of endosperm development. Also, the quantitative distribution ofthe some transcripts in endosperm of mutant lines is specific for each mutantand different from that of the wild-type. Furthermore, the amount of the O2transcript, present in the nucleus and cytoplasm of wild-type cells, variessubstantially in the different o2 mutations considered, in one mutant almostexclusively confined within the nucleus. These data suggest a specific controlof the spatial expression of storage protein genes and a heterogeneousmolecular composition of protein bodies throughout the endosperm tissue.
232                                                   NAL Call. No.: QK710.P68Stress induction and developmental regulation of a rice chitinase promoter intransgenic tobacco.Zhu, Q.; Doerner, P.W.; Lamb, C.J.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Feb.The plant journal v. 3 (2): p. 203-212; 1993 Feb.  Includes references.
Language:  English
Descriptors: Oryza sativa; Promoters; Chitinase; Pathogenesis-relatedproteins; Structural genes; Recombinant  DNA; Reporter genes;Beta-glucuronidase; Genetic transformation; Transgenic plants; Nicotianatabacum; Gene expression; Histoenzymology; Abiotic injuries; Geneticregulation; Roots; Stems; Flowers; Cell wall components; Phytophthoramegasperma; Deletions
233                                                   NAL Call. No.: QK710.P62Structure and expression during the germination of rice seeds of the gene fora carboxypeptidase.Washio, K.; Ishikawa, K.Dordrecht : Kluwer Academic Publishers; 1992 Jul.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (4): p. 631-640; 1992 Jul.Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Carboxypeptidases; Dna; Introns;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Seed germination; Aleurone layer; Endosperm; Genetic regulation; Abscisicacid; Gibberellic acid; Restriction mapping
Abstract:  The carboxypeptidase gene from rice and corresponding cDNA cloneswere isolated. The SalI 11.2 kb fragment of DNA cloned from asize-fractionated genome library contained eight introns and an open readingframe that encoded 500 amino acids (Mr 55445). The structure deduced for thecarboxypeptidase from rice was very similar to those of type III serinecarboxypeptidases from barley and wheat. The extent of homology of the aminoacid sequence to that of these carboxypeptidases from barley and wheat was92.3% and 87.2%, respectively. The accumulation of mRNA for the ricecarboxypeptidase was conspicuous in germinating endosperms that containedaleurone layers, but levels were lower in leaves and roots. The abundance ofthe mRNA in endosperms was enhanced by gibberellic acid (GA) and accumulationof the mRNA was inhibited by abscisic acid (ABA). The rice gene forcarboxypeptidase contained some pyrimidine boxes ((C/T)CTTTT(C/T)), in the 5'flanking region, which are a characteristic of a GA-responsive gene.
234                                                   NAL Call. No.: QK710.P62Structure and expression of a barley acidic beta-glucanase gene.Malehorn, D.E.; Scott, K.J.; Shah, D.M.Dordrecht : Kluwer Academic Publishers; 1993 May.Plant molecular biology v. 22 (2): p. 347-360; 1993 May.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Multigene families; Structural genes;Beta-glucanase; Pathogenesis-related proteins; Nucleotide sequences; Aminoacid sequences; Introns; Exons; Gene expression; Messenger  RNA; Roots;Leaves; Genetic regulation; Infections; Erysiphe graminis f.sp. hordei;Mercuric chloride; Restriction mapping
Abstract:  A barley acidic beta-1,3-glucanase gene was recovered from a barleygenomic library by homology with a partial cDNA of barley basicbeta-1,3-glucanase isoenzyme GII. The gene, Abg2, is homologous to the PR2family of pathogenesis-related beta-1,3-glucanase genes. The ABG2 protein has81% amino acid similarity to barley basic beta-1,3-glucanase GII. The ABG2protein is encoded as a preprotein of 336 amino acids including a 28 aminoacid signal peptide. A 299 bp intron occurs within codon 25. The mature ABG2protein has a predicted mass of 32642 Da and a calculated isoelectric point of4.9. The second exon of the Abg2 gene shows a strong preference for G + C inthe third position of degenerate codons. The Abg2 gene was functionallyexpressed in Escherichia coli. Abg2 mRNA is constitutively expressed in barleyroot; leaf expression of Abg2 mRNA is induced by mercuric chloride andinfection by Erysiphe graminis f. sp. hordei. Southern blot analysis indicatesthat Abg2 is a member of a small gene family.
235                                                    NAL Call. No.: 381 J824Structure and expression of the Kas12 gene encoding a beta-ketoacyl-acylcarrier protein synthase I isozyme for barley.Kauppinen, S.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1992Nov25.The Journal of biological chemistry v. 267 (33): p. 23999-24006; 1992 Nov25.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Long-chain-fatty-acid-coa ligase; Isoenzymes;Gene expression; Nucleotide sequences; Amino acid sequences
Abstract:  The beta-ketoacyl-acyl carrier protein (ACP) synthase I in theplant fatty acid synthetase catalyzes the condensations of acetate units to agrowing acyl-ACP leading to the synthesis of palmitoyl-ACP. Barleychloroplasts contain three cerulenin sensitive beta-ketoacyl-ACP synthase Iisoforms, alpha(2), alpha beta, and beta(2). The Kas12 gene encoding thebeta(2) isozyme has been isolated and sequenced. The gene spans 3.8 kilobasesand contains seven exons separated by six intervening sequences varying from75 to 1008 base pairs in length. The mosaic gene structure is differentcompared with that of the beta-ketoacyl synthase in the multifunctional ratand goose fatty acid synthetases. Southern blot analyses of genomic DNA frombarley, wheat, and the barley-wheat chromosome addition lines indicate thatKas12 is a single copy gene located on chromosome 2. Primer extension analysesidentified four transcription start sites located 168-171 nucleotides upstreamfrom the translation initiation codon. The Kas12 promoter lacks anappropriately positioned TATA box and contains a GC-rich region including twoGC elements similar to the Sp1 transcription factor-binding site. In thisregard Kas12 closely resembles a set of ubiquitously expressed eucaryoticgenes. In accord with this deduction, polymerase chain reaction analysisshowed that the Kas12 transcript is present in barley roots, germinatingembryos, developing kernels, and leaves.
236                                                   NAL Call. No.: QK710.P62Structure and expression of the lignin O-methyltransferase gene from Zea maysL.Collazo, P.; Montoliu, L.; Puigdomenech, P.; Rigau, J.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (5): p. 857-867; 1992 Dec.Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Dna; Transferases; Lignin; Nucleotidesequences; Amino acid sequences; Introns; Gene expression; Messenger  RNA;Roots; Enzyme activity
Abstract:  The isolation and characterization of cDNA and homologous genomicclones encoding the lignin O-methyltransferase (OMT) from maize is reported.The cDNA clone has been isolated by differential screening of maize root cDNAlibrary. Southern analysis indicates that a single gene codes for thisprotein. The genomic sequence contains a single 916 bp intron. The deducedprotein sequence from DNA shares significant homology with the recentlyreported lignin-bispecific caffeic acid/5-hydroxyferulic OMTs from alfalfa andaspen. It also shares homology with OMTs from bovine pineal glands and apurple non-sulfur photosynthetic bacterium. The mRNA of this gene is presentat different levels in distinct organs of the plant with the highestaccumulation detected in the elongation zone of roots. Bacterial extracts fromclones containing the maize OMT cDNA show an activity in methylation ofcaffeic acid to ferulic acid comparable to that existing in the plantextracts. These results indicate that the described gene encodes the caffeicacid 3-O-methyltransferase (COMT) involved in the lignin biosynthesis ofmaize.
237                                                    NAL Call. No.: QH426.C8Structure and expression of the rice mitochondrial apocytochrome b gene(cob-1) and pseudogene (cob-2).Kaleikau, E.K.; Andre, C.P.; Walbot, V.Berlin, W. Ger. : Springer International; 1992.Current genetics v. 22 (6): p. 463-470; 1992.  The accession numbers 170064and 533699 do not conform to standard format.  Includes references.
Language:  English
Descriptors: Oryza sativa; Mitochondrial  DNA; Structural genes; Pseudogenes;Cytochrome b; Apoproteins; Nucleotide sequences; Transcription; Promoters;Messenger  RNA; Gene expression; Molecular conformation
Abstract:  Rice mitochondrial DNA contains an intact copy and a pseudogenecopy of a apocytochrome b gene (cob-1 and cob-2, respectively). Using primerextension and capping analyses, the transcriptional start site has beenmapped; an 11-base motif at the transcription start site closely matches theconsensus promoter motifs proposed for maize, wheat and soybean mitochondrialgenes. Although both copies are identical in the 5' upstream region andthrough most of the coding region, only cob-1-specific mRNA is detected on RNAgel-blots. Run-on transcription analysis indicates, however, that both cob-1and cob-2 mRNAs are synthesized in vivo but less cob-2 is accumulated. At itsmapped 3' terminus the cob-1 transcript possesses a sequence that could foldinto a double stem-loop structure. The possible roles of a double stem-loopstructure in mitochondrial gene expression are discussed.
238                                                     NAL Call. No.: QK1.C83Structure and expression of zein genes of maize.Feix, G.; Quayle, T.Boca Raton, Fla. : CRC Press; 1993.Critical reviews in plant sciences v. 12 (1/2): p. 111-127; 1993.  Literaturereview.  Includes references.
Language:  English
Descriptors: Zea mays; Gene expression; Endosperm; Zein; Transcription;Genetic regulation; Literature reviews
239                                                   NAL Call. No.: 442.8 Z34Structure of the genes encoding Hordeum vulgare (1 to 3,1 to 4)-beta-glucanaseisoenzymes I and II and functional analysis of their promoters in barleyaleurone protoplasts.Wolf, N.Berlin, W. Ger. : Springer International; 1992 Jul.M G G : Molecular and general genetics v. 234 (1): p. 33-42; 1992 Jul.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Beta-glucanase; Isoenzymes;Nucleotide sequences; Amino acid sequences; Promoters; Introns; Geneexpression; Genetic regulation; Gibberellic acid; Reporter genes;Chloramphenicol acetyltransferase; Protoplasts; Aleurone cells; Seedgermination
Abstract:  Barley (1 leads to 3, 1 leads to 4)-beta-glucanase isoenzyme II issynthesized in the aleurone cells during germination and secreted into theendosperm for hydrolysis of the cell walls. Its synthesis is stimulated bygibberellic acid (GA3) and repressed by abscisic acid. The gene for isoenzymeI is expressed in the aleurone, scutellum and prominently in young leaves.Close functional relatedness between the two enzymes is attested by 92%identity at the level of the amino acid sequence. The structural genes for thetwo enzymes each contain a large intron of 2505 bp and 2952 bp, respectively,in the codon for amino acid 25 of the 28-residue signal peptide. Duringevolution, homologous regions of the two introns have changed position andorientation. Furthermore, a large palindromic sequence of 327 bp in the 5' endof the intron is present only in the gene for isoenzyme II. In transientexpression assays using barley aleurone protoplasts and chloramphenicol acetyltransferase as reporter the promoter of the isoenzyme I gene showed noresponse to GA3. However, removal of a unique 151 bp region extending frompositions -402 to -552 upstream of the TATA box permitted low levels ofGA3-induced expression of the reporter gene, suggesting a silencer functionfor this domain. High levels of GA3-responsive expression were obtained inaleurone protoplasts using the promoter of the gene encoding isoenzyme II.Truncation of this promoter revealed that sequences located within 253 bpupstream from the TATA box are sufficient to direct GA3-stimulated expression.Using the homologous barley aleurone protoplast transfection assay, it waspossible to reproduce the in vivo expression characteristics of the genes forthe barley (1 leads to 3, 1 leads to 4)-beta-glucanase isoenzymes I and IIwith reporter gene constructs.
240                                                     NAL Call. No.: 450 C16Susceptibility and resistance in Canadian spring wheat cultivars to commonbunt (Tilletia tritici and T. laevis).Gaudet, D.A.; Puchalski, B.J.; Kozub, G.C.; Schaalje, G.B.Ottawa : Agricultural Institute of Canada, 1957-; 1993 Oct.Canadian journal of plant science v. 73 (4): p. 1217-1224; 1993 Oct.  Includesreferences.
Language:  English
Descriptors: Canada; Cabt; Triticum aestivum; Tilletia tritici; Tilletialaevis; Plant pathogenic fungi; Disease resistance; Pathogenicity;Susceptibility; Cultivars; Genetic variation; Genotype environmentinteraction; Gene expression; Plant breeding; Variety trials
241                                              NAL Call. No.: S494.5.B563C87Synthesis and expression of a gene for mature small subunit of rice Rubisco.Chen, H.B.; Wang, G.A.Dordrecht : Kluwer Academic Publishers; 1993.Current plant science and biotechnology in agriculture v. 15: p. 160-164;1993.  In the series analytic: Biotechnology in Agriculture / edited by C.You, Z. Chen, Y. Ding.  Proceedings of the First Asia-Pacific Conference onAgricultural Biotechnology held August 20-24, 1992, Beijing, China.  Includesreferences.
Language:  English
Descriptors: Oryza sativa; Structural genes; Synthetic genes;Ribulose-bisphosphate carboxylase; Gene expression; Escherichia coli
242                                                   NAL Call. No.: QK710.P62Systemic induction of a potato pin2 promoter by wounding, methyl jasmonate,and abscisic acid in transgenic rice plants.Xu, D.; McElroy, D.; Thornburg, R.W.; Wu, R.Dordrecht : Kluwer Academic Publishers; 1993 Jul.Plant molecular biology v. 22 (4): p. 573-588; 1993 Jul.  Includes references.
Language:  English
Descriptors: Solanum tuberosum; Oryza sativa; Promoters; Proteinaseinhibitors; Recombinant  DNA; Reporter genes; Beta-glucuronidase; Geneexpression; Genetic regulation; Abiotic injuries; Abscisic acid; Jasmonicacid; Derivatives; Introns; Actin; Structural genes; Transgenic plants;Genetic transformation; Multigene families; Histoenzymology
Abstract:  To address the question whether common signal(s) and transductionpathways are used to mediate a systemic wound response in monocot and dicotplants, a fusion of the potato proteinase inhibitor II gene (pin2) promoterand the bacterial beta-glucuronidase gene (Gus)-coding region was introducedinto rice. In transgenic rice plants, the expression of the pin2-Gus fusiongene displays a systemic wound response, although the expression level isrelatively low. Incorporation of the first intron from the rice actin 1 gene(Act1) into the 5'-untranslated region of the pin2-Gus construct results inhigh-level, systemically wound-inducible expression of the modified constructin transgenic rice plants. Histochemical analysis shows that this high-level,wound-inducible expression is associated with the vascular tissue in bothleaves and roots. Furthermore, the expression of the pin2-Act1 intron-Gusfusion gene in transgenic rice plants can be systemically induced by bothmethyl jasmonate (MJ) and the phytohormone abscisic acid (ABA). These resultssuggest that the signal(s) mediating the observed systemic wound response andcertain steps of the transduction pathways are conserved between dicot andmonocot plants. Transient expression assays show that the pin2-Act1 intron-Gusconstruct is also actively expressed in transformed cells and tissues ofseveral other monocot plants. Thus, the wound-inducible pin2 promoter incombination with the rice Act1 intron 1 might be used as an efficientregulator for foreign gene expression in transgenic monocot plants.
243                                                   NAL Call. No.: QK710.P62Temporal and spatial regulation of a novel gene in barley embryos.Smith, L.M.; Handley, J.; Li, Y.; Martin, H.; Donovan, L.; Bowles, D.J.Dordrecht : Kluwer Academic Publishers; 1992 Oct.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (2): p. 255-266; 1992 Oct.Includes references.
Language:  English
Descriptors: Hordeum vulgare; Structural genes; Plant proteins; Plant embryos;Gene expression; Temporal variation; Spatial variation; Messenger  RNA;Scutellum; Coleoptiles; Embryogenesis; Flowers; Dna; Nucleotide sequences
Abstract:  The temporal and spatial pattern of expression of a novel barleygene is described. The gene has been identified through the differentialscreening of a cDNA library constructed to poly(A)+ RNA of zygotic embryos.Transcripts corresponding to the cDNA, pZE40, become abundant in the non-axialtissues of the developing embryo within 8-10 days after anthesis, whensteady-state levels are high in the scutellum, coleoptile and coleorhiza, withthe exception of the scutellar epithelium. This expression pattern ismaintained throughout maturation of the embryo until levels eventually declineas the grain desiccates. On germination, there is a transient re-appearance ofmRNA to pZE40, with accumulation specifically restricted to the scutellum ofthe seedling. In situ hybridization has enabled the detection of transcriptselsewhere in the barley plant, in highly localized groups of cells. The timingand cell specificity of expression suggests the gene product is involved inthe synthesis and/or transport of metabolites.
244                                                    NAL Call. No.: 500 N21PTissue culture-induced DNA methylation variation in maize.Kaeppler, S.M.; Phillips, R.L.Washington, D.C. : National Academy of Sciences,; 1993 Oct01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (19): p. 8773-8776; 1993 Oct01.  Includes references.
Language:  English
Descriptors: Zea mays; Dna methylation; Gene expression; Epigenetics;Heritability; Inbred lines; Genetic variation; Mutations; Somaclonalvariation; Transposable elements; Tissue culture
Abstract:  Twenty-one progeny lines derived from tissue cultures of two embryosources of maize inbred strain A188 were examined for DNA methylation changes.Total DNA was cut with the isoschizomers Hpa II and Msp I and probed with 18single-copy Pst I genomic clones and two cDNA clones. Eight of these probescould detect both increases and decreases in methylation. With these probes39% of the families were found to contain an altered methylation pattern. Allchanges represented a decrease in methylation. The other 12 probes coulddetect only increases in methylation; no methylation variation was seen withthese probes. Fifteen percent of the methylation changes were homozygous inthe original regenerated plant. Changes were stably inherited upon twogenerations of self-pollination. No sequence variation was observed in MspI-digested DNA from the same 21 progeny lines. Certain probes detectedmethylation changes much more often than others. Our study provides evidencethat demethylation occurs at a high frequency and could be an important causeof tissue culture-induced variation. Occurrence of the frequent homozygousalterations in original regenerated plants implies a nonrandom mutationalmechanism.
245                                                    NAL Call. No.: 500 N21PTissue-specific light-regulated expression directed by the promoter of a C4gene, maize pyruvate, orthophosphate dikinase, in a C3 plant, rice.Matsuoka, M.; Tada, Y.; Fujimura, T.; Kano-Murakami, Y.Washington, D.C. : National Academy of Sciences,; 1993 Oct15.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (20): p. 9586-9590; 1993 Oct15.  Includes references.
Language:  English
Descriptors: Oryza sativa; Gene expression; Genetic code; Genetictransformation; Lines; Reporter genes; Transgenics; Beta-glucuronidase;Binding proteins; Nucleoproteins; Orthophosphates; Photosynthesis; Pyruvatekinase
Abstract:  Pyruvate, orthophosphate dikinase (PPDK; EC 2.7.9.1) activity isabundant in leaves of C4 plants, while it is difficult to detect in leaves ofC3 Plants. Recent studies have indicated that C3 plants have a gene encodingPPDK, with a structure similar to that of PPDK in C4 plants. However, lowexpression makes PPDK detection difficult in C3 plants. This finding suggeststhat high PPDK expression in C4 plants is due to regulatory mechanisms whichare not operative in C3 plants. We have introduced a chimeric gene consistingof the gene encoding beta-glucuronidase (GUS; EC 3.2.1.31) controlled by thePPDK promoter from a C4 plant, maize, into a C3 cereal, rice. The chimericgene was exclusively expressed in photosynthetic organs, leaf blades andsheaths, and not in roots or stems. Histochemical analysis of GUS activitydemonstrated high expression of the chimeric gene in photosynthetic organs,localized in mesophyll cells, and no or very low activity in other cells. GUSexpression was also regulated by light in that it was low in etiolated leavesand was enhanced by illumination. These observations indicate that themechanisms responsible for cell-specific and light-inducible regulation ofPPDK observed in C4 plants are also present in C3 plants. We directly testedwhether rice has DNA-binding protein(s) which interact with a previouslyidentified cis-acting element of the C4-type gene. Gel retardation assaysindicate the presence in rice of a protein which binds this element and issimilar to a maize nuclear protein which binds PPDK in maize. Taken together,these results indicate that the regulatory system which controls PPDKexpression in maize is not unique to C4 plants.
246                                                   NAL Call. No.: QK710.P62Transcient and stable expression of gusA fusions with rice genes in rice,barley and perennial ryegrass.Hensgens, L.A.M.; Bakker, E.P.H.M. de; Os-Ruygrok, E.P. van; Rueb, S.; Mark,F. van de; Maas, H.M. van der; Veen, S. van der; Kooman-Gersmann, M.; Hart,L.; Schilperoort, R.A.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 643-669; 1993 Nov.  Includes references.
Language:  English
Descriptors: Oryza sativa; Lolium perenne; Hordeum vulgare; Genetictransformation; Transgenic plants; Reporter genes; Recombinant  DNA;Beta-glucuronidase; Gene expression; Histoenzymology; Callus; Promoters;Introns; Plant proteins
Abstract:  Transcriptional and translational fusions were made between thereading frame coding for beta-D-glucuronidase and sequences of either aconstitutively expressed rice gene (GOS2) involved in initiation oftranslation or a light-inducible rice gene (GOS5). The transient expression ofthe fusions was studied via particle bombardment of seedling tissues of rice,perennial ryegrass and barley. Furthermore, the results of transient andstable expression were compared for cell suspensions of four rice varieties,one barley variety and one perennial ryegrass variety. The GOS2-gusA fusionswere active in all three monocots studied. Best results were obtained for aconstruct having both a transcriptional and a translational fusion as well asintron and exon sequences (PORCEHyg). The level of GUS activity was in therange of activities as obtained by the 35S CaMV promoter transcriptionallyfused to gusA. The gusA fusion with the light-inducible gene (GOS5) was activein green seedling tissues of all monocots studied. Also a weak expressioncompared to the GOS2 constructs was found in stably transformed rice callus.The gusA fusions with the mannopine synthase promoters 1' and 2' of theT(R)-DNA were transiently expressed at lower levels in cell suspensions thanPORCEHyg. For stably transformed rice callus the expression ofthe GOS2-gusAfusion often decreased during prolonged subculture. This decrease in GUSactivity and the various GUS-staining phenotypes of transgenic calli areexplained by the presence of different cell types in the suspensions used andin the calli. It is presumed that the nature of the cells and their relativecontribution in the calli change drastically upon further subculture.
247                                                   NAL Call. No.: QK710.P62Transcription of the gene coding for subunit 9 of ATP synthase in ricemitochondria.Kaleikau, E.K.; Andre, C.P.; Walbot, V.Dordrecht : Kluwer Academic Publishers; 1993 Aug.Plant molecular biology v. 22 (5): p. 899-905; 1993 Aug.  Includes references.
Language:  English
Descriptors: Oryza sativa; Structural genes; Adenosinetriphosphatase;Mitochondrial  DNA; Transcription; Gene expression; Messenger  RNA; Promoters;Alternative splicing; Nucleotide sequences; Molecular conformation; Molecularmapping
Abstract:  Transcription of the single-copy rice mitochondrial atp9 gene hasbeen analyzed. We propose that there is a 0.65 kb primary transcript that isprocessed to an abundant 0.45 kb mRNA; a sequence motif at the 5' terminus ofthe 0.65 kb transcript shares 9 out of 11 nucleotides homology to theconsensus promoter proposed for maize. There are several 3' termini based onRNase protection, and these termini map within or just distal to invertedrepeats that could fold into a double stem-loop structure.
248                                                   NAL Call. No.: QK710.P62Transcriptional charcterization of an alpha-zein gene cluster in maize.Liu, C.N.; Rubenstein, I.Dordrecht : Kluwer Academic Publishers; 1993 May.Plant molecular biology v. 22 (2): p. 323-336; 1993 May.  Includes references.
Language:  English
Descriptors: Zea mays; Multigene families; Structural genes; Zein;Transcription; Gene expression; Genetic code; Messenger  RNA; Nucleotidesequences; Genetic regulation; Endosperm; Complementary  DNA
Abstract:  A cluster of five alpha-zein subfamily 4 (alpha-zein SF4) genes arepresent in a 56 kb region of the maize W22 genome. Two types of alpha-zein SF4genes are in the cluster. One of the genes, termed a type 1 (T1) alpha-zeinSF4 gene, contains no early in-frame stop codons. Four of the genes, termedtype 2 (T2) alpha-zein SF4 genes, contain one or two early in-frame stopcodons. The base sequence of the T1 alpha-zein SF4 gene is similar (> 90%) tothe sequences of any of the four T2 alpha-zein SF4 genes. However, theirsequences differ markedly at distances greater than -875 bp upstream from thetranslation initiation codon of the alpha-zein coding region. This region ofdissimilarity is well inside the functional 5'-flanking region for the genessince a 1.8 kb transcript is initiated in this region and the sequences of theT2 alpha-zein SF4 genes are similar in this region. Two sizes of mRNAtranscripts, 1.8 kb and 0.9 kb, were detected in a gene specific manner for 4of the 5 genes in this alpha-zein SF4 gene cluster. One of the T2 alpha-zeinSF4 genes had only the 0.9 kb transcript. The RNA level for the 0.9 kbtranscript of the T1 alpha-zein SF4 gene was 5- to 10-fold higher than thetranscript levels of any of the T2 alpha-zein SF4 genes. In each case, theamount of the 0.9 kb transcript detected was at least 5-fold higher than theamount of the 1.8 kb transcript. A cDNA clone with a sequence identical to aT2 alpha-zein SF4 gene was isolated, providing the first direct evidence forthe transcription of T2 alpha-zein genes containing early in-frame stopcodon(s) in maize endosperm.
249                                          NAL Call. No.: SB123.57.T732 1993Transgenic rice plants: tools for studies in gene regulation and cropimprovement.Kyozuka, J.; Shimamoto, K.New York : M. Dekker; 1993.Transgenic plants : fundamentals and applications /. p. 173-193; 1993.Includes references.
Language:  English
Descriptors: Oryza sativa; Transgenic plants; Genetic transformation; Plantbreeding; Gene expression; Genetic regulation; Genetic analysis; Literaturereviews
250                                                   NAL Call. No.: QK710.P68Transgenic tobacco plants expressing rgp1, a gene encoding a ras-relatedGTP-binding protein from rice, show distinct morphological characteristics.Kamada, I.; Yamauchi, S.; Youssefian, S.; Sano, H.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Sep.The plant journal v. 2 (5): p. 799-807; 1992 Sep.  Includes references.
Language:  English
Descriptors: Nicotiana tabacum; Structural genes; Binding proteins; Guanosinetriphosphate; Genetic transformation; Transgenic plants; Plant morphology;Plant development; Phenotypes; Abnormal development; Inheritance; Flowers;Flowering; Tillering
251                                                   NAL Call. No.: QK710.P68Transient gene expression in vegetative shoot apical meristems of wheat afterballistic microtargeting.Bilang, R.; Zhang, S.; Leduc, N.; Iglesias, V.A.; Gisel, A.; Simmonds, J.;Potrykus, I.; Sautter, C.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1993 Oct.The Plant journal : for cell and molecular biology v. 4 (4): p. 735-744; 1993Oct.  Includes references.
Language:  English
Descriptors: Oryza sativa; Sorghum bicolor; Triticum aestivum; Apicalmeristems; Gene expression; Gene transfer; Genetic transformation; Genotypes;Shoot tip culture; Transgenics
252                                                  NAL Call. No.: QK725.P532Translation of the mRNA of the maize transcriptional activator Opaque-2 isinhibited by upstream open reading frames present in the leader sequence.Lohmer, S.; Maddaloni, M.; Motto, M.; Salamini, F.; Thompson, R.D.Rockville, Md. : American Society of Plant Physiologists; 1993 Jan.The Plant cell v. 5 (1): p. 65-73; 1993 Jan.  Includes references.
Language:  English
Descriptors: Zea mays; Controlling elements; Messenger  RNA; Dna bindingproteins; Translation; Genetic regulation; Promoters; Structural genes;Opaque-2 maize; Gene expression
Abstract:  The protein encoded by the Opaque-2 (O2) gene is a transcriptionfactor, translated from an mRNA that possesses an unusually long 5' leadersequence containing three upstream open reading frames (uORFs). The efficiencyof translation of O2 mRNA has been tested in vivo by a transient assay inwhich the level of activation of the b32 promoter, a natural target of O2protein, is measured. We show that uORF-less O2 alleles possess a highertransactivation value than the wild-type allele and that the reduction intransactivation due to the uORFs is a cis-dominant effect. The data presentedindicate that both uORF1 and uORF2 am involved in the reducing effect andsuggest that both are likely to be translated.
253                                                      NAL Call. No.: 30 Ad9Transposable elements in maize: their role in creating plant geneticvariability.Peterson, P.A.San Diego, Calif. : Academic Press; 1993.Advances in agronomy v. 51: p. 79-124; 1993.  Includes references.
Language:  English
Descriptors: Zea mays; Transposable elements; Genetic engineering; Geneticvariation; Plant breeding; Variegation; Gene expression; Literature reviews
254                                                  NAL Call. No.: QK725.P532Transposon-mediated mutations in the untranslated leader of maize Adh1 thatincrease and decrease pollen-specific gene expression.Dawe, R.K.; Lachmansingh, A.R.; Freeling, M.Rockville, Md. : American Society of Plant Physiologists; 1993 Mar.The Plant cell v. 5 (3): p. 311-319; 1993 Mar.  Includes references.
Language:  English
Descriptors: Zea mays; Transposable elements; Induced mutations; Insertionalmutagenesis; Structural genes; Alcohol dehydrogenase; Alleles; Geneticregulation; Gene expression; Pollen; Roots; Scutellum; Messenger  RNA;Nucleotide sequences; Anaerobic conditions; Spikelets; Histoenzymology
Abstract:  The unstable mutation Adh1-Fm335 contains a Dissociation (Ds1)transposable element at position +53 in the untranslated leader of the maizeAlcohol dehydrogenase-1 (Adh1) gene. Excision of Ds1 is known to generate newalleles with small additions and rearrangements of Adh1 DNA. We characterized16 revertant alleles with respect to ADH1 activity levels in scutellum(nutritive tissue of the seed), anaerobic root, and pollen. Whereas geneexpression was not different from the wild type in the sporophytic tissues ofthe scutellum and anaerobic root, there were strong allelic differences inpollen. One allele underexpressed pollen ADH1 at 48% of the wild-type level,and another overexpressed pollen ADH1 at 163% of the wild-type level.Quantitative RNase protection assays demonstrated that the mutant phenotypesreflected changes in the levels of steady state mRNA in pollen. These dataprovide a definitive demonstration of an overexpression mutant in plants andfurther show that marked increases in mRNA levels can follow minor alterationsin central untranslated leader sequences. The nucleotide sequence of 12 newrevertant alleles and the molecular mechanisms responsible for pollen-specificgene expression are discussed.
255                                             NAL Call. No.: S494.5.B563B554Trypsin/alpha-amylase inhibitors and thionins: possible defence proteins frombarley.Garcia-Olmedo, F.; Salcedo, G.; Sanchez-Monge, R.; Hernandez-Lucas, C.;Carmona, M.J.; Lopez-Fando, J.J.; Fernandez, J.A.; Gomez, L.; Royo, J.;Garcia-Maroto, F.Wallingford, Oxford, UK : CAB International; 1992.Biotechnology in agriculture (5): p. 335-350; 1992.  In the series analytic:Barley : genetics, biochemistry, molecular biology and biotechnology / editedby P.R. Shewry.  Includes references.
Language:  English
Descriptors: Hordeum; Alpha-amylase; Enzyme inhibitors; Trypsin inhibitors;Polypeptides; Defense; Plant pathogens; Plant pests; Genetic variation; Genomeanalysis; Spatial distribution; Genes; Gene mapping; Amino acid sequences;Gene expression; Molecular genetics
256                                                 NAL Call. No.: 442.8 J8224Tubulin gene expression in maize (Zea mays L.): change in isotype expressionalong the developmental axis of seedling root.Joyce, C.M.; Villemur, R.; Snustad, D.P.; Silflow, C.D.London : Academic Press; 1992 Sep05.Journal of molecular biology v. 227 (1): p. 97-107; 1992 Sep05.  Includesreferences.
Language:  English
Descriptors: Zea mays; Multigene families; Multiple genes; Tubulin; Isotypes;Gene expression; Roots; Seedlings; Root tips; Immunohistochemistry
Abstract:  Two-dimensional gel/western blot analysis was used to characterizealpha- and beta-tubulin isotype expression along the developmental axis of themaize (Zea mays) seedling primary root. We identified four distinctalpha-tubulin isotypes and a minimum of six beta-tubulin isotypes. Thisanalysis showed differences between the alpha- and beta-tubulin isotypesexpressed in rapidly dividing tissue at the root tip and differentiated roottissues proximal to the tip. The alpha-1 and alpha-4 isotypes predominated insamples from immature rapidly dividing tissues such as root tips, whereas inmature tissues such as differentiated root and pollen, alpha-2, alpha-3 andalpha-4 isotypes predominated. The beta-1 and beta-2 isotypes were moreabundant in protein samples from root cortex than in samples from the root tipor vascular cylinder. In contrast, the beta-4 and beta-5 isotypes appeared tobe more abundant in root tip and vascular cylinder samples than in root cortexsamples. Hybridization probes from the 3' non-coding region of sixalpha-tubulin cDNA clones were used to quantify the levels of correspondingtubulin transcripts in selected tissues, from embryonic to mature and fromlargely undifferentiated to highly differentiated. The results from thesehybridization experiments showed that all of the tubulin genes were expressedin all tissues examined, although each gene showed a unique pattern ofdifferential transcript accumulation. A transcript produced from cDNA clonerepresenting the tua5 alpha-tubulin gene was translated in vitro and producedan alpha-tubulin that comigrated with the alpha-2 isotype.
257                                                   NAL Call. No.: QK710.P62Two members of the ERabp gene family are expressed differentially inreproductive organs but to similar levels in the coleoptile of maize.Hesse, T.; Garbers, C.; Brzobohaty, B.; Kreimer, G.; Soll, D.; Melkonian, M.;Schell, J.; Palme, K.Dordrecht : Kluwer Academic Publishers; 1993 Oct.Plant molecular biology v. 23 (1): p. 57-66; 1993 Oct.  Includes references.
Language:  English
Descriptors: Zea mays; Multigene families; Structural genes; ComplementaryDNA; Binding proteins; Auxins; Nucleotide sequences; Amino acid sequences;Gene expression; Messenger  RNA; Coleoptiles; Styles; Tassels; Maize ears
Abstract:  A Zea mays cDNA clone, ZmERabp4, coding for a new member of theauxin-binding protein family was isolated. The primary amino acid sequencecontains an N-terminal hydrophobic leader sequence, a potential glycosylationsite (Asn136-Thr-Thr) and a C-terminal KDEL motif known to be responsible forretention of proteins within the lumen of the ER. The expression pattern ofthe ZmERabp4 gene in various organs of maize differs from the expressionpattern previously observed for the ZmERabp1 gene. The ZmERabp4 gene isexpressed highly in male flower organs, whereas the ZmERabp1 gene showshighest expression in female flower parts. In situ hybridization and analysisby laser scanning microscopy revealed enhanced levels of expression for bothgenes in the coleoptile when compared with the primary leaf of etiolated maizeseedlings.
258                                                   NAL Call. No.: QK710.P62Unusual sequence of group 3 LEA (II) mRNA inducible by dehydration stress inwheat.Curry, J.; Walker-Simmons, M.K.Dordrecht : Kluwer Academic Publishers; 1993 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (5): p. 907-912; 1993 Mar.Includes references.
Language:  English
Descriptors: Triticum aestivum; Complementary  DNA; Messenger  RNA; Nucleotidesequences; Amino acid sequences; Plant proteins; Gene expression; Geneticregulation; Desiccation; Water stress; Abscisic acid
Abstract:  A cDNA clone, pMA1949, detects two mRNA species in wheat seedlingtissue that are late embryogenesis-abundant (LEA) and dehydrationstress-inducible. Sequence analysis of the pMA1949 clone shows it to be a 991bp partial cDNA encoding a polypeptide of 317 amino acids with homology to twogroup 3 LEA proteins, carrot (DC8) and a soybean protein encoded by pGmPM2cDNA. Molecular analysis of the deduced protein reveals a 33 kDa acidic andextremely hydrophilic protein with potential amphiphilic alpha-helicalregions. In addition, the protein contains eleven similar, contiguous repeatsof 11 amino acids, which are separated by 118 amino acids from two additionaland unique repeats of 36 residues each at the carboxyl end of the protein.Comparisons of sequences of reported group 3 LEA proteins revealed that thereare two types, separable by sequence similarity of the 11 amino acid repeatingmotifs and by the presence or absence of a certain amino acid stretch at thecarboxyl terminus. Based on results from these comparisons, we propose asecond type of group 3 LEA proteins, called group 3 LEA (II).
259                                                    NAL Call. No.: 500 N21PAn upstream open reading frame represses expression of Lc, a member of the R/Bfamily of maize transcriptional activators.Damiani, R.D. Jr; Wessler, S.R.Washington, D.C. : National Academy of Sciences,; 1993 Sep01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (17): p. 8244-8248; 1993 Sep01.  Includes references.
Language:  English
Descriptors: Zea mays; Amino acid sequences; Anthocyanins; Gene expression;Genetic code; Nucleotide sequences; Transcription
Abstract:  The R/B genes of maize encode a family of basic helix-loop-helixproteins that determine where and when the anthocyanin-pigment pathway will beexpressed in the plant. Previous studies showed that allelic diversity amongfamily members reflects differences in gene expression, specifically intranscription initiation. We present evidence that the R gene Lc is undertranslational control. We demonstrate that the 235-nt transcript leader of Lcrepresses expression 25- to 30-fold in an in vivo assay. Repression ismediated by the presence in cis of a 38-codon upstream open reading frame.Furthermore, the coding capacity of the upstream open reading frame influencesthe magnitude of repression. It is proposed that translational control doesnot contribute to tissue specificity but prevents overexpression of the Lcprotein. The diversity of promoter and 5' untranslated leader sequences amongthe R/B genes provides an opportunity to study the coevolution oftranscriptional and translational mechanisms of gene regulation.
260                                                    NAL Call. No.: QK710.A9The use of the Emu promoter with antibiotic and herbicide resistance genes forthe selection of transgenic wheat callus and rice plants.Chamberlain, D.A.; Brettell, R.I.S.; Last, D.I.; Witrzens, B.; McElroy, D.;Dolferus, R.; Dennis, E.S.Melbourne, Commonwealth Scientific and Industrial Research Organization; 1994.Australian journal of plant physiology v. 21 (1): p. 95-112; 1994.  Includesreferences.
Language:  English
Descriptors: Triticum aestivum; Oryza sativa; Gene transfer; Transgenicplants; Callus; Gene expression; Selection; Marker genes; Leaves; Enzymeactivity; Promoters
261                                                    NAL Call. No.: 450 P692Visualizing enzyme secretion from individual barley (Hordeum vulgare) aleuroneprotoplasts.Hillmer, S.; Gilroy, S.; Jones, R.L.Rockville, Md. : American Society of Plant Physiologists; 1993 May.Plant physiology v. 102 (1): p. 279-286; 1993 May.  Includes references.
Language:  English
Descriptors: Hordeum vulgare; Aleurone layer; Protoplasts; Plant composition;Alpha-amylase; Genetic regulation; Gene expression; Transcription; Enzymeactivity; Starch; Hydrolysis
Abstract:  A method was developed to detect alpha-amylase gene expression andalpha-amylase secretion from individual barley (Hordeum vulgare L. cvHimalaya) aleurone protoplasts. Protoplasts are incubated in liquid media withor without hormones and embedded in a thin film of agarose and starch, wherethey remain viable for up to 24 h. alpha-Amylase secreted by individualprotoplasts digests the starch, and starch hydrolysis is visualized after 45min by staining the preparation with I2KI. After I2KI staining, secretingprotoplasts are surrounded by a clear, starch-free halo visible by lightmicroscopy. The formation of starch-free halos is dependent on the synthesisand secretion of alpha-amylase and is not caused by carry-over of preformedenzyme from incubation media. Treating protoplasts with inhibitors of proteinsynthesis or exposing them to anaerobic conditions for 2 h before embeddingthem in agarose prevents the formation of halos. When alpha-amylase secretionis observed by counting the percentage of secreting protoplasts, the data arecomparable to that obtained by measuring alpha-amylase secretion from apopulation of cells. The response of individual protoplasts to gibberellicacid (GA3) and abscisic acid measured by the thin-film method is almostidentical to the response of populations of protoplasts to these hormones,validating the utility of this method. Although not generally practical forquantifying secretion, the thin-film method is uniquely useful indistinguishing secreting from nonsecreting protoplasts. In none of ourexperiments did more than 60% of the protoplasts secrete alpha-amylase whenexposed to GA3, even though more than 95% of the protoplasts in thepreparations were viable. Similar results were obtained when the response toGA3 was assayed at the level of gene transcription by visualizing thetransient expression of a plasmid containing the promoter from alpha-amylasefused to the reporter gene glucuronidase in single protoplasts. The thin-filmsecretion assay also revealed that the response of a population of protoplaststo GA3 was not uniform with time.  The effect of GA3 treatment was togradually increase the percentage of responding protoplasts up to a maximum of50 to 60%.  Abscisic acid, which inhibits alpha-amylase secretion byGA3-treated protoplasts, reduced the proportion of protoplasts that secretethe enzyme.
262                                                    NAL Call. No.: QP501.E8Wheat Ec metallothionein genes. Like mammalian Zn2+ metallothionein genes,wheat Zn2+ metallothionein genes are conspicuously expressed duringembryogenesis.Kawashima, I.; Kennedy, T.D.; Chino, M.; Lane, B.G.New York, NY : Springer-Verlag New York Inc; 1992 Nov.European journal of biochemistry v. 209 (3): p. 971-976; 1992 Nov.  Includesreferences.
Language:  English
Descriptors: Triticum aestivum; Plant embryos; Polyploidy; Metallothionein;Genes; Zinc; Metal ions; Embryogenesis; Seed germination; Messenger  RNA;Nucleotide sequences; Amino acid sequences; Comparisons; Gene expression
Abstract:  A cDNA library was prepared from the bulk mRNA of mature wheatembryos and screened with mixed 32P-labeled oligonucleotide probes thatencoded parts of the partial amino-acid sequence for the Zn-containing E(c)protein. Each DNA insert in 11 positives from a screen of 10(5) plaquesencoded a 5' untranslated and a 3' untranslated region, in addition to an openreading frame (of 81 amino acids) which, in every case, corresponded to atleast 56 of the 59 amino acids in the partial polypeptide sequence previouslydetermined for the E(c) protein. The three different mRNA sequences encoded inthe cDNA probably correspond to single-copy genes in the A, B and D genomes ofhexaploid wheat. A wheat genomic library was screened with 32P-labeled cDNAand gave a single positive in a screen of 5 X 10(5) plaques. A 3.1-kb genomicfragment (gf-3.1) was sequenced and a cap site for the encoded mRNA wasdetermined by primer extension. The gf-3.1 sequence encodes an intronless mRNAfor the E(c) protein and contains appreciable amounts of 5' and 3' flankingsequences. In addition to a putative TATA box, two inverted-repeat sequencesand one direct-repeat sequence, the 5' flank in gf-3.1 contains a sequencesimilar to the abscisic-acid-responsive element in other higher-plant genesbut does not contain sequences similar to the metal-responsive elements inanimal metallothionein genes. Consistent with these findings, RNA blottingshows that accumulation of E(c) mRNA is abundant in immature embryos,undetectable in germinated embryos and can be induced by adding abscisic acid,but not by adding Zn2+ to the medium in which mature wheat embryos aregerminated. The findings suggest that the wheat E(c) metallothionein genes,like mammalian liver metallothionein genes, are conspicuously expressed duringembryogenesis.
263                                                   NAL Call. No.: QK710.P68A wheat histone H3 promoter confers cell division- dependent and -independentexpression of the gus A gene in transgenic rice plants.Terada, R.; Nakayama, T.; Iwabuchi, M.; Shimamoto, K.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Feb.The plant journal v. 3 (2): p. 241-252; 1993 Feb.  Includes references.
Language:  English
Descriptors: Triticum aestivum; Oryza sativa; Promoters; Histones; Deletions;Recombinant  DNA; Reporter genes; Beta-glucuronidase; Gene expression; Celldivision; Transgenic plants; Genetic transformation; Gene splicing; Geneticregulation; Histoenzymology; Apical meristems; Roots; Shoots; Anthers;Gynoecium; Leaves
264                                                   NAL Call. No.: QK710.P62WIP1, wound-inducible gene from maize with homology to Bowman-Birk proteinaseinhibitors.Rohrmeier, T.; Lehle, L.Dordrecht : Kluwer Academic Publishers; 1993 Aug.Plant molecular biology v. 22 (5): p. 783-792; 1993 Aug.  Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Structural genes; Proteinaseinhibitors; Plant proteins; Nucleotide sequences; Introns; Amino acidsequences; Genetic regulation; Abiotic injuries; Coleoptiles; Gene expression;Messenger  RNA
Abstract:  We have cloned and sequenced a wound-inducible cDNA clonedesignated WIP1 (for wound-induced protein) from maize coleoptiles. It wasisolated by differential screening of a cDNA library prepared from excisedmaize coleoptile segments. The deduced amino acid sequence predicts asecretory, cysteine-rich protein of 102 residues with a calculated molecularmass of 11 kDa and a typical N-terminal signal sequence. The protein has about30% identity with various Bowman-Birk type proteinase inhibitors. Mostinterestingly, it is novel in that it is double-headed with exclusivespecificity for chymotrypsin. WIP1 is strongly wound-induced in contrast toother members of the Bowman-Birk proteinase inhibitor family, which occur inseeds and are regulated during development. The response is fast, similar todefence-induced genes, and measurable as early as 30 min after wounding.Induction can also be evoked in the intact coleoptiles and the signal issystemically transmitted in the coleoptile to adjacent regions of the woundedarea. Isolation and analysis of the corresponding genomic clone reveals thatWIP1 contains an intron of 90 nucleotides.
265                                                   NAL Call. No.: 450 J8224The ypt gene family from maize and Arabidopsis: structural and functionalanalysis.Palme, K.; Diefenthal, T.; Moore, I.Oxford : Oxford University Press; 1993 Jan.Journal of experimental botany v. 44 (suppl.): p. 183-195; 1993 Jan.  In thespecial issue: Vesicle traffic and protein transport in plants and yeast /edited by D.G. Robinson, K.J. Oparka and M.D. Watson. Papers presented at anInternational Symposium, March 23-27, 1992, Gottingen, FRG.  Includesreferences.
Language:  English
Descriptors: Zea mays; Arabidopsis thaliana; Multigene families; Structuralgenes; Nucleotide sequences; Amino acid sequences; Binding proteins; Guanosinetriphosphate; Guanosine diphosphate; Gene expression; Anthers; Pollen; Genetictransformation
Abstract:  Small G-proteins are encoded by ras-related genes and play acentral role in cell differentiation and vesicle transport. Here we describeexperiments to identify members of this gene family in higher plants. Severaloligonucleotide mixtures, corresponding to strictly conserved amino acidsequences in all the ras and ras-related proteins, from yeast to man, wereused to search for members of the plant ras gene family. With these probes weinitially screened a coleoptile-specific cDNA library from Zea mays (L.) andisolated two genes, denoted yptm1 and yptm2, encoding proteins homologous tothe ypt/rab protein family. Using these cDNAs as probes additional members ofthe ypt/rab gene family were isolated from Zea mays and Arabidopsis thaliana.The proteins predicted from the cDNAs isolated from maize and Arabidopsisshowed high similarity to other members of the ras family, in particular inthe regions involved in GTP/GDP binding, GTPase activity, and membranebinding. Homology to the ypt/rab family was in the range 70-80%, whereassimilarity to p21ras and other ras-related genes was less than 40%. Inaddition, we identified genes from maize and Arabidopsis, ypt3 and At-rab2,encoding proteins homologous to the mammalian rab2 protein. These genes wereexpressed preferentially in male flower tissue, in particular in the anthersand pollen. This expression pattern was confirmed by expression of the E. colibeta-glucuronidase gene under the control of the At-rab2 promoter. We observedthat, in A. thaliana plants stably transformed with this construct, thereporter gene was predominantly expressed in vascular tissues and in pollen.
266                                                  NAL Call. No.: QH442.A1G4Zea mI, the maize homolog of the allergen-encoding Lol pI gene of rye grass.Broadwater, A.H.; Rubinstein, A.L.; Chay, C.H.; Klapper, D.G.; Bedinger, P.A.Amsterdam : Elsevier Science Publishers; 1993.Gene v. 131 (2): p. 227-230; 1993.  Includes references.
Language:  English
Descriptors: Zea mays; Complementary  DNA; Structural genes; Plant proteins;Nucleotide sequences; Amino acid sequences; Multigene families; Geneexpression; Pollen; Immunohistochemistry; Comparisons; Allergens; Loliumperenne
Abstract:  Sequence analysis of a pollen-specific cDNA from maize hasidentified a homolog (Zea mI) of the gene (Lol pI) encoding the major allergenof rye-grass pollen. The protein encoded by the partial cDNA sequence is 59.3%identical and 72.7% similar to the comparable region of the reported aminoacid sequence of Lol pIA. Southern analysis indicates that this cDNArepresents a member of a small multigene family in maize. Northern analysisshows expression only in pollen, not in vegetative or female floral tissues.The timing of expression is developmentally regulated, occurring at a lowlevel prior to the first pollen mitosis and at a high level after thispostmeiotic division. Western analysis detects a protein in maize pollenlysates using polyclonal antiserum and monoclonal antibodies directed againstpurified Lolium perenne allergen.
267                                                   NAL Call. No.: QK710.P62A zein gene promoter fragment drives GUS expression in a cell layer that isinterposed between the endosperm and the seed coat.Matzke, A.J.M.; Stoger, E.M.; Matzke, M.A.Dordrecht : Kluwer Academic Publishers; 1993 Jun.Plant molecular biology v. 22 (3): p. 553-554; 1993 Jun.  Includes references.
Language:  English
Descriptors: Zea mays; Promoters; Zein; Recombinant  DNA; Beta-glucuronidase;Reporter genes; Gene expression; Histoenzymology; Endosperm; Testas
268                                                   NAL Call. No.: QH506.E46Zmhox1a, the product of a novel maize homeobox gene, interacts with theShrunken 26 bp feedback control element.Bellmann, R.; Werr, W.Oxford, Eng. : IRL Press; 1992 Sep.The EMBO journal - European Molecular Biology Organization v. 11 (9): p.3367-3374; 1992 Sep.  Includes references.
Language:  English
Descriptors: Zea mays; Structural genes; Dna binding proteins; Nucleotidesequences; Amino acid sequences; Binding site; Dna; Gene location;Chromosomes; Gene expression; Messenger  RNA; Genetic regulation;Transcription; Translation; Molecular conformation
Abstract:  A new maize homeobox gene was isolated by screening a lambda gt11expression library with the 26 bp Shrunken feedback control element. Zmhox1a(Zea mays homeobox) is an unidentified maize gene mapping to the long arm ofchromosome 8. It is a member of a new class of maize homeobox genes onlydistantly related to the Knotted class. The 3.1 kb Zmhox1a transcript can bedetected in different maize tissues and encodes a polypeptide of 719 aminoacids. Western blotting experiments detect the native 112 or 115 kDa proteinin nuclear protein extracts, the nuclear localization being compatible with afunction in transcriptional control. No Zmhox1a protein is detected in maizeroots despite the presence of the Zmhox1a transcript; this may indicate apost-transcriptional control mechanism. A highly acidic central region of theZmhox1a polypeptide implies a transcriptional activator function. Thecarboxy-terminal part of the maize homeodomain protein is related to the humanOct2 transcription factor, but homology to the POU specific domain isrestricted to the POU-B subdomain. It was confirmed by DNase I footprintingexperiments that DNA binding of the Zmhox1a homeodomain was at three sitesflanking the TATA-box of the Shrunken promoter.