TITLE: Gene Expression in Oilseed, Fiber and Forage CropsPUBLICATION DATE: August, 1994ENTRY DATE: August, 1994EXPIRATION DATE: NoneUPDATE FREQUENCY: As neededCONTACT: Biotechnology Information Center(biotech@nalusda.gov)         National Agricultural LibraryDOCUMENT TYPE: TextDOCUMENT SIZE: 326k, approx. 181 pp.
United States Department of AgricultureNational Agricultural Library10301 Baltimore Blvd.Beltsville, Maryland 20705 - 2351
Gene Expression in Oilseed, Fiber and Forage CropsJan 1992 - May 1994
QB 94-48Quick Bibliographies
Ray Dobert
           Gene Expression in Oilseed, Fiber and Forage Crops                                    
                             SEARCH STRATEGY
     SET       ITEMS     DESCRIPTION            S1 872   (EXPRESS?(3W)(GENE OR GENES))/TI      S29327   GENE()EXPRESS?/DE      S320326  COTTON OR FLAX OR KENAF OR (FIBER()CROP?)      S48327   GOSSYPIUM OR LINUM OR HIBISCUS      S522922  S3 OR S4      S69568   S1 OR S2      S7  55   S5 AND S6      S851813  SOYBEAN? OR SOYABEAN? OR COTTON OR CANOLA OR               RAPE OR  SUNFLOWER? OR CRAMBE OR PEANUT? OR               SAFFLOWER? OR (OIL OR OILSEED)()CROP?      S914075  GLYCINE()MAX OR BRASSICA()CAMPESTRIS OR                     HELIANTHUS()ANNUS  OR CARTHAMUS()TINCTORIUSOR             ARACHIS()HYPOGAEA     S1055494  S8 OR S9     S1118710  S5 AND S10     S12 435   S6 AND S10     S1337185  (FORAGE OR FODDER OR PASTURE)()CROP? OR ALFALFA OR               CLOVER OR LUPINE? OR FESCUE OR BROMEGRASS? OR               SUDAN()GRASS? OR TREFOIL OR SAINFOIN OR GRASS?     S1410567  MEDICAGO OR LUPINUS OR ASTRAGALUS OR CORONILLA                   OR CROTALARIA OR HEDYSARUM OR LABLAB OR                TRIGONELLA OR VICIA     S1543854  S13 OR S14     S16 237   S6 AND S15     S17 682   S7 OR S12 OR S16     S18 251   S17 AND PY=1992:19941                                                    NAL Call. No.: QK725.P532
A 62-kD sucrose binding protein is expressed and localized in tissues activelyengaged in sucrose transport.Grimes, H.D.; Overvoorde, P.J.; Ripp, K.; Franceschi, V.R.; Hitz, W.D.Rockville, Md. : American Society of Plant Physiologists; 1992 Dec.The Plant cell v. 4 (12): p. 1561-1574; 1992 Dec.  Includes references.
Language:  English
Descriptors: Glycine max; Structural genes; Plant proteins; Sucrose; Bindingproteins; Dna; Nucleotide sequences; Amino acid sequences; Active transport;Plasma membranes; Mesophyll; Phloem companion cells; Cotyledons; Geneexpression; Messenger  RNA
Abstract:  Sucrose transport from the apoplasm, across the plasma membrane,and into the symplast is critical for growth and development in most plantspecies. Phloem loading, the process of transporting sucrose against aconcentration gradient into the phloem, is an essential first step inlong-distance transport of sucrose and carbon partitioning. We report herethat a soybean 62-kD sucrose binding protein is associated with the plasmamembrane of several cell types engaged in sucrose transport, including themesophyll cells of young sink leaves, the companion cells of mature phloem,and the cells of the developing cotyledons. Furthermore, the temporalexpression of the gene and the accumulation pattern of the protein closelyparallel the rate of sucrose uptake in the cotyledon. Molecular cloning andsequence analysis of a full-length cDNA for this 62-kD sucrose binding proteinindicated that the protein is not an invertase, contains a 29-amino acidleader peptide that is absent from the mature protein, and is not an integralmembrane protein. We conclude that the 62-kD sucrose binding protein isinvolved in sucrose transport, but is not performing this functionindependently.
2                                                     NAL Call. No.: QK710.P62Accumulation of a Brazil nut albumin in seeds of transgenic canola results inenhanced levels of seed protein methionine.Altenbach, S.B.; Kuo, C.C.; Staraci, L.C.; Pearson, K.W.; Wainwright, C.;Georgescu, A.; Townsend, J.Dordrecht : Kluwer Academic Publishers; 1992 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (2): p. 235-245; 1992 Jan.Includes references.
Language:  English
Descriptors: Bertholletia excelsa; Brassica napus; Gene transfer; Genetictransformation; Transgenics; Albumins; Genes; Chimeras; Gene expression;Seeds; Methionine; Plant proteins; Protein value; Seed development; Aminoacids
Abstract:  We have increased the methionine content of the seed proteins of acommercial winter variety of canola-rich seed protein from Brazil nut in theseeds of by expressing a chimeric gene encoding a methionine-rich seed proteinfrom Brazil nut in the seeds of transgenic plants. Transgenic canola seedsaccumulate the heterologous methionine-rich protein at levels which range from1.7% to 4.0% of the total seed protein and contain up to 33% more methionine.The precursor of the methionine-rich protein is processed correctly in theseeds, resulting in the appearance of the mature protein in the 2S proteinfraction. The 2S methionine-rich protein accumulates in the transgenic seedsat the same time in development as the canola 11S seed proteins and disappearsrapidly upon germination of the seed. The increase in methionine in the canolaseed proteins should increase the value of canola meal which is used in animalfeed formulations.
3                                                      NAL Call. No.: QK710.A9Acid-tolerant species of Medicago produce root exudates at low pH which inducethe expression of nodulation genes in Rhizobium meliloti.Howieson, J.G.; Robson, A.D.; Abbott, L.K.East Melbourne : Commonwealth Scientific and Industrial Research Organization;1992.Australian journal of plant physiology v. 19 (3): p. 287-296; 1992.  Includesreferences.
Language:  English
Descriptors: Medicago; Medicago polymorpha; Medicago truncatula; Medicagolittoralis; Rhizobium meliloti; Rhizobium leguminosarum; Escherichia coli;Symbiosis; Root nodules; Nodulation; Genetic regulation; Plasmids; Geneexpression; Transcription; Acidity; Tolerance; Ph; Root exudates; Calcium;Genes
4                                                     NAL Call. No.: QK710.P62Activation of flavonoid biosynthesis in roots of Vicia sativa subsp. nigraplants by inoculation with Rhizobium leguminosarum biovar viciae.Recourt, K.; Tunen, A.J. van; Mur, L.A.; Brussel, A.N.A. van; Lugtenbergh,B.J.J.; Kijne, J.W.Dordrecht : Kluwer Academic Publishers; 1992 Jun.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (3): p. 411-420; 1992 Jun.Includes references.
Language:  English
Descriptors: Vicia sativa subsp. nigra; Rhizobium leguminosarum; Roots;Infection; Phenylalanine ammonia-lyase; Transferases; Naringenin-chalconesynthase; Enzyme activity; Bacterial proteins; Gene expression; MessengerRNA; Nodulation; Flavonoids; Biosynthesis
Abstract:  Infective (nodulating) Rhizobium leguminosarum biovar viciae (R.l.viciae) bacteria release Nod factors which stimulate the release of nodulationgene-inducing flavanones and chalcones from roots of the host plant Viciasativa subsp. nigra (K. Recourt et al., Plant Mol Biol 16: 841-852; H.P.Spaink et al., Nature 354: 125-130). The hypothesis that this release resultsfrom increased synthesis of flavonoids was tested by studying the effect ofinoculation of V. sativa with infective and uninfective R.l. viciae bacteriaon (i) activity of L-phenylalanine ammonia-lyase, (ii) level of chalconesynthase mRNA, and (iii) activity of (eriodictyol) methyltransferase in roots.Consistent with the hypothesis, each of these parameters was found to increase1.5 to 2-fold upon inoculation with infective R.l. viciae bacteria relative tothe situation for uninoculated roots and for roots inoculated with uninfectiverhizobia.
5                                                     NAL Call. No.: QK710.P62Activation of flavonoid biosynthesis in roots of Vicia sativa subsp. nigraplants by inoculation with Rhizobium leguminosarum biovar viciae.Recourt, K.; Tunen, A.J. van; Mur, L.A.; Brussel, A.N.A. van; Lugtenbergh,B.J.J.; Kijne, J.W.Dordrecht : Kluwer Academic Publishers; 1992 Jun.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (3): p. 411-420; 1992 Jun.Includes references.
Language:  English
Descriptors: Vicia sativa subsp. nigra; Rhizobium leguminosarum; Roots;Infection; Phenylalanine ammonia-lyase; Transferases; Naringenin-chalconesynthase; Enzyme activity; Bacterial proteins; Gene expression; MessengerRNA; Nodulation; Flavonoids; Biosynthesis
Abstract:  Infective (nodulating) Rhizobium leguminosarum biovar viciae (R.l.viciae) bacteria release Nod factors which stimulate the release of nodulationgene-inducing flavanones and chalcones from roots of the host plant Viciasativa subsp. nigra (K. Recourt et al., Plant Mol Biol 16: 841-852; H.P.Spaink et al., Nature 354: 125-130). The hypothesis that this release resultsfrom increased synthesis of flavonoids was tested by studying the effect ofinoculation of V. sativa with infective and uninfective R.l. viciae bacteriaon (i) activity of L-phenylalanine ammonia-lyase, (ii) level of chalconesynthase mRNA, and (iii) activity of (eriodictyol) methyltransferase in roots.Consistent with the hypothesis, each of these parameters was found to increase1.5 to 2-fold upon inoculation with infective R.l. viciae bacteria relative tothe situation for uninoculated roots and for roots inoculated with uninfectiverhizobia.
6                                                     NAL Call. No.: QK710.P62The activation process of Arabidopsis thaliana A1 gene encoding thetranslation elongation factor EF-1 alpha conserved among angiosperms.Curie, C.; Liboz, T.; Montane, M.H.; Rouan, D.; Axelos, M.; Lescure, B.Dordrecht : Kluwer Academic Publishers; 1992 Apr.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (6): p. 1083-1089; 1992 Apr.Includes references.
Language:  English
Descriptors: Arabidopsis thaliana; Nicotiana tabacum; Zea mays; Brassicacampestris; Lycopersicon esculentum; Multigene families; Translation;Proteins; Introns; Controlling elements; Promoters; Mutations; Dna bindingproteins; Evolution; Transgenics; Genetic transformation; Gene expression;Transcription; Nucleotide sequences
Abstract:  In Arabidopsis thaliana, the activation process of the A1 EF-1alpha gene depends on several elements. Using the GUS reporter gene, transientexpression experiments have shown that mutations of upstream cis-actingelements of the A1 promoter, or the deletion of an intron located within the5' non-coding region, similarly affect expression in dicot or monocotprotoplasts. The results reported here strongly suggest that this 5' intron isproperly spliced in Zea mays. We show that two trans-acting factors,specifically interacting with an upstream activating sequence (the TEF 1 box),are present in nuclear extracts prepared from A. thaliana, Brassica rapa,Nicotiana tabacum and Z. mays. In addition, a DNA sequence homologous to theTEF 1 box, found at approximately the same location within a Lycopersiconesculentum EF-1 alpha promoter, interacts with the same trans-acting factors.Homologies found between the A. thaliana and L. esculentum TEF 1 box sequenceshave allowed us to define mutations of this upstream element which affect theinteraction with the corresponding trans-acting factors. These results supportthe notion that the activation processes of A. thaliana EF-1 alpha genes havebeen conserved among angiosperms and provide interesting data on thefunctional structure of the TEF 1 box.
7                                                     NAL Call. No.: QK710.P68Active cdc2 genes and cell cycle phase-specific cdc2-related kinase complexesin hormone-stimulated alfalfa cells.Magyar, Z.; Bako, L.; Bogre, L.; Dedeoglu, D.; Kapros, T.; Dudits, D.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Jul.The plant journal v. 4 (1): p. 151-161; 1993 Jul.  Includes references.
Language:  English
Descriptors: Medicago sativa; Structural genes; Protein kinase; Transcription;Gene expression; Messenger  RNA; Cell suspensions; Mesophyll; Protoplasts;Roots; Genetic regulation; Cell division; 2,4-d; Naa; Zeatin riboside; Callus;Enzyme activity; Histones; Phosphorylation
8                                                      NAL Call. No.: 23 AU792The adaptation of Medicago polymorpha to a range of edaphic and environmentalconditions: effect of temperature on growth, and acidity stress on nodulationand nod gene induction.Loi, A.; Howieson, J.G.; Cocks, P.S.; Caredda, S.East Melbourne : Commonwealth Scientific and Industrial Research Organization;1993.Australian journal of experimental agriculture v. 33 (1): p. 25-30; 1993.Includes references.
Language:  English
Descriptors: Sardinia; Medicago polymorpha; Genotypes; Adaptation; Edaphicfactors; Environmental factors; Growth; Nodulation; Rhizobium meliloti; Geneexpression; Soil acidity; Stress
9                                                     NAL Call. No.: QK725.P54Agrobacterium tumefaciens-mediated beta-glucuronidase (GUS) gene expression inlentil (Lens culinaris Medik.) tissues.Warkentin, T.D.; McHughen, A.Berlin, W. Ger. : Springer International; 1992.Plant cell reports v. 11 (5/6): p. 274-278; 1992.  Includes references.
Language:  English
Descriptors: Lens culinaris; Beta-glucuronidase; Gene expression; Genetictransformation; Agrobacterium tumefaciens; Extracts; In vitro culture
Abstract:  Lentil (Lens culinaris Medik.) shoot apex, epicotyl, and rootexplants were capable of expressing an intron-containing beta-glucuronidase(GUS) gene after inoculation with the disarmed Agrobacterium strainGV2260:p35SGUSINT. Expression occurred at all wound sites on these explantsexcept at the end of the root explants proximal to the cotyledonary node. GUSexpression was detected using both histochemical and fluorescence assays andwas stable for at least nine days after inoculation for epicotyl and rootexplants, and for at least seventeen days for shoot apices. Non-inoculatedcontrols, or controls inoculated with an Agrobacterium strain lacking the GUSgene, did not produce any background blue staining in the histochemical assay.Expression levels for all lentil explants were substantially lower than forcomparable flax (Linum usitatissimum L.) explants which served as a positivecontrol.
10                                                    NAL Call. No.: QK725.P54Agrobacterium tumefaciens-mediated transformation of safflower (Carthamustinctorius L.) cv. 'Centennial'.Ying, M.C.; Dyer, W.E.; Bergman, J.W.Berlin, W. Ger. : Springer International; 1992.Plant cell reports v. 11 (11): p. 581-585; 1992.  Includes references.
Language:  English
Descriptors: Carthamus tinctorius; Agrobacterium tumefaciens; Genetictransformation; Explants; Callus; Regenerative ability; Shoots; Buds; Geneexpression; Beta-glucuronidase; Reporter genes; Culture media; Laboratorymethods
Abstract:  Efficient callus formation was achieved from cotyledon, stem, andleaf explants of the domestic safflower cultivar 'Centennial' on MS saltsmedium containing 1 mg/L BAP and 1 mg/L NAA. Shoot buds were regenerated from26% of leaf-derived calli on callus induction medium, although attempts toroot regenerated shoots were not successful. 'Centennial' explants inoculatedwith Agrobacterium tumefaciens containing NPT II and GUS genes producedkanamycin-resistant calli from which buds were regenerated. Transformation andstable integration of transgenes was confirmed by GUS assay and DNAhybridization in kanamycin-resistant calli, and GUS assay in regeneratedshoots.
11                                                    NAL Call. No.: QK710.P63Agrobacterium-mediated transformation of kenaf (Hibiscus cannabinus L.) withthe beta-glucuronidase (GUS) gene.Banks, S.W.; Gossett, D.R.; Lucas, M.C.; Milhollon, E.P.; LaCelle, M.G.Athens, Ga. : International Society for Plant Molecular Biology, University ofGeorgia; 1993 Jun.Plant molecular biology reporter - ISPMB v. 11 (2): p. 101-104; 1993 Jun.Includes references.
Language:  English
Descriptors: Hibiscus cannabinus; Agrobacterium; Genetic transformation; Genetransfer; Beta-glucuronidase; Genetic code; Tissue culture; Regenerativeability; Enzyme activity; Gene expression
12                                                   NAL Call. No.: QK725.P532Alfalfa cyclins: differential expression during the cell cycle and in plantorgans.Hirt, H.; Mink, M.; Pfosser, M.; Bogre, L.; Gyorgyey, J.; Jonak, C.; Gartner,A.; Dudits, D.; Heberle-Bors, E.Rockville, Md. : American Society of Plant Physiologists; 1992 Dec.The Plant cell v. 4 (12): p. 1531-1538; 1992 Dec.  Includes references.
Language:  English
Descriptors: Medicago sativa; Medicago varia; Structural genes; Dna; Plantproteins; Nucleotide sequences; Amino acid sequences; Gene expression;Messenger  RNA; Cell division; Leaves; Roots; Stems; Flowers; Buds
Abstract:  Cell division in eukaryotes is mediated by the action of themitosis promoting factor, which is composed of the CDC2 protein kinase and oneof the various mitotic cyclins. We have recently isolated a cdc2 gene fromalfalfa. Here, we report the isolation of two cyclin genes, cycMs1 and cycMs2,from alfalfa. The cycMs2 gene shows highest similarity to type B cyclins. Incontrast, the predicted amino acid sequence of the cycMs1 gene shows similarhomology scores to cyclins of all types (25 to 35%). Both genes are expressedin dividing suspension cultured cells but cease to be expressed when the cellsenter stationary phase. In synchronized alfalfa suspension cultured cells, themRNAs of cycMs1 and cycMs2 show maximal expression in the G2 and M phases.Transcripts of cycMs2 are found only in late G2 and M phase cells, anexpression pattern typical for cyclin B genes, whereas cycMs1 appears with theonset of G2. This pattern indicates that alfalfa cycMs1 and cycMs2 belong todifferent classes of cyclins. In young leaves, expression of both genes ishigh, whereas in mature leaves no transcripts can be detected, indicating thatthe two cyclin genes are true cell division markers at the mRNA level. Inother organs, a more complex expression pattern of the two cyclin genes wasfound.
13                                                    NAL Call. No.: QK710.P62Alfalfa root nodule phosphoenolpyruvate carboxylase: characterization of thecDNA and expression in effective and plant-controlled ineffective nodules.Pathirana, S.M.; Vance, C.P.; Miller, S.S.; Gantt, J.S.Dordrecht : Kluwer Academic Publishers; 1992 Nov.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (3): p. 437-450; 1992 Nov.Includes references.
Language:  English
Descriptors: Medicago sativa; Structural genes; Dna; Multigene families;Phosphoenolpyruvate carboxylase; Nucleotide sequences; Amino acid sequences;Gene expression; Root nodules; Genetic regulation; Enzyme activity; MessengerRNA
Abstract:  Phosphoenolpyruvate carboxylase (PEPC) plays a key role in N2fixation and ammonia assimilation in legume root nodules. The enzyme cancomprise up to 2% of the soluble protein in root nodules. We report here theisolation and characterization of a cDNA encoding the nodule-enhanced form ofPEPC. Initially, a 2945 bp partial-length cDNA was selected by screening aneffective alfalfa nodule cDNA library with antibodies prepared against rootnodule PEPC. The nucleotide sequence encoding the N-terminal region of theprotein was obtained by primer-extension cDNA synthesis and PCR amplification.The complete amino acid sequence of alfalfa PEPC was deduced from these cDNAsequences and shown to bear striking similarity to other plant PEPCs. Southernblots of alfalfa genomic DNA indicate that nodule PEPC is a member of a smallgene family. During the development of effective root nodules, nodule PEPCactivity increases to a level that is 10- to 15-fold greater than that in rootand leaf tissue. This increase appears to be the result of increases in amountof enzyme protein and PEPC mRNA. Ineffective nodules have substantially lessPEPC mRNA, enzyme protein and activity than do effective nodules. Maximumexpression of root nodule PEPC appears to be related to two signals. The firstsignal is associated with nodule initiation while the second signal isassociated with nodule effectiveness. Regulation of root nodule PEPC activitymay also involve post-translational processes affecting enzyme activity and/ordegradation.
14                                                    NAL Call. No.: 442.8 D49Altered morphology in transgenic tobacco plants that overproduce cytokinins inspecific tissues and organs.Li, Y.; Hagen, G.; Guilfoyle, T.J.Orlando, Fla. : Academic Press; 1992 Oct.Developmental biology v. 153 (2): p. 386-395; 1992 Oct.  Includes references.
Language:  English
Descriptors: Nicotiana tabacum; Cytokinins; Transgenics; Genetictransformation; Escherichia coli; Agrobacterium tumefaciens;Beta-glucuronidase; Reporter genes; Promoters; Genes; Gene expression; Plantmorphology; Plant development; Plant tissues; Plant organs; Histochemistry
Abstract:  An auxin-inducible bidirectional promoter from the soybean SAURgene locus was fused to a reporter gene in one direction and a cytokininbiosynthetic gene in the opposite direction and the expression of these fusedgenes was examined in transgenic tobacco. The Escherichia coli uidA gene,which encodes the enzyme beta-glucuronidase (GUS), was used as the reportergene and the Agrobacterium tumefaciens ipt gene, which encodes the enzymeisopentenyl transferase, was used as the cytokinin biosynthetic gene. Theseconstructs allowed the overproduction of cytokinins in tobacco in a tissueand organ-specific manner. Localized overproduction of cytokinins wasmonitored using the GUS reporter gene and measured by an ELISA assay. Thetissue- and organ-specific overproduction of cytokinins produced a number ofmorphological and physiological changes, including stunting, loss of apicaldominance, reduction in root initiation and growth, either acceleration orprolonged delayed senescence in leaves depending on the growth conditions,adventitious shoot formation from unwounded leaf veins and petioles, alterednutrient distribution, and abnormal tissue development in stems. While some ofthese morphological changes result directly from the localized overproductionof cytokinins, other changes probably result from the mobilization of plantnutrients to tissues rich in cytokinins.
15                                                     NAL Call. No.: 450 P692Appearance of new lipoxygenases in soybean cotyledons after germination andevidence for expression of a major new lipoxygenase gene.Kato, T.; Ohta, H.; Tanaka, K.; Shibata, D.Rockville, Md. : American Society of Plant Physiologists; 1992 Jan.Plant physiology v. 98 (1): p. 324-330; 1992 Jan.  Includes references.
Language:  English
Descriptors: Glycine max; Cotyledons; Plant composition; Lipoxygenase; Seedgermination; Genetic regulation; Gene expression; Genetic code; Amino acidsequences
Abstract:  The appearance and subsequent disappearance of lipoxygenaseactivity at pH 6.8 in germinated cotyledons of soybean (Glycine max [L.]) wasshown using a variant soybean cultivar (Kanto 101) that lacks the twolipoxygenase isozymes, L-2 and L-3, that are present in dry seeds of a normalsoybean cultivar (Enrei). Three new lipoxygenases, designated lipoxygenaseL-4, L-5, and L-6, were purified using anionic or cationic ion exchangechromatography. The major lipoxygenase in 5-day-old cotyledons of the variantsoybean was lipoxygenase L-4. Lipoxygenases L-5 and L-6 preferentiallyproduced 13(S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid (13S-HPOD) as areaction product of linoleic acid, whereas lipoxygenase L-4 produced both13S-HPOD and 9(S)-hydroperoxy-10(E),12(Z)-octadecadienoic acid. All threeisozymes have pH optima of 6.5, no activity at pH 9.0, and preferred linolenicacid to linoleic acid as a substrate. Partial amino acid sequencing oflipoxygenase L-4 showed that this isozyme shares amino acid sequence homologywith lipoxygenases L-1, L-2, and L-3 but is not identical to any of them. Thisindicates that a new lipoxygenase, L-4, is expressed in cotyledons.
16                                                    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).
17                                                     NAL Call. No.: QK710.A9Auxin-regulated transcription.Guilfoyle, T.J.; Hagen, G.; Li, Y.; Ulmasov, T.; Liu, Z.; Strabala, T.; Gee,M.Melbourne, Commonwealth Scientific and Industrial Research Organization; 1993.Australian journal of plant physiology v. 20 (4/5): p. 489-502; 1993.Includes references.
Language:  English
Descriptors: Arabidopsis; Glycine max; Auxins; Amino acid sequences;Beta-glucuronidase; Cytokinins; Gene expression; Messenger  RNA; Plantdevelopment; Plant physiology; Transcription
18                                                      NAL Call. No.: QK1.B38Bacterial-induced changes in plant form and function.Hirsch, A.M.; McKhann, H.I.; Lobler, M.Chicago, Ill. : University of Chicago Press; 1992 Sep.International journal of plant sciences v. 153 (3,pt.2): p. S171-S181; 1992Sep.  Paper presented at the "Katherine Esau Symposium on Plant Structure:Concepts, Connection and Challenges," March 28-31, 1992, Davis, California.Includes references.
Language:  English
Descriptors: Medicago sativa; Rhizobium meliloti; Agrobacterium tumefaciens;Roots; Root hairs; Root nodules; Nodulation; Cell differentiation; Nitrogenfixation; Gene expression; Meristems; Mutants; Recombinant  DNA; Genetictransformation
19                                                    NAL Call. No.: QK710.P68cdc2MsB, a cognate cdc2 gene from alfalfa, complements the G1/S but not theG2/M transition of budding yeast cdc28 mutants.Hirt, H.; Pay, A.; Bogre, L.; Meskiene, I.; Heberle-Bors, E.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Jul.The plant journal v. 4 (1): p. 61-69; 1993 Jul.  Includes references.
Language:  English
Descriptors: Medicago sativa; Saccharomyces cerevisiae; Complementary  DNA;Structural genes; Protein kinase; Nucleotide sequences; Amino acid sequences;Complementation; Mutants; Gene expression; Messenger  RNA; Cell division
20                                                    NAL Call. No.: QK710.P62cDNA sequence and expression of a phosphoenolpyruvate carboxylase gene fromsoybean.Sugimoto, T.; Kawasaki, T.; Kato, T.; Whittier, R.F.; Shibata, D.; Kawamura,Y.Dordrecht : Kluwer Academic Publishers; 1992 Nov.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (4): p. 743-747; 1992 Nov.Includes references.
Language:  English
Descriptors: Glycine max; Structural genes; Phosphoenolpyruvate carboxylase;Dna; Nucleotide sequences; Amino acid sequences; Gene expression; Leaves;Stems; Roots; Seeds; Messenger  RNA
Abstract:  A full-length cDNA encoding a subunit of phosphoenolpyruvatecarboxylase (PEPC) was isolated from a developing seed expression library ofthe C3 plant Glycine max. The corresponding mRNA is present at similar levelsin leaf, stem, root and developing seed. Two potential start codons exist, andthe activity of protein initiated from the first such codon could be subjectto regulation by protein kinase. Sequence comparison shows a similar upstreamstart codon in the case of the Ppc2 gene from Mesembryanthemum crystallinum,previously assumed to lack the sequences necessary for phosphorylation. Thesoybean encoded protein tends to resemble other 'C3-type' PEPC proteins moreclosely than those implicated in C4 or crassulacean acid metabolism.
21                                                     NAL Call. No.: 450 P692cDNA sequence, expression, and transcript stability of a coldacclimation-specific gene, cas18, of alfalfa (Medicago falcata) cells.Wolfraim, L.A.; Langis, R.; Tyson, H.; Dhindsa, R.S.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Apr.Plant physiology v. 101 (4): p. 1275-1282; 1993 Apr.  Includes references.
Language:  English
Descriptors: Medicago falcata; Complementary  DNA; Structural genes;Nucleotide sequences; Amino acid sequences; Plant proteins; Cold;Acclimatization; Gene expression; Messenger  RNA; Cell suspensions; Geneticregulation
Abstract:  The nucleotide sequence of a full-length cDNA, the deduced aminoacid sequence, and the regulation of expression of a cold acclimation-specificgene, cas18, in cell suspension cultures of a freezing-tolerant cultivar ofalfalfa (Medicago falcata cv Anik) have been determined. The deducedpolypeptide, CAS18, is relatively small (17.6 kD), is highly hydrophilic, isrich in glycine and threonine, and contains two distinctive repeat elements.It exhibits homology with members of the LEA/RAB/dehydrin family of proteins,which accumulate in response to abscisic acid (ABA) or water stress. It isintriguing that cas18 is induced by neither ABA nor water stress. The cas18cDNA hybridizes to three transcripts of 1.6, 1.4, and 1.0 kb, and the cDNAcharacterized here corresponds to the 1.0-kb transcript. The expression ofthis gene is about 30-fold greater in cold-acclimated cells than innonacclimated cells. Although the accumulation of transcripts during coldacclimation is relatively slow, their disappearance during deacclimation isdramatically rapid, becoming undetectable in less than 5 h. Studies of nuclearrun-on transcription show that cold acclimation enhances the transcription ofthis gene nearly 9-fold. The stability of cas18 -detectable transcripts duringdeacclimation is considerably increased if transcription is inhibited withcordycepin. It therefore appears that low temperature regulates the expressionof cas18 at both the transcriptional and posttranscriptional levels.
22                                                    NAL Call. No.: QK710.P62cDNA sequence of a sunflower oleosin and transcript tissue specificity.Cummins, I.; Murphy, D.J.Dordrecht : Kluwer Academic Publishers; 1992 Aug.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (5): p. 873-876; 1992 Aug.Includes references.
Language:  English
Descriptors: Helianthus annuus; Structural genes; Plant proteins; Nucleotidesequences; Amino acid sequences; Gene expression; Messenger  RNA; Plantembryos; Seeds
Abstract:  Oleosins (oil body membrane proteins) of 20.5 and 18 kDa have beenpurified from sunflower (Helianthus annuus) seeds and polyclonal antibodiesraised against them. The precipitated rabbit immunoglobulin fraction waspurified by affinity chromatography on cyanogen bromide-activated Sepharoseand specifically recognised polypeptides of 18 and 20.5 kDa in sunflowerhomogenate and oil body fractions assayed by western blotting. Anear-full-length cDNA clone was isolated for the 20.5 kDa oleosin. The 694 bpcDNA contained an open reading frame of 534 bp, followed by an untranslatedregion of 81 bp and a poly(A) region of 70 bp. The open reading frame encodeda polypeptide of 19.8 kDa. Study of transcript localisation revealed messageto be abundant in the embryo during the later stage of development and stillpresent in the dry seed. No signal was observed in RNA prepared from expandingleaves.
23                                                    NAL Call. No.: 450 J8224Changes in levels of gene trasncripts and their corresponding proteins innodules of soybean plants subjected to dark-induced stress.Gordon, A.J.; Ougham, H.J.; James, C.L.Oxford : Oxford University Press; 1993 Sep.Journal of experimental botany v. 44 (266): p. 1453-1460; 1993 Sep.  Includesreferences.
Language:  English
Descriptors: Glycine max; Messenger  RNA; Gene expression; Root nodules;Leghemoglobin; Glutamate-ammonia ligase; Sucrose synthase; Enzyme activity;Dark; Stress
Abstract:  Experiments were carried out to investigate the effects of stresson the levels and activities of key nodule proteins and the amounts of themRNAs encoding these proteins. Soybean plants, subjected to 3 d of continuousdarkness and then returned to the normal light/dark regime, were used as amodel system. Samples of nodules were taken during the stress/recovery cycleand total RNA and total soluble protein were extracted. The levels of mRNAsencoding leghaemoglobin (Lb), sucrose synthase (SS) and glutamine synthetase(GS) were estimated using Northern and slot blots. Within 24 h of completedarkness the levels of all three transcripts had fallen significantly (by 90%,70% and 50% for SS, Lb and GS mRNAs, respectively) and continued to declinefor the next 2 d of darkness. When the plants were returned to the normallight/dark regime, all transcript levels rapidly increased again. Thecorresponding proteins were analysed for biological activity (enzymeactivities in the cases of SS and GS, and haem content for Lb) and amount ofprotein (using Western blotting and specific antibodies raised against Lb, SSand GS). The amounts and activities of Lb and GS were unchanged, whilst thoseof SS declined significantly over the 3 d dark period and increased againduring the period following return to the normal light/dark regime. Neitherthe imposition of a 30 min light break each 24 h during the continuous darktreatments, nor the addition of 50 mol m-3 sucrose to the daily supply ofnutrients had any effect on the changes described.
24                                                  NAL Call. No.: SB732.6.M65Characterization of a chimeric cauliflower mosaic virus isolate that is moresevere and accumulates to higher concentrations than either of the strainsfrom which it was derived.Anderson, E.J.; Trese, A.T.; Sehgal, O.P.; Schoelz, J.E.St. Paul, Minn. : APS Press; 1992 Jan.Molecular plant-microbe interactions : MPMI v. 5 (1): p. 48-54; 1992 Jan.Includes references.
Language:  English
Descriptors: Brassica campestris var. rapa; Cauliflower mosaic caulimovirus;Strains; Strain differences; Virulence; Dwarfing; Symptoms; Chimeras;Phenotypes; Viral antigens; Genes; Gene expression; Dna; Rna; Geneticanalysis; Stability; Synergism; Molecular biology
25                                                    NAL Call. No.: QK710.P62Characterization of a Gy4 glycinin gene from soybean Glycine max cv. Forrest.Xue, Z.T.; Xu, X.L.; Shen, W.; Zhuang, N.L.; Hu, W.H.; Shen, S.C.Dordrecht : Kluwer Academic Publishers; 1992 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (5): p. 897-908; 1992 Mar.Includes references.
Language:  English
Descriptors: Glycine max; Multigene families; Plant proteins; Nucleotidesequences; Amino acid sequences; Molecular conformation; Exons; Introns;Cultivars; Transposable elements; Repetitive  DNA; Restriction mapping; Geneexpression; Messenger  RNA
Abstract:  The glycinin gene family encoding the glycinin subunits in soybeanplants is composed of at least five gene members. A genomic clone lambda S312containing the Gy4 gene from a genomic library of cv. Forrest was isolated andpartially characterized. The organization of this gene was found to be similarto that of a null allele from cv. Raiden, but different from the Gy4 gene fromcv. Dare. The complete nucleotide sequence of this gene has been determined.It is 2599 bp long consisting of four exons and three introns. Comparing theDNA sequences between this gene and the gene from Dare and a null allele fromRaiden, the difference found in the coding region was 5'-GCAGTGCAAG-3' (nt 824to 833) in the former case versus 5'-TGGAGTTGCAATT-3' (nt 1314 to 1326) in thelatter case in the exon 2 domain, resulting in three amino acid differencesand one amino acid absence. Some other differences were also found in thenon-coding region. The coding sequence and 5'-flanking region of the Gy4 gene,when compared with that of other legumin genes as well as group 1 glycininsubunit genes, revealed some interesting features: (1) a transposableelement-like sequence was found in the hypervariable region (HVR) of the exon3 domain, which was lacking in the legumin and the glycinin group 1 genes; (2)in the 5'-flanking region from nt -145 to -1, two high-homology sequences werefound: one from nt -141 to nt -132, the other from nt -118 to nt -92 whichincludes the 'legumin box' and the RY repeat element.
26                                                     NAL Call. No.: 450 P692Characterization of a novel protein induced by progressive or rapid droughtand salinity in Brassica napus leaves.Reviron, M.P.; Vartanian, N.; Sallantin, M.; Huet, J.C.; Pernollet, J.C.;Vienne, D. deRockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.Plant physiology v. 100 (3): p. 1486-1493; 1992 Nov.  Includes references.
Language:  English
Descriptors: Brassica napus var. oleifera; Plant proteins; Leaves; Waterstress; Drought; Salinity; Adaptation; Messenger  RNA; Gene expression; Waterdeficit; Amino acid sequences
Abstract:  Under progressive drought stress, Brassica napus displaysdifferential leaf modifications. The oldest leaves, developed before the onsetof water deficit, wilt gradually, whereas the youngest leaves harden.Hardening was distinguished by leaf turgor and bluish wax bloom when the shootwater potential was below -3 MPa and the leaf water saturation deficit wasabout 60%. This adaptive change was accompanied by modifications intwo-dimensional protein profiles. Ten percent of the polypeptides had alteredabundance or were unique to drought-stressed plants. Two-dimensional analysisof in vitro translation products did not reveal a general decrease in mRNApopulation. A 22-kD double polypeptide was increased by progressive or rapidwater stress and salinity and disappeared upon rehydration. These polypeptideshave a common N-terminal sequence, which does not reveal homology with anyknown water-stress protein but which contains the signature motif of soybeanKunitz trypsin inhibitors. Immunoprecipitation allowed these polypeptides tobe identified on two-dimensional gels of in vitro translation products. Theyappeared to be synthesized as a 24-kD precursor, and their transcript waspresent in the control well-watered leaves, where the polypeptides were neverdetected, indicating a possible translational regulation. A putative functionof this protein, named BnD22, in the retardation of drought-induced leafsenescence is discussed.
27                                                    NAL Call. No.: QK710.P68Characterization of a pollen-specific cDNA from sunflower encoding a zincfinger protein.Baltz, R.; Domon, C.; Pillay, D.T.N.; Steinmetz, A.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Sep.The plant journal v. 2 (5): p. 713-721; 1992 Sep.  Includes references.
Language:  English
Descriptors: Helianthus annuus; Complementary  DNA; Structural genes; Dnabinding proteins; Nucleotide sequences; Pollen; Amino acid sequences; Introns;Multigene families; Gene expression; Messenger  RNA; Zinc; Binding site
28                                                    NAL Call. No.: QK710.P62Characterization of a stress-induced, developmentally regulated gene familyfrom soybean.Crowell, D.N.; John, M.E.; Russell, D.; Amasino, R.M.Dordrecht : Kluwer Academic Publishers; 1992 Feb.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (3): p. 459-466; 1992 Feb.Includes references.
Language:  English
Descriptors: Glycine max; Multigene families; Plant proteins; Gene expression;Stress; Roots; Leaves; Seedlings; Senescence; Abiotic injuries; Nucleotidesequences; Amino acid sequences
Abstract:  We describe a family of stress-induced, developmentally regulatedsoybean genes for which cDNAs have been obtained from two different cultivars(Glycine max cv. Mandarin and Glycine max cv. Williams). The mRNAscorresponding to these cDNAs, called SAM22 and H4, respectively, accumulatepredominantly in the roots of soybean seedlings but are present at high levelsin the roots and leaves of mature plants. SAM22 accumulation is especiallydramatic in senescent leaves. In addition, SAM22 accumulation can be inducedin young leaves by wounding or by transpiration-mediated uptake of salicylicacid, methyl viologen, fungal elicitor, hydrogen peroxide or sodium phosphate(pH 6.9). Taken together, these data indicate that the genes corresponding toSAM22 and H4 are induced by various stresses and developmental cues. Southernblot analysis indicates that multiple copies of sequences related to SAM22exist in the soybean genome. We also show that the nucleotide sequences of thecDNAs corresponding to SAM22 and H4 are 86% identical at the nucleotide levelto each other and 70% identical at the amino acid level to the 'diseaseresistance response proteins' of Pisum sativum.
29                                                    NAL Call. No.: QK710.P68Characterization of GmENOD40, a gene showing novel patterns of cell-specificexpression during soybean nodule development.Yang, W.C.; Katinakis, P.; Hendriks, P.; Smolders, A.; Vries, F. de; Spee, J.;Kammen, A. van; Bisseling, T.; Franssen, H.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Apr.The plant journal v. 3 (4): p. 573-585; 1993 Apr.  Includes references.
Language:  English
Descriptors: Glycine max; Pisum sativum; Root nodules; Ontogeny; Geneticregulation; Genetic code; Nucleotide sequences; Gene expression; Roots; Celldivision; Developmental stages; Plant anatomy
30                                                     NAL Call. No.: QH426.C8Characterization of the Brassica campestris mitochondrial gene for subunit sixof NADH dehydrogenase: nad6 is present in the mitochondrion of a wide range offlowering plants.Nugent, J.M.; Palmer, J.D.Berlin ; New York : Springer-Verlag, 1979-; 1993.Current genetics v. 23 (2): p. 148-153; 1993.  Includes references.
Language:  English
Descriptors: Brassica campestris; Plants; Structural genes; Nadhdehydrogenase; Nucleotide sequences; Amino acid sequences; Mitochondrial  DNA;Rna editing; Transcription; Gene expression
Abstract:  We have isolated the Brassica campestris mitochondrial gene nad6,coding for subunit six of NADH dehydrogenase. The deduced amino-acid sequenceof this gene shows considerable similarity to mitochondrially encoded NAD6proteins of other organisms as well as to NAD6 proteins coded for by plantchloroplast DNAs. The B. campestris nad6 gene appears to lack introns andproduces an abundant transcript which is comparable in size to a previouslydescribed, unidentified transcript (#18) mapped to the B. campestrismitochondrial genome. An alignment of NAD6 proteins (deduced from DNAsequences) suggests that B. campestris nad6 transcripts are edited.Southern-blot hybridization indicates that nad6 is present in themitochondrial genome of all of a wide range of flowering plant speciesexamined.
31                                                    NAL Call. No.: QK710.P62Characterization of the soybean early nodulin cDNA clone GmENOD55.Blank, C. de; Mylona, P.; Yang, W.C.; Katinakis, P.; Bisseling, T.; Franssen,H.Dordrecht : Kluwer Academic Publishers; 1993 Sep.Plant molecular biology v. 22 (6): p. 1167-1171; 1993 Sep.  Includesreferences.
Language:  English
Descriptors: Glycine max; Complementary  DNA; Nodulins; Multigene families;Nucleotide sequences; Amino acid sequences; Gene expression; Geneticregulation; Nodulation; Bradyrhizobium japonicum; Rhizobium
Abstract:  Two cDNA clones of the soybean early nodulin GmENOD55 werecharacterized. These clones may represent two members of the soybean earlynodulin gene family GmENOD55. GmENOD55 has an N-terminal signal peptide and itcontains an internal domain consisting of proline and serine residues.Analyses of nodules lacking infection threads and intracellular bacteriasuggest that the GmENOD55 gene is first expressed after release ofBradyrhizobium japonicum in plant cells. This conclusion is supported by insitu hybridization studies showing that the expression is restricted to theinfected cell type.
32                                                     NAL Call. No.: 450 P693Chitinase and peroxidase in effective (fix+) and ineffective (fix-) soybeannodules.Staehelin, C.; Muller, J.; Mellor, R.B.; Wiemken, A.; Boller, T.Berlin : Springer-Verlag; 1992.Planta v. 187 (3): p. 295-300; 1992.  Includes references.
Language:  English
Descriptors: Glycine max; Bradyrhizobium japonicum; Cortex; Roots; Rootnodules; Plant composition; Chitinase; Peroxidase; Symbiosis; Diseaseresistance; Gene expression; Plant pathogens
Abstract:  Chitinase and peroxidase, two enzymes thought to be involved in thedefense of plants against pathogens, were measured in soybean (Glycine max L.Merr.) roots and in nodules colonized by Bradyrhizobium japonicum strainsdiffering in their symbiotic potential. Activities of both enzymes were higherin nodules than in roots. In "effective", nitrogen-fixing nodules, colonizedby wild-type bacteria, chitinase and peroxidase activities had low levels inthe central infected zone and were enhanced primarily in the nodule cortex. Anascorbate-specific peroxidase, possibly involved in radical scavenging, hadsimilarly high activities in the infected zone and in the cortex."Ineffective" nodules colonized by bacteria unable to fix nitrogensymbiotically showed a similar distribution of chitinase and peroxidase. Inanother type of "ineffective" nodule, colonized by a B. japonicum straineliciting a hypersensitive response, activities of both enzymes were enhancedto a similar degree in the infected zone as well as in the cortex. Tissueprints using a direct assay for peroxidase and an antiserum against beanchitinase corroborated these results. The antiserum against bean chitinasecross-reacted with a nodule protein of Mr 32 000; it inhibited most of thechitinase activity in the nodules but barely affected the chitinase inuninfected roots. It is concluded that proteins characteristic of the defensereaction accumulate in the cortex of nodules independently of their ability tofix nitrogen, and in the entire body of hypersensitively reacting nodules.
33                                                     NAL Call. No.: 450 P692Chlorophyll a/b-binding protein gene expression in cotton.Anderson, D.M.; Hudspeth, R.L.; Hobbs, S.L.; Grula, J.W.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul.Plant physiology v. 102(3): p. 1047-1048; 1993 Jul.  Includes references.
Language:  English
Descriptors: Gossypium hirsutum; Structural genes; Chlorophyll a/b bindingprotein; Gene expression; Messenger  RNA; Nucleotide sequences; Amino acidsequences; Leaves; Stems; Promoters; Recombinant  DNA; Reporter genes;Beta-glucuronidase; Histoenzymology
34                                                    NAL Call. No.: QK710.P62Chlorophyll a/b-binding protein genes are differentially expressed duringsoybean development.Chang, Y.C.; Walling, L.L.Dordrecht : Kluwer Academic Publishers; 1992 May.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (2): p. 217-230; 1992 May.Includes references.
Language:  English
Descriptors: Glycine max; Multigene families; Chlorophyll a/b binding protein;Structural genes; Transcription; Gene expression; Genetic regulation;Messenger  RNA; Embryogenesis; Plant development; Stems; Roots; Cotyledons;Ribulose-bisphosphate carboxylase
Abstract:  The levels of chlorophyll a/b-binding protein (Cab) gene polysomalpoly(A)+ mRNA were quantitated throughout the development of Glycine max L.Cab mRNAs were abundant in young expanding leaves, representing 6.1% of theleaf mRNA population. Lower Cab mRNA levels were present in embryos, stems,and cotyledons of developing seedlings; the lowest levels were found in rootswhere they accounted for 0.04% of the polysomal poly(A)+ mRNA of this organ.To determine the contribution of different members of the Cab gene family tothe Cab mRNA populations, a quantitative S1 nuclease reconstruction assay wasdeveloped. Cab3, Cab4, and Cab5 mRNAs were detected in all stages examinedduring soybean development but their levels underwent differential changes.Cab3 encodes the most abundant Cab mRNA in young leaves, developing embryos,and in Stage VII cotyledons from the developing soybean seedling. The levelsof Cab mRNAs were compared to the levels of ribulose-1,5-bisphosphatecarboxylase small subunit gene mRNA and differences in their patterns ofaccumulation were noted. Collectively these data indicate that during soybeanembryogenesis developmental control mechanisms supersede light-regulatorysignals.
35                                                    NAL Call. No.: QK710.P62Cis-acting regulatory regions of the soybean seed storage 11S globulin geneand their interactions with seed embryo factors.Itoh, Y.; Kitamura, Y.; Arahira, M.; Fukazawa, C.Dordrecht : Kluwer Academic Publishers; 1993 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (6): p. 973-984; 1993 Mar.Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Agrobacterium tumefaciens;Structural genes; Globulins; Seeds; Promoters; Deletions; Recombinant  DNA;Reporter genes; Beta-glucuronidase; Gene expression; Genetic regulation;Binding site; Dna binding proteins; Transgenic plants; Genetic transformation;Plant embryos; Embryogenesis
Abstract:  A 2.2 kb fragment containing the 5'-flanking region of the soybeanglycinin A2B1a gene and its successive deletions with a shorter 5'-flankingsequence were fused, in frame, to the beta-glucuronidase (GUS) reporter gene.The resultant fusions were introduced into tobacco plants via Agrobacteriumtumefaciens. Assays of the GUS activity in seeds of transgenic tobacco showedthat the upstream region, -657 to -327 (relative to the transcriptioninitiation site [ + 1 ]), of the glycinin gene is required for optimalexpression of the transformed gene. Interactions between embryo nuclearfactors and DNA fragments covering the downstream region of -326, in which areincluded the TATA box and legumin boxes, were not apparent. The embryo factorscapable of binding specifically to three subregions, -653 to -527, -526 to-422, and -427 to -321, of the upstream regulatory region were detected. Suchfactors appeared to be organ-specific and could be found solely in developingseeds at the early middle stage of embryogenesis (around 24 days afterflowering). Evidence obtained by characterizing the nature of the bindingproteins and by gel mobility shift assays established that the same factordoes interact with a consensus motif 5'-ATA/TATTTCN-/CTA-3' which occurs fourtimes in the cis-acting regulatory region between -657 and -327. Moreover,this conserved motif could also be found in the 5' regulatory region ofanother glycinin A1aB1b gene. Thus it is likely that the observed interactionbetween the nuclear factor and the conserved motifs would lead to activationof transcription from the glycinin genes in maturing soybean seeds.
36                                                    NAL Call. No.: QK710.P68Cis-analysis of a seed protein gene promoter: the conservative RY repeatCATGCATG within the legumin box is essential for tissue-specific expression ofa legumin gene.Baumlein, H.; Nagy, I.; Villarroel, R.; Inze, D.; Wobus, U.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1992Mar.The plant journal v. 2 (2): p. 233-239; 1992 Mar.  Includes references.
Language:  English
Descriptors: Vicia faba; Nicotiana tabacum; Seeds; Protein synthesis; Geneticregulation; Promoters; Gene expression; Legumin; Dna; Nucleotide sequences
37                                                    NAL Call. No.: QK710.P62Cloning and expression of an embryo-specific mRNA up-regulated in hydrateddormant seeds.Goldmark, P.J.; Curry, J.; Morris, C.F.; Walker-Simmons, M.K.Dordrecht : Kluwer Academic Publishers; 1992 Jun.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (3): p. 433-441; 1992 Jun.Includes references.
Language:  English
Descriptors: Bromus secalinus; Gene expression; Genetic regulation; MessengerRNA; Cloning; Nucleotide sequences; Amino acid sequences; Plant embryos;Seeds; Seed dormancy; Imbibition; Abscisic acid
Abstract:  Dormant seeds do not germinate when imbibed in water even whenconditions are favorable for germination. These hydrated seeds remain viable,but growth-arrested for weeks due to unknown restrictions within the embryo.As a model system for the study of the molecular processes occurring indormant seeds, we have chosen to examine gene expression in Bromus secalinas,a grass species that produces seeds with high levels of embryonic dormancy.Using differential screening for mRNAs present in hydrated dormant embryos, wehave identified a cDNA clone, pBS128, that encodes a mRNA transcript found inthe embryos of hydrated seeds of B. secalinus as well as in embryos frommature dry seeds. Striking differences in pBS128 transcript levels appear uponhydration of dormant and nondormant seeds. Upon imbibition pBS128 transcriptlevels increase over four-fold in dormant seeds, but rapidly decline anddisappear in nondormant seeds, which subsequently germinate. The pBS128transcript appears to be embryo-specific since the transcript is notdetectable in either non-stressed or dehydrated seedling tissue. Applicationof 50 micromolar ABA to nondormant seeds arrests germination and enhancespBS128 transcript levels. The nucleotide sequence of the nearly full-lengthpBS128 cDNA shows no homology to other reported genes, and the putativeprotein sequence does not exhibit the hydrophilic characteristics of theABA-responsive LEA (late embryogenesis abundant) proteins.
38                                                   NAL Call. No.: 448.3 Ar23The coat protein genes of squash mosaic virus: cloning, sequence analysis, andexpression in tobacco protoplasts.Hu, J.S.; Pang, S.Z.; Nagpala, P.G.; Siemieniak, D.R.; Slightom, J.L.;Gonsalves, D.Wien : Springer,; 1993.Archives of virology v. 130 (1/2): p. 17-31; 1993.  Includes references.
Language:  English
Descriptors: Squash mosaic comovirus; Coat proteins; Genes; Cloning; Aminoacid sequences; Nucleotide sequences; Dna sequencing; Gene expression;Tobacco; Protoplasts; In vitro
Abstract:  Complementary DNA of the middle-component RNA of the melon strainof squash mosaic comovirus (SqMV) was cloned. Clones containing the coatprotein genes were identified by hybridization with a degenerateoligonucleotide synthesized according to the amino acid sequence of a purifiedpeptide fragment of the SqMV large coat protein. A clone containing of 2.5 kbpcDNA insert of SqMV M-RNA was sequenced. The total insert sequence of 25 10 bpincluded a 2373 bp open reading frame (ORF) (encoding 791 amino acids), a 123bp 3'-untranslated region, and a poly(A) region. This ORF is capable ofencoding both the 42 and 22 k SqMV coat proteins. Direct N-terminal sequenceanalysis of the 22 k coat protein revealed its presence at the 3' end of thisORF and the position of the proteolytic cleavage site (Q/S) used to separatethe large and small coat proteins from each other. A putative location of theN-terminal proteolytic cleavage site of the 42 k coat protein (Q/N) waspredicted by comparisons with the corresponding coat proteins of cowpea mosaicvirus, red clover mottle virus, and bean-pod mottle virus. Although theavailable nucleotide sequences of these viruses revealed little similarity,their encoded coat proteins shared about 47% identity. The identity of theencoded 42 k and 22 k peptides was confirmed by engineering the respectiveregions for expression followed by transfer into tobacco protoplasts using thepolyethylene glycol method. Both SqMV coat proteins were expressed in vivo asdetermined by their reactivity to SqMV coat protein specific antibodies.
39                                                     NAL Call. No.: 450 P692Cold-induced changes in freezing tolerance, protein phosphorylation, and geneexpression: evidence for a role of calcium.Monroy, A.F.; Sarhan, F.; Dhindsa, R.S.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug.Plant physiology v. 102 (4): p. 1227-1235; 1993 Aug.  Includes references.
Language:  English
Descriptors: Medicago sativa; Freezing; Tolerance; Plant proteins;Phosphorylation; Regulation; Calcium ions; Cell suspensions; Phosphoproteins;Gene expression; Messenger  RNA; Cold; Acclimatization; Metabolic inhibitors;Enzyme inhibitors; Protein kinase
Abstract:  The role of Ca2+ in cold-induced changes in proteinphosphorylation, gene expression, and development of freezing tolerance hasbeen studied in cell-suspension cultures of a freezing-tolerant cultivar ofalfalfa (Medicago sativa spp. falcata cv Anik). Chemical treatments to blockCa2+ channels, antagonize calmodulin action, or inhibit protein kinasesmarkedly inhibited the cellular capacity to develop cold-induced freezingtolerance but had little effect on cell viability. An analysis ofphosphoprotein profile by two-dimensional polyacrylamide gel electrophoresisrevealed that at low temperature the relative level of phosphorylation ofseveral proteins increased, whereas that of several others decreased. Whencold acclimation was carried out in the presence ofN-(6-amino-hexyl)-5-chloro-1-naphthalene-sulfonamide hydrochloride, anantagonist of calmodulin and Ca2+-dependent protein kinases, or the Ca2+channel blocker La3+, the cold-induced changes in protein phosphorylation werestrongly inhibited, cells lost their capacity to develop freezing tolerance,and accumulation of transcripts of cold acclimation-specific genes wassubstantially reduced. An inhibitor of protein kinases,1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had lesspronounced effects on the cold-induced protein phosphorylation and caused onlya partial inhibition of the cold-induced development of freezing tolerance andaccumulation of the transcripts. The level of phosphorylation of one protein,of about 15 kD, increased more than 10-fold at low temperature and showed astrong positive correlation with cold-induced freezing tolerance and geneexpression even when the latter were altered with various chemical treatments.These results suggest that Ca and protein phosphorylation, or perhaps acoupling of the two, play an important role during the acquisition of freezingtolerance during cold acclimation.
40                                                     NAL Call. No.: 500 N21PCombination of H-box [CCTACC(N)7CT] and G-box (CACGTG) cis elements isnecessary for feed-forward stimulation of a chalcone synthase promoter by thephenylpropanoid-pathway intermediate p-coumaric acid.Loake, G.J.; Faktor, O.; Lamb, C.J.; Dixon, R.A.Washington, D.C. : The Academy; 1992 Oct01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 89 (19): p. 9230-9234; 1992 Oct01.  Includes references.
Language:  English
Descriptors: Medicago sativa; Phaseolus vulgaris; Gene expression; Geneticregulation; Growth promoters; Naringenin-chalcone synthase; Nucleotidesequences; P-coumaric acid
Abstract:  The phenylpropanoid pathway intermediate p-coumaric acid (4-CA)stimulated expression of the bean (Phaseolus vulgaris L.) chalcone synthase(malonyl-CoA:4-coumaroyl-CoA, EC 2.3.1.74) chs15 gene promoter inelectroporated protoplasts of alfalfa (Medicago sativa L.). We have analyzedthe effects of 5' deletions, mutations, and competition with promotersequences in trans on the expression of a chs15 promoter-chloramphenicolacetyltransferase gene fusion in elicited alfalfa protoplasts. Two distinctsequence elements, the H-box (consensus CCTACC(N)7CT) and the G-box (CACGTG),are required for stimulation of the chs15 promoter by 4-CA. Furthermore, a38-base-pair chs15 promoter sequence containing both cis elements conferredresponsiveness to 4-CA on the cauliflower mosaic virus 35S minimal promoter.The H-box and G-box in combination establish the complex developmental patternof chs15 expression and are also involved in stress induction. Hence,potential internal pathway regulation through feed-forward stimulation by 4-CAoperates by modulation of the signal pathways for developmental andenvironmental regulation.
41                                                    NAL Call. No.: QK710.P62A complex ensemble of cis-regulatory elements controls the expression of aVicia faba non-storage seed protein gene.Fiedler, U.; Filistein, R.; Wobus, U.; Baumlein, H.Dordrecht : Kluwer Academic Publishers; 1993 Jul.Plant molecular biology v. 22 (4): p. 669-679; 1993 Jul.  Includes references.
Language:  English
Descriptors: Vicia faba; Structural genes; Plant proteins; Seeds; Promoters;Deletions; Gene expression; Transcription; Genetic regulation; Genetictransformation; Transgenic plants; Reporter genes; Beta-glucuronidase;Histoenzymology; Nicotiana tabacum
Abstract:  We have identified cis-regulatory elements within the 5'-upstreamregion of a Vicia faba non-storage seed protein gene, called usp, by studyingthe expression of usp-promoter deletion fragments fused to reporter genes intransgenic tobacco seeds. 0.4 kb of usp upstream sequence contain at leastsix, but probably more, distinct cis-regulatory elements which are responsiblefor seemingly all quantitative, spatial and temporal aspects of expression.Expression-increasing and -decreasing elements are interspersed and include anAT-rich sequence, a G-box element and a CATGCATG motif. The latter acts as anegative element in contrast to what has been found for the same motif inlegumin- and vicilin-type seed storage protein gene promoters. Seedspecificity of expression is mainly determined by the -68/+51 region whichconfers, however, only very low levels of expression. The data support thecombinatorial model of promoter function.
42                                                     NAL Call. No.: QH426.C8Complex organization of the soybean mitochondrial genome: recombinationrepeats and multiple transcripts at the atpA loci.Chanut, F.A.; Grabau, E.A.; Gesteland, R.F.Berlin ; New York : Springer-Verlag, 1979-; 1993.Current genetics v. 23 (3): p. 234-247; 1993.  Includes references.
Language:  English
Descriptors: Glycine max; Loci; Structural genes; Plant proteins;Mitochondrial  DNA; Repetitive  DNA; Nucleotide sequences; Amino acidsequences; Pseudogenes; Restriction mapping; Mitochondrial genetics;Transcription; Gene expression; Messenger  RNA; Multiple genes; Homologousrecombination
Abstract:  Identification of the soybean mitochondrial atpA open reading frame(atpA ORF) was based on sequence similarity with atpA genes in other plantmitochondria and partial protein sequencing. The atpA reading frame ends withfour tandem UGA codons which overlap four tandem AUG codons initiating anunidentified reading frame, orf214. The atpA-orf214 region is found inmultiple sequence contexts in soybean mitochondrial DNA (mtDNA), which can beattributed to the presence of two recombination repeats. A 1-kb repeat spans600 nucleotides (nt) of atpa N-terminal coding region and 400 nt of upstreamsequence. Its four configurations correspond to two full-length atpA-orf214genes and two truncated pseudogenes. A 2-kb repeat lies 3 kb downstream fromthe 1-kb repeat. Restriction maps of cosmid clones suggest that a 10-kbsegment containing both repeats is itself duplicated in the mt genome. Withtwo recombination repeats present in a total of three copies per genome,soybean mtDNA is expected to consist of a complex population of subgenomicmolecules. Transcription of the atpa loci was analysed by Northern blottingand S1 nuclease protection. The atpA genes express multiple transcripts withone major 3' end and heterogeneous 5' sequences extending several kb upstreamof the atpA coding region. The atpa gene and orf214 are co-transcribed on allmajor transcripts. The pseudogenes do not express stable RNAs.
43                                                     NAL Call. No.: 381 B523Conserved histidine residues in soybean lipoxgenase: functional consequencesof their replacement.Steczko, J.; Donoho, G.P.; Clemens, J.C.; Dixon, J.E.; Axelrod, B.Washington, D.C. : American Chemical Society; 1992 Apr28.Biochemistry v. 31 (16): p. 4053-4057; 1992 Apr28.  Includes references.
Language:  English
Descriptors: Glycine max; Lipoxygenase; Histidine; Amino acid sequences;Mutations; Gene expression; Cloning; Enzyme activity; Binding site
Abstract:  Sequences of 13 lipoxygenases from various plant and mammalianspecies, thus far reported, display a motif of 38 amino acid residues whichincludes 5 conserved histidines and a 6th histidine about 160 residuesdownstream. These residues occur at positions 494, 499, 504, 522, 531, and 690in soybean lipoxygenase isozyme L-1. Since the participation of iron in thelipoxygenase reaction has been established and existing evidence based onMossbauer and EXAFS spectroscopy suggests that histidines may be involved iniron binding, the effect of the above residues has been examined in soybeanlipoxygenase L-1. Six singly mutated lipoxygenases have been produced in whicheach of the His residues has been replaced with glutamine. Two additionalmutants have been constructed wherein the codons for His-494 and His-504 havebeen replaced by serine codons. All of the mutant lipoxygenases, which wereobtained by expression in Escherichia coli, have mobilities identical to thatof the wild-type enzyme on denaturing gel electrophoresis and respond tolipoxygenase antibodies. The mutated proteins H499Q, H504Q, H504S, and H690Qare virtually inactive, while H522Q has about 1% of the wild-type activity.H494Q, H494S, and H531Q are about 37%, 8%, and 20% as active as the wild type,respectively. His-517 is conserved in the several lipoxygenase isozymes butnot in the animal isozymes. The mutant H517Q has about 33% of the wild-typeactivity. The inactive mutants, H499Q, H504Q, H504S, and H690Q, becomeinsoluble when heated for 3 min at 65 degrees C, as does H522Q. The othermutants and the wild-type are stable under these conditions. Although theessentiality of His-499, -504, and -690 is not proven, they are tentativelyconsidered to be prime candidates for iron ligands. Judgment on the role ofH-522 is more uncertain, since mutant H522Q has weak but detectable activity.The Km values of the active mutants and the wild-type L-1, when determinedagainst linoleic acid, differ only moder
44                                                     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.
45                                                    NAL Call. No.: QK710.P62Constitutive expression of the beta-phaseolin gene in different tissues oftransgenic alfalfa does not ensure phaseolin accumulation in non-seed tissue.Bagga, S.; Sutton, D.; Kemp, J.D.; Sengupta-Gopalan, C.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 951-958; 1992 Sep.Includes references.
Language:  English
Descriptors: Phaseolus vulgaris; Medicago sativa; Agrobacterium tumefaciens;Structural genes; Multigene families; Introns; Exons; Phaseolin; RecombinantDNA; Cauliflower mosaic caulimovirus; Promoters; Genetic transformation;Transgenics; Gene expression; Seeds; Roots; Root nodules; Leaves; Stems;Reporter genes; Phosphotransferases; Ligases
Abstract:  Phaseolin is a glycoprotein that constitutes the major storageprotein in bean seeds. The phaseolin gene promoters function in aseed-specific manner. In an attempt to understand if events followingtranscription of the gene also contribute to the seed-specific accumulation ofthe phaseolin protein, we studied the effect of substituting the constitutiveCaMV-35S promoter for the beta-phaseolin gene promoter on expression of thephaseolin gene in different plant organs. A chimeric gene consisting of the35S promoter, the coding sequence of the beta-phaseolin gene (all five intronsand six exons) and the 3'-flanking region of the beta-phaseolin gene, wasintroduced into alfalfa via Agrobacterium tumefaciens. While all organsexamined shared high levels of phaseolin transcripts, the only organ thatshowed significant accumulation of the phaseolin protein were the matureseeds. Co-migration of the major immunoreactive polypeptides from the non-seedorgans with the authentic beta-phaseolin polypeptides on SDS-PAGE indicatesthat the protein in non-seed organs undergoes correct post-translationalprocessing and modification, but are more unstable in a non-seed environment.
46                                                     NAL Call. No.: 450 P692Contrasting storage protein synthesis and messenger RNA accumulation duringdevelopment of zygotic and somatic embryos of alfalfa (Medicago sativa L.).Krochko, J.E.; Pramanik, S.K.; Bewley, J.D.Rockville, Md. : American Society of Plant Physiologists; 1992 May.Plant physiology v. 99 (1): p. 46-53; 1992 May.  Includes references.
Language:  English
Descriptors: Medicago sativa; Plant embryos; Somatic embryogenesis; Zygotes;Plant proteins; Protein synthesis; Genetic regulation; Messenger  RNA; Geneexpression; Seed development
Abstract:  During development on hormone-free media, somatic embryos passthrough distinct morphological stages that superficially resemble those ofzygotic embryo development (globular, heart, torpedo, cotyledonary stages).Despite these similarities, they differ from zygotic embryos in the extent ofcotyledonary development and the patterns of synthesis and quantitativeexpression of seed-specific storage proteins (7S, 11S, and 2S proteins). Alfin(7S) is the first storage protein synthesized in developing zygotic embryos(stage IV). The 11S (medicagin) and 2S (Low Molecular Weight, LMW) storageproteins are not detectable until the following stage of development (stageV), although all three are present before the completion of embryoenlargement. Likewise, the 7S storage protein is the first to be synthesizedin developing somatic embryos (day 5). Medicagin is evident by day 7 and theLMW protein by day 10. In contrast to zygotic embryos, alfin remains thepredominant storage protein in somatic embryos throughout development. Notonly are the relative amounts of medicagin and the LMW protein reduced insomatic embryos but the LMW protein is accumulated much later than the otherproteins. Quantification of the storage protein mRNAs (7S, 11 S, and 2S) bynorthern blot analysis confirms that there are substantial differences in thepatterns of message accumulation in zygotic and somatic embryos of alfalfa(Medicago sativa). In zygotic embryos, the 7S, 11S, and 2S storage proteinmRNAs are abundant during maturation and, in particular, during the stages ofmaximum protein synthesis (alfin, stages VI and VII; medicagin, stage VII;LMW, stage VII). In somatic embryos, the predominance of the 7S storageprotein is correlated with increased accumulation of its mRNA, whereas thelimited synthesis of the 11S storage protein is associated with much lowersteady-state levels of its message. The mRNA for the LMW protein is presentalready by 3 days after transfer to hormone-free medi
47                                                     NAL Call. No.: 450 P692Coregulation of soybean vegetative storage protein gene expression by methyljasmonate and soluble sugars.Mason, H.S.; DeWald, D.B.; Creelman, R.A.; Mullet, J.E.Rockville, Md. : American Society of Plant Physiologists; 1992 Mar.Plant physiology v. 98 (3): p. 859-867; 1992 Mar.  Includes references.
Language:  English
Descriptors: Glycine max; Protein synthesis; Gene expression; Regulation;Jasmonic acid; Sucrose; Messenger  RNA; Fructose; Glucose; Injuries;Photosynthesis
Abstract:  The soybean vegetative storage protein genes vspA and vspB arehighly expressed in developing leaves, stems, flowers, and pods as comparedwith roots, seeds, and mature leaves and stems. In this paper, we report thatphysiological levels of methyl jasmonate (MeJA) and soluble sugarssynergistically stimulate accumulation of vsp mRNAs. Treatment of excisedmature soybean (Glycine max Merr. cv Williams) leaves with 0.2 molar sucroseand 10 micromolar MeJA caused a large accumulation of vsp mRNAs, whereaslittle accumulation occurred when these compounds were supplied separately. Insoybean cell suspension cultures, the synergistic effect of sucrose and MeJAon the accumulation of vspB mRNA was maximal at 58 millimolar sucrose and wasobserved with fructose or glucose substituted for sucrose. In dark-grownsoybean seedlings, the highest levels of vsp mRNAs occurred in the hypocotylhook, which also contained high levels of MeJA and soluble sugars. Lowerlevels of vsp mRNAs, MeJA, and soluble sugars were found in the cotyledons,roots, and nongrowing regions of the stem. Wounding of mature soybean leavesinduced a large accumulation of vsp mRNAs when wounded plants were incubatedin the light. Wounded plants kept in the dark or illuminated plants sprayedwith dichlorophenyldimethylurea, an inhibitor of photosynthetic electrontransport showed a greatly reduced accumulation of vsp mRNAs. The time coursesfor the accumulation of vsp mRNAs induced by wounding or sucrose/MeJAtreatment were similar. These results strongly suggest that vsp expression iscoregulated by endogenous levels of MeJA (or jasmonic acid) and solublecarbohydrate during normal vegetative development and in wounded leaves.
48                                                  NAL Call. No.: 442.8 J8224Crystallization and preliminary X-ray crystallographic analysis of the soybeanproglycinin expressed in Escherichia coli.Utsumi, S.; Gidamis, A.B.; Mikami, B.; Kito, M.London ; New York : Academic Press, 1959-; 1993 Sep05.Journal of molecular biology v. 233 (1): p. 177-178; 1993 Sep05.  Includesreferences.
Language:  English
Descriptors: Glycine max; Globulins; Seeds; Precursors; X ray diffraction;Molecular conformation; Crystals; Crystallization; Recombinant  DNA; Geneexpression; Escherichia coli
Abstract:  Glycinin is one of the dominant storage proteins of soybean seeds.Soybean proglycinin expressed in Escherichia coli has been crystallized fromTris.HCl buffer (pH 7.6) by the dialysis equilibrium method. The crystalsbelong to the tetragonal system, Space group P41 or P43, with unit celldimensions of a=b=115.2 A, and c=147.1 A. The asymmetric unit contains threemolecules of proglycinin, with crystal volume per protein mass (Vm) of 3.05A(3)/Da and solvent content of 58.4% by volume. The crystals diffract X-raysto a resolution limit of at least 2.9 A and are resistant to X-ray radiationdamage. They appear to be suitable for X-ray structure analysis.
49                                               NAL Call. No.: QK725.P56 1993Cytoplasmic male sterility in sunflower.Smart, C.J.; Moneger, F.; Leaver, C.J.Weinheim ; New York : VCH; 1993.Plant mitochondria : with emphasis on RNA editing and cytoplasmic malesterility /. p. 403-410; 1993.  Includes references.
Language:  English
Descriptors: Helianthus annuus; Mitochondrial  DNA; Cytoplasmic malesterility; Mitochondrial genetics; Molecular mapping; Restriction mapping;Transcription; Gene expression
50                                                    NAL Call. No.: QK710.P62Cytoplasmic ribosomal protein S15a from Brassica napus: molecular cloning anddevelopmental expression in mitotically active tissues.Bonham-Smith, P.C.; Oancia, T.L.; Moloney, M.M.Dordrecht : Kluwer Academic Publishers; 1992 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (5): p. 909-919; 1992 Mar.Includes references.
Language:  English
Descriptors: Brassica napus; Multigene families; Ribosomes; Proteins; Cloning;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Leaves; Flowers; Buds; Apical meristems
Abstract:  We have isolated two cDNA clones which appear to encode the 40Sribosomal subunit protein S15a from Brassica napus (oilseed rape). The openreading frame in both clones contains 390 bases, encoding a deducedpolypeptide sequence of 130 amino acids (100% homology between clones) with76% sequence identity to the N-terminal 37 amino acids of the rat ribosomalprotein S15a and 80% identity to the S24 polypeptide of yeast. Both the yeastand rapeseed proteins have a net positive charge of + 9 and the rapeseed S15aprotein has a molecular mass of 14,778 Da compared to 14,762 Da for the yeastprotein. The rapeseed ribosomal protein S15a is encoded by a small multi-genefamily with at least two actively transcribed members. A single transcript ofca. 1.0 kb, corresponding to ribosomal protein S15a, is abundant in activelydividing tissues such as apical meristem, flower buds and young leaves andless abundant in mature stem and fully expanded leaves.
51                                                    NAL Call. No.: QK710.P62Deletion analysis and localization of SbPRP1, a soybean cell wall proteingene, in roots of transgenic tobacco and cowpea.Suzuki, H.; Fowler, T.J.; Tierney, M.L.Dordrecht : Kluwer Academic Publishers; 1993 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (1): p. 109-119; 1993 Jan.Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Vigna aconitifolia; Multigenefamilies; Structural genes; Promoters; Plant proteins; Cell wall components;Genetic transformation; Agrobacterium tumefaciens; Transgenics; Reportergenes; Beta-glucuronidase; Gene expression; Deletions; Histoenzymology; Roots;Epidermis; Agrobacterium rhizogenes; Messenger  RNA; Genetic regulation
Abstract:  SbPRP1 is a member of the soybean (Glycine max L. Merr)proline-rich cell wall protein family and is expressed at high levels in roottissue. To characterize the sequences required for this expression, we havefused 1.1 kb of upstream flanking DNA sequence from an SbBPRP1 genomic cloneto a gene encoding beta-glucuronidase (GUS). This construct was introducedinto tobacco using Agrobacterium tumefaciens-mediated transformation.Histochemical staining of GUS activity in transgenic tobacco indicated thatSbPRP1 is expressed in the apical and elongating region of both primary andlateral roots, most strongly in the epidermis. A similar localization patternwas found in transformed hairy roots when this construct was introduced intocowpea (Vigna aconitifolia) using Agrobacterium rhizogenes-mediatedtransformation. Nested 5'-deletion analysis of the SbPRP1 promoter indicatedthat a minimal promoter for SbPRP1 expression in roots is located within thefirst 262 bases of upstream flanking DNA and that the region between -1080 and-262 is required for maximal expression of this gene. Gel retardation assaysshowed that nuclear factors can be detected in soybean roots whichspecifically bind to sequences located between -1080 and -623, a region whichis needed for maximal expression of the SbPRP1 promoter. Northernhybridization analysis was also used to show that little SbPRP1 mRNA waspresent in roots during the first 24 h after imbibition. These studiesindicate that SbPRP1 expression is localized to the actively growing region ofthe root and that this expression is temporally regulated during very earlystages of seedling growth.
52                                                    NAL Call. No.: QK710.P62Developmental and environmental concurrent expression of sunflowerdry-seed-stored low-molecular-weight heat-shock protein and Lea mRNAs.Almoguera, C.; Jordano, J.Dordrecht : Kluwer Academic Publishers; 1992 Aug.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (5): p. 781-792; 1992 Aug.Includes references.
Language:  English
Descriptors: Helianthus annuus; Dna; Structural genes; Heat shock proteins;Plant proteins; Seeds; Plant embryos; Nucleotide sequences; Gene expression;Messenger  RNA; Seedlings; Embryogenesis; Genetic regulation; Abscisic acid;Osmotic pressure; Stress; Heat shock
Abstract:  We have cloned and sequenced three different cDNAs from sunflowerseed-stored mRNA. Sequence similarities and response to heat-shock identifiedone of the cDNAs a low-molecular-weight heat-shock protein (lmw-HSP). Theother two clones showed significant sequence similarity to the cotton andcarrot late-embryogenesis-abundant (Lea) proteins D-113 and Emb-1,respectively. The three cDNAs showed similar expression patterns duringzygotic embryo development, as well as in vegetative tissues of 3-day-oldseedlings in response to stress. Maximal accumulation of all three mRNAs wasdetected in dry seeds and during embryo mid-maturation stage, in the absenceof exogenous stress. In seedlings, mRNAs accumulated to lower levels inresponse to osmotic stress and exogenous abscisic acid (ABA) treatments. Adifferential time course of response to osmotic stress was observed: lmw-HSPmRNA accumulation was induced earlier than that of Lea mRNAs. The coordinateaccumulation of Lea and lmw-HSP transcripts during embryo development and inresponse to stress and ABA suggests the existence of common regulatoryelements for Lea and lmw-HSP genes, and supports the notion that HSPs mighthave alternative functions in the plant cell.
53                                                    NAL Call. No.: QK710.P62Differential expression of a chimeric CaMV-tomato proteinase Inhibitor I genein leaves of transformed nightshade, tobacco and alfalfa plants.Narvaez-Vasquez, J.; Orozco-Cardenas, M.L.; Ryan, C.A.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (6): p. 1149-1157; 1992 Dec.Includes references.
Language:  English
Descriptors: Lycopersicon esculentum; Solanum nigrum; Nicotiana tabacum;Medicago sativa; Transgenics; Genetic transformation; Structural genes;Proteinase inhibitors; Gene transfer; Gene expression; Recombinant  DNA;Promoters; Cauliflower mosaic caulimovirus; Messenger  RNA; Leaves; Flowers;Vacuoles; Immunoblotting
Abstract:  The open reading frame and terminator region of a wound-inducibletomato Inhibitor I gene, regulated by the CaMV 35S promoter, was stablyintegrated into the genomes of nightshade (Solanum nigrum), tobacco (Nicotianatabacum), and alfalfa (Medicago sativa), using an Agrobacterium-mediatedtransformation system. The expression of the foreign Inhibitor I gene inleaves of each species was studied at the mRNA and protein levels. The levelsof Inhibitor I protein present in leaves of each species correlated with thelevels of mRNA. The average levels of both mRNA and Inhibitor I protein werehighest in leaves of transgenic nightshade plants (over 125 micrograms ofInhibitor I per g tissue), less in tobacco plants (about 75 micrograms/gtissue), and lowest in leaves of transgenic alfalfa plants (below 20micrograms/g tissue). Inhibitor I protein was observed in all tissuesthroughout transgenic plant species, but inhibitor concentration per gram oftissue was 2-3 times higher in young developing leaf tissues and floralorgans. The differences in the expression of the CaMV-tomato Inhibitor I geneamong the different plant genera suggests that either the rate oftranscription of the foreign gene or the rate of degradation of the nascentInhibitor I mRNA varies among genera. Using electron microscopy techniques,the newly synthesized pre-pro-Inhibitor I protein was shown to be correctlyprocessed and stored as a mature Inhibitor I protein within the centralvacuoles of leaves of transgenic nightshade and alfalfa. The results of theseexperiments suggest that maximal expression of foreign proteinase inhibitorgenes, and perhaps other foreign defense genes, may require gene constructsthat are fashioned with promoters and terminators that allow maximumexpression in the selected plant species.
54                                                    NAL Call. No.: QK710.P62Differential expression of bean chitinase genes by virus infection, chemicaltreatment and UV irradiation.Margis-Pinheiro, M.; Martin, C.; Didierjean, L.; Burkard, G.Dordrecht : Kluwer Academic Publishers; 1993 Jul.Plant molecular biology v. 22 (4): p. 659-668; 1993 Jul.  Includes references.
Language:  English
Descriptors: Phaseolus vulgaris; Structural genes; Chitinase; Gene expression;Messenger  RNA; Leaves; Defense mechanisms; Genetic regulation; Alfalfa mosaicvirus; Infections; Ultraviolet radiation; Mercuric chloride; ComplementaryDNA; Nucleotide sequences; Amino acid sequences; Cloning
Abstract:  Three chitinases have been shown previously to be induced uponvarious stresses of bean leaves. Time course studies of mRNA accumulation oftwo of them (P3- and P4-chitinases) have been studied upon virus infection,mercuric chloride treatment and UV irradiation. In alfalfa mosaic virus(AlMV)-infected plants both mRNAs, absent in uninfected bean leaves, becomedetectable 36 h after inoculation. A maximum level of mRNAs is reached 84 hafter inoculation and, whereas the amount of P3-ch mRNA decreases soon afterhaving reached the maximum, the amount of P4-ch mRNA remains at high levelsfor several days. In mercuric chloride-treated leaves P4-ch mRNA becomesdetectable 1-1.5 h after onset of treatment and a maximum level is observedbetween 6 h and 24 h after treatment; P3-ch mRNA becomes detectable later thanP4-ch mRNA in treated leaves and reaches a maximum as late as 18 h aftertreatment has been applied. UV light also induces the synthesis of both mRNAsbut, here again, important differences are observed in the accumulation rateof the two transcripts. The relative amounts of each mRNA induced by thedifferent stresses have been compared. The most effective inducer of P3-chmRNA is AlMV. In contrast, mercuric chloride induces P4-ch mRNA moreefficiently than AlMV or UV light. We have also determined the completenucleotide sequence of the cDNA encoding P3-chitinase that has been isolatedfrom a cDNA library by using the cucumber lysozyme-chitinase cDNA as a probe.The 1072 bp P3-ch cDNA encodes a mature protein of 268 amino acid residues andthe 25 residue NH2-terminal signal peptide of the precursor. Because of itshigh structural homology to the cucumber and Arabidopsis acidic chitinases aswell as to the N-terminal amino acid sequence of the bifunctionallysozyme-chitinase from P. quinquifolia, bean P3-chitinase can be consideredto belong to the class III chitinases. Southern blot analysis of bean genomicDNA revealed that P3-chitinase is encoded by a single gene.
55                                                     NAL Call. No.: 450 P692Differential expression of histone H3 gene variants during cell cycle andsomatic embryogenesis in alfalfa.Kapros, T.; Bogre, L.; Nemeth, K.; Bako, L.; Gyorgyey, J.; Wu, S.C.; Dudits,D.Rockville, Md. : American Society of Plant Physiologists; 1992 Feb.Plant physiology v. 98 (2): p. 621-625; 1992 Feb.  Includes references.
Language:  English
Descriptors: Medicago sativa; Clones; Messenger  RNA; Gene expression;Histones; Genetic regulation; Somatic embryogenesis; Cell growth;Transcription
Abstract:  Northern analysis has revealed substantial differences in mRNAaccumulation of the two histone H3 gene variants represented by ph3c-1 andph3c-11 cDNA clones. Both in partially synchronized cell suspension culturesand in protoplast-derived cells from alfalfa, Medicago varia, the maximallevel of the histone H3-1 gene transcript coincided with the peak in[(3)H]thymidine incorporation. Histone H3-11 mRNA was detectable in cellsthroughout the period of the cell cycle studied. Various stress factors suchas medium replacement, enzyme digestion of the cell wall, osmotic shock, andauxin treatment considerably increased the level of the histone H3-11transcript. In alfalfa (Medicago sativa), the presence of H3-11 mRNA inunorganized tissues of microcallus suspension and in somatic embryos inducedby auxin treatment supports the idea that this H3 variant exists in acontinuously active state of transcription. During embryo development, theearly globular stage embryos showed increased accumulation of histone H3-11mRNA in comparison with the later stages. The highest level of the histoneH3-1 transcript was detectable 1 day after treatment of callus tissues with2,4-dichlorophenoxyacetic acid. Somatic embryos contained appreciable levelsof histone H3-1 transcripts at all stages of somatic embryo development. Theseobservations suggest that the histone H3-1 gene belongs to the class ofreplication-dependent histone genes. The histone H3-11 gene showedcharacteristics of a constitutively expressed replacement-type histone gene,with a specific characteristic that external factors can influence the levelof gene transcription.
56                                                    NAL Call. No.: QK725.P54Differential expression of two peanut peroxidase cDNA clones in peanut plantsand cells in suspension culture in response to stress.Breda, C.; Buffard, D.; Huystee, R.B. van; Esnault, R.Berlin, W. Ger. : Springer International; 1993.Plant cell reports v. 12 (5): p. 268-272; 1993.  Includes references.
Language:  English
Descriptors: Arachis hypogaea; Leaves; Stems; Roots; Cell suspensions; Stressresponse; Injuries; Ethylene; Gene expression; Peroxidase; Enzyme activity;Transcription; Genes
Abstract:  Peanut (Arachis hypogea L.) peroxidase gene expression was analyzedby measuring the accumulation of transcripts in cultured cells and variousplant parts (leaf, stem, root) and upon their treatment with ethylene orwounding, respectively. Two transcripts (prxPNC1 and prxPNC2) corresponding totwo peroxidase genes are expressed at higher levels in cultured cells ascompared to various plant organs. Analysis of total poly(A)+ RNA with anoligonucleotide probe corresponding to a highly conserved region of peroxidasegenes showed the expression of three peroxidase related sequences (1,000,1,400 or 2,600 bp) in stem or leaf but barely detectable in roots. The prxPNC2transcript transiently expressed at high levels in response to ethylenetreatment of cells or wounding of leaves. This suggests that the correspondinggene(s) are expressed in response to stress.
57                                                     NAL Call. No.: 450 P692Differential expression of two soybean (Glycine max L.) proline-rich proteingenes after wounding.Suzuki, H.; Wagner, T.; Tierney, M.L.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Apr.Plant physiology v. 101 (4): p. 1283-1287; 1993 Apr.  Includes references.
Language:  English
Descriptors: Glycine max; Structural genes; Plant proteins; Proline; Cell wallcomponents; Gene expression; Messenger  RNA; Abiotic injuries; Seedlings;Leaves; Multigene families; Hypocotyls; Roots; Iaa; Naa; 2,4-d
Abstract:  We have investigated the wound-induced expression of two members ofthe soybean (Glycine max L.) proline-rich cell wall protein gene family andshow that SbPRP1 and SbPRP2 exhibit unique patterns of expression afterphysical damage. SbPRP1 mRNA can be detected in the hook of soybean seedlingswithin 2 h after wounding and is present at high levels in the hook andelongating hypocotyl 20 h after wounding. In contrast, SbPRP2 mRNA increasestransiently and rapidly throughout the soybean seedling after wounding. SbPRP2is also induced by wounding in soybean leaves, but the pattern of mRNAaccumulation in leaves is distinct from that seen in seedlings and reacheshigh levels of expression 20 h after physical damage. SbPRP2 mRNA levels werealso found to increase in the mature hypocotyl and roots of seedlings inresponse to treatment with 10 micromolar indoleacetic acid andnaphthalene-1-acetic acid. These data indicate that the wound-inducedexpression of PRPs in soybean is tissue specific and that the regulation ofthese genes after physical damage may operate through different signaltransduction pathways.
58                                                     NAL Call. No.: 450 P692Differential expression within the glutamine synthetase gene family of themodel legume Medicago truncatula.Stanford, A.C.; Larsen, K.; Barker, D.G.; Cullimore, J.V.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Sep.Plant physiology v. 103 (1): p. 73-81; 1993 Sep.  Includes references.
Language:  English
Descriptors: Medicago truncatula; Gene expression; Genetic code; Nucleicacids; Plant development
Abstract:  The glutamine synthetase (GS) gene family of Medicago truncatulaGaertn. contains three genes related to cytosolic GS (MtGSa, MtGSb, andMtGSc), although one of these (MtGSc) appears not to be expressed. Sequenceanalysis suggests that the genes are more highly conserved interspecificallyrather than intraspecifically: MtGSa and MtGSb are more similar to theirhomologs in Medicago sativa and Pisum sativum than to each other. Studies inwhich gene-specific probes are used show that both MtGSa and MtGSb are inducedduring symbiotic root nodule development, although not coordinately. MtGSa isthe most highly expressed GS gene in nodules but is also expressed to lowerextents in a variety of other organs. MtGSb shows higher levels of expressionin roots and the photosynthetic cotyledons of seedlings than in nodules orother organs. In roots, both genes are expressed in the absence of anexogenous nitrogen source. However the addition of nitrate leads to ashort-term, 2- to 3-fold increase in the abundance of both mRNAs, and theaddition of ammonium leads to a 2-fold increase in MtGSb mRNA. The nitrogensupply, therefore, influences the expression of the two genes in roots, but itis clearly not the major effector of their expression. In the discussionsection, the expression of the GS gene family of the model legume M.truncatula is compared to those of other leguminous plants.
59                                                   NAL Call. No.: QK725.P532Dissection of the functional architecture of a plant defense gene promoterusing a homologous in vitro transcription initiation system.Arias, J.A.; Dixon, R.A.; Lamb, C.J.Rockville, Md. : American Society of Plant Physiologists; 1993 Apr.The Plant cell v. 5 (4): p. 485-496; 1993 Apr.  Includes references.
Language:  English
Descriptors: Glycine max; Phaseolus vulgaris; Nicotiana tabacum; Promoters;Naringenin-chalcone synthase; Multigene families; Molecular mapping;Transcription; Gene expression; Genetic regulation; In vitro
Abstract:  CHS15 is one of a family of bean genes encoding chalcone synthase,which catalyzes the first reaction in a branch pathway of phenylpropanoidbiosynthesis for the production of flavonoid pigments and UV protectants andisoflavonoid-derived phytoalexins. The functional architecture of the CHS15promoter was dissected by a novel homologous plant in vitro transcriptioninitiation system in which whole-cell and nuclear extracts fromsuspension-cultured soybean cells direct accurate and efficient RNA polymeraseII-mediated transcription from an immobilized promoter template. Authentictranscription from the CHS15 promoter template was also observed withwhole-cell extracts from suspension-cultured cells of bean, tobacco, and themonocot rice, and the soybean whole-cell extract transcribed several otherimmobilized promoter templates. Hence, this procedure may be of general use inthe study of plant gene regulation mechanisms in vitro. Assay of the effectsof depletion of the soybean whole-cell extract by preincubation with smallregions of the CHS15 promoter or defined cis elements showed that transfactors that bind to G-box (CACGTG, -74 to -69) and H-box (CCTACC, -61 to -56and -121 to -126) cis elements, respectively, make major contributions to thetranscription of the CHS15 promoter in vitro. Both cis element/trans factorinteractions in combination are required for maximal activity. Delineation ofthese functional cis element/trans factor interactions in vitro provides thebasis for study of the mechanisms underlying developmental expression of CHS15in pigmented petal cells established by G-box and H-box combinatorialinteractions, and for characterization of the terminal steps of the signalpathway for stress induction of the phytoalexin defense response.
60                                                   NAL Call. No.: QK725.P532Downstream DNA sequences are required to activate a gene expressed in the rootcortex of embryos and seedlings.Dietrich, R.A.; Radke, S.E.; Harada, J.J.Rockville, Md. : American Society of Plant Physiologists; 1992 Nov.The Plant cell v. 4 (11): p. 1371-1382; 1992 Nov.  Includes references.
Language:  English
Descriptors: Brassica napus; Structural genes; Controlling elements; Roots;Cortex; Plant embryos; Seedlings; Genetic regulation; Gene expression; Celldifferentiation; Root meristems; Recombinant  DNA; Beta-glucuronidase;Reporter genes; Transgenics; Genetic transformation; Embryogenesis
Abstract:  We showed previously that a gene, designated AX92, which isexpressed at an early stage of cortex differentiation in the root apex ofoilseed rape seedlings, is also expressed in embryos. To compare AX92 generegulation during embryo-genesis and postembryonic growth, we constructed achimeric gene consisting of AX92 5'and 3' untranslated and flanking regionsfused with a beta-glucuronidase protein coding region. We showed that thechimeric gene is active in both developing cortex cells in the root apicalmeristems of transgenic oilseed rape seedlings and in cortex cells at the rootend of embryonic axes. To determine whether the AX92 gene is regulated by acommon mechanism in embryos and seedlings, we analyzed the expression ofmodified chimeric genes. We showed that the AX92 chimeric gene is regulatedcombinatorially and that DNA sequences located 3' of the protein coding regionare necessary for its activation in the root cortex of both embryos andseedlings. Our results suggest that common regulatory sequences are requiredto activate the gene in the embryonic and postembryonic root cortex.
61                                                     NAL Call. No.: 450 Am36Duplicate gene expression for isocitrate dehydrogenase and 6-phosphogluconatedehydrogenase in diploid species of Eleusine (Gramineae).Werth, C.R.; Hilu, K.; Langner, C.A.; Baird, W.V.Columbus, Ohio : Botanical Society of America; 1993 Jun.American journal of botany v. 80 (6): p. 705-710; 1993 Jun.  Includesreferences.
Language:  English
Descriptors: Eleusine; Plant composition; Isocitrate dehydrogenase;Phosphogluconate dehydrogenase; Isoenzymes; Genetic regulation; Geneexpression; Phenotypes; Alleles; Genetic variation; Diploidy; Genetic code;Genetic analysis
Abstract:  In the course of a survey of isozyme variation in the grass genusEleusine, complex band patterns were observed for the enzymes isocitratedehydrogenase (IDH) and 6-phosphogluconate dehydrogenase (6PGD). Thesepatterns were interpreted as the result of duplicate expression for one of thetwo genes that ordinarily codes subcellularly compartmentalized forms of eachof these enzymes. The interpretation of IDH phenotypes was facilitated byintraspecific allelic variation at one of the putatively duplicated genes(Idh-2), and was verified by examining phenotype ratios in progeny arrays fromselfed heterozygotes of E. indica. The lack of analogous intraspecificvariation for 6PGD precluded genetic tests, but the duplicate nature ofexpression was supported by interspecific patterns of variation. Four out ofthe five diploid species of Eleusine studied (E. indica, E. jaegeri, E.multiflora, E. tristachya) exhibited both duplications; E. floccifoliaappeared to lack the IDH duplication, but possessed the 6PGD duplication. Bothenzymes showed evidence of hyperduplication in the tetraploid species E.coracana.
62                                                     NAL Call. No.: 450 P692Effect of brassinolide on gene expression in elongating soybean epicotyls.Clouse, S.D.; Zurek, D.M.; McMorris, T.C.; Baker, M.E.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.Plant physiology v. 100 (3): p. 1377-1383; 1992 Nov.  Includes references.
Language:  English
Descriptors: Glycine max; Gene expression; Genes; Genetic regulation;Brassinolide; 2,4-d; Epicotyls; Length; Seedling growth; Transcription;Messenger  RNA
Abstract:  We have studied the effect of brassinolide (BR), a plant steroidallactone, on the expression of auxin-regulated genes in soybean (Glycine max L.cv Williams 82) epicotyls. BR caused up to 4-fold increases in epicotyl lengthduring extended assays at 10-7 M, in the absence of added auxin. Structurallyrelated steroids failed to induce elongation or to alter the BR effect.Northern blot analysis, using sequences corresponding to auxin-regulated genesas probes, has shown that the molecular mechanism of BR-induced elongation islikely to differ from that of auxin-induced elongation in this system. BR doesnot rapidly induce members of the GH, SAUR, or JCW auxin-inducible genefamilies before the onset of elongation. BR enhances SAUR and GH1 transcriptsafter 18 h but has no effect on JCW1 or GH3 transcripts at any time examined.We have shown by two-dimensional gel analysis of in vitro translated mRNA thata submicromolar concentration of BR alters the pattern of gene expression inelongating soybean epicotyls.
63                                                    NAL Call. No.: 381 J8223Effects of deletion of disulfide bonds by protein engineering on theconformation and functional properties of soybean proglycinin.Utsumi, S.; Gidamis, A.B.; Kanamori, J.; Kang, I.J.; Kito, M.Washington, D.C. : American Chemical Society; 1993 Apr.Journal of agricultural and food chemistry v. 41 (4): p. 687-691; 1993 Apr.Includes references.
Language:  English
Descriptors: Glycine max; Targeted mutagenesis; Plant proteins; Precursors;Genetic transformation; Gene transfer; Gene expression; Escherichia coli;Induced mutations; Deletions; Cysteine; Gelation; Gels; Sulfhydryl groups
Abstract:  Glycinin, one of the dominant storage proteins of soybean seeds,has two disulfide bonds in subunit: Cys12-Cys45 and Cys88-Cys298 in theproglycinin A(1a)B(1b) subunit. To examine the effects of disrupting disulfidebonds on the formation and maintenance of structure and on the functionalproperties of proglycinin, we replaced the cysteine residues (Cys12 and Cys88)by oligonucleotide-directed mutagenesis, giving mutant proglycinins Gly12,Ser88 and Gly12Ser88. The mutant proglycinins overproduced in Escherichia colicells accumulated as soluble proteins and self-assembled into trimers like thenative proglycinin. The functional properties of proglycinins Gly12 and Ser88purified to near homogeneity were examined as models of modified glycinins.Proglycinin Ser88 formed a harder gel than native glycinin and unmodifiedexpressed proglycinin even at the protein concentrations at which nativeglycinin did not form a hard gel. On the other hand, proglycinin Gly12 formeda gel only at higher protein concentrations (>6%), the hardness of which wassimilar to that of the native glycinin. Both proglycinins Gly12 and Ser88exhibited emulsifying activity similar to that of unmodified expressedproglycinin. These results suggest that the number and topology of freesulfhydryl residues are closely related to the heat-induced gel-formingability and the gel properties of glycinin but not to its emulsification.
64                                                     NAL Call. No.: 450 P692Effects of sulfur nutrition on expression of the soybean seed storage proteingenes in transgenic petunia.Fujiwara, T.; Hirai, M.Y.; Chino, M.; Komeda, Y.; Naito, S.Rockville, Md. : American Society of Plant Physiologists; 1992 May.Plant physiology v. 99 (1): p. 263-268; 1992 May.  Includes references.
Language:  English
Descriptors: Petunia; Glycine max; Gene transfer; Transgenics; Geneexpression; Seeds; Protein synthesis; Sulfur; Nutrient requirements; Geneticregulation; Methionine
Abstract:  The 7S seed storage protein (beta-conglycinin) of soybean (Glycinemax [L]. Merr.) has three major subunits; alpha, alpha', and beta.Accumulation of the beta-subunit, but not the alpha- and alpha-subunits, hasbeen shown to be repressed by exogenously applied methionine to the immaturecotyledon culture system (LP Holowach, JF Thompson, JT Madison [1984] PlantPhysiol 74: 576-583) and to be enhanced under sulfate deficiency in soybeanplants (KR Gayler, GE Sykes [1985] Plant Physiol 78: 582-586). Transgenicpetunia (Petunia hybrida) harboring either the alpha'- or beta-subunit genewere constructed to test whether the patterns of differential expression wereretained in petunia. Petunia regulates these genes in a similar way as soybeanin response to sulfur nutritional stimuli, i.e. (a) expression of thebeta-subunit gene is repressed by exogenous methionine in in vitro culturedseeds, whereas the alpha'-subunit gene expression is not affected; and (b)accumulation of the beta-subunit is enhanced by sulfur deficiency. The patternof accumulation of major seed storage protein of petunia was not affected bythese treatments. These results indicate that this mechanism of generegulation in response to sulfur nutrition is conserved in petunia even thoughit is not used to regulate its own major seed storage proteins.
65                                                    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.
66                                                  NAL Call. No.: SB732.6.M65ENOD8, a novel early nodule-specific gene, is expressed in empty alfalfanodules.Dickstein, R.; Prusty, R.; Peng, T.; Ngo, W.; Smith, M.E.St. Paul, MN : APS Press, [c1987-; 1993 Nov.Molecular plant-microbe interactions : MPMI v. 6 (6): p. 715-721; 1993 Nov.Includes references.
Language:  English
Descriptors: Medicago sativa; Rhizobium meliloti; Complementary  DNA;Structural genes; Nodulins; Nucleotide sequences; Amino acid sequences;Messenger  RNA; Gene expression; Root nodules; Nodulation; Mutants
67                                                     NAL Call. No.: 450 P692Expression and accumulation patterns of nitrogen-responsive lipoxygenase insoybeans.Grimes, H.D.; Tranbarger, T.J.; Franceschi, V.R.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Oct.Plant physiology v. 103 (2): p. 457-466; 1993 Oct.  Includes references.
Language:  English
Descriptors: Glycine max; Lipoxygenase; Enzyme activity; Genetic regulation;Gene expression; Nitrogen; Nutrient availability; Protein synthesis; Messenger RNA; Protein content; Plant composition; Life cycle; Nutrient deficiencies;Amino acids
Abstract:  Gene expression and protein accumulation patterns ofnitrogen-responsive lipoxygenase (LOX-NR), as a representative vegetativestorage protein, were investigated in nonnodulated soybeans (Glycine max [L.]Merr. cv Wye). The form of available nitrogen (supplied as NH4NO3, NH4+,NO3(-1), or urea) influenced the mRNA level and the amount of LOX protein,indicating that preferential accumulation of LOX may occur. Soybeans weregrown with 0, 2, 5, and 16 mM total nitrogen to determine the extent to whichLOX accumulation responded to soil nitrogen levels. Analysis of both mRNA andprotein levels was conducted in shoot tips, stems, pod walls, and leaves overthe entire life cycle of the plant. A general correlation between increasingavailable nitrogen level and LOX level was seen in the shoot tip and otherorgans throughout the soybean life cycle. However, appreciable amounts ofLOX-NR mRNA and protein accumulated even when plants were grown underconditions of nitrogen deficiency. The results indicate that LOX may play animportant role as a temporary storage site for amino acids in the developingshoot tip. The expression patterns of LOX-NR in plants grown under nitrogendeficiency suggest that these proteins, although responsive to nitrogenstatus, may not function solely as temporary storage pools for amino acids.
68                                                     NAL Call. No.: 381 J824Expression and characterization of the N-terminal doma in of an oleosinprotein from sunflower.Li, M.; Keddie, J.S.; Smith, L.J.; Clark, D.C.; Murphy, D.J.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993Aug15.The Journal of biological chemistry v. 268 (23): p. 17504-17512; 1993 Aug15.Includes references.
Language:  English
Descriptors: Helianthus annuus; Plant proteins; Lipid bodies; Molecularconformation; Recombinant  DNA; Gene transfer; Gene expression; Escherichiacoli
Abstract:  Oil bodies of plant seeds contain a triacylglycerol matrixsurrounded by a monolayer of phospholipids embedded with alkaline proteinstermed oleosins. Although oleosins are amphipathic proteins, they are unlikebilayer membrane proteins since they are associated with a single lipid:waterinterface at the oil body surface. Oleosins are unusual proteins because theycontain a 70-80-residue uninterrupted nonpolar domain, flanked by relativepolar C- and N-terminal domains. In the present study, we report theexpression of the N-terminal domain of the 18-kDa oleosin isoform fromsunflower as a recombinant fusion protein in Escherichia coli and thedetermination of its secondary structure using CD and Fourier transforminfrared spectroscopy either as a purified but partially denatured peptide orreconstituted into liposomes. The structure derived from physical studies wasthen compared and assigned with those predicted from analysis of the primarysequence of the N-terminal domain. Based on data derived from CD spectroscopyanalysis of purified and partially renatured N-terminal polypeptide, itcontains about 10% alpha-helical structure, 20-30% beta-strand structure,approximately 8% beta-turn structure, and 60% random coil structure. However,analysis of the polypeptide reconstituted into liposomes showed an increasedcontent of alpha-helical structure to about 20% and an increased beta-strandstructure content to about 30-40%. Data derived from Fourier transforminfrared spectroscopy studies and compared with the data predicted from theprimary sequence showed the peptide is well structured with some antiparallelbeta-strand structure from residues 2-9, parallel beta-strand structure fromresidues 30-37 and/or 42-49, and alpha-helical structure from residues 10-23and/or 43-49. There is potential amphipathic alpha-helix from residues 10-23.Based on these results, the following model for the secondary structure of theN-terminal domain of sunflower oleosin can be proposed. Residues 2-9 wouldproduce amphipathic antiparallel beta-strand structure. Residues 10-23 wouldproduce an amphipathic alpha-helical structure. Residues 30-37 and/or 42-49would give parallel beta-strand structure, or residues 42-49 could form anonpolar alpha-helical structure that would insert into the oil matrix.
69                                                      NAL Call. No.: 381 AR2Expression cloning in Escherichia coli and preparative isolation of thereductase coacting with chalcone synthase during the key step in thebiosynthesis of soybean phytoalexins.Welle, R.; Schroder, J.Orlando, Fla. : Academic Press; 1992 Mar.Archives of biochemistry and biophysics v. 293 (2): p. 377-381; 1992 Mar.Includes references.
Language:  English
Descriptors: Glycine max; Phytoalexins; Biosynthesis; Naringenin-chalconesynthase; Oxidoreductases; Dna; Cloning; Transformation; Gene expression;Genetic engineering; Purification; Enzyme activity
Abstract:  The cDNA for the reductase involved in the biosynthesis of6'-deoxychalcone (4,2',4'-trihydroxychalcone), the first specific intermediatein the pathway to soybean phytoalexins, was cloned into the expression vectorpKK233-2 and transformed into Escherichia coli. Using this source, about 5 mgof homogeneous reductase was isolated from 45 g of cells. The proteinpurification protocol differs completely from the scheme applied to soybeancell cultures. Size, N-terminal and specific enzyme activities were identicalfor the plant and E. coli protein. The pure protein is fairly stable,retaining 70% of initial activity after storage at 5 degrees C during 4 weeks.This protein is used for crystallization and in the study of itsprotein-protein interaction with chalcone synthase.
70                                                  NAL Call. No.: QD415.A1B58Expression of auxin-responsive genes in soybean and transgenic tobacco.Guilfoyle, T.J.; Hagen, G.; Li, Y.; Gee, M.A.; Ulmasov, T.N.; Martin, G.London : Portland Press; 1992 Feb.Transactions - Biochemical Society v. 20 (1): p. 97-101; 1992 Feb.  Includesreferences.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Transgenics; Auxins
71                                                    NAL Call. No.: QK827.S48Expression of S-locus glycoprotein genes from Brassica oleracea and B.campestris in transgenic plants of self-compatible B. napus cv Westar.Nishio, T.; Toriyama, K.; Sato, T.; Kandasamy, M.K.; Paolillo, D.J.;Nasrallah, J.B.; Nasrallah, M.E.Heidelberg : Springer International; 1992.Sexual plant reproduction v. 5 (2): p. 101-109; 1992.  Includes references.
Language:  English
Descriptors: Brassica oleracea; Brassica campestris; Brassica napus;Agrobacterium tumefaciens; Genetic transformation; Transgenics; Geneexpression; Self compatibility; Self incompatibility; Glycoproteins; Proteinsynthesis; Genetic regulation; Immunocytochemistry; Cell ultrastructure;Spatial distribution; Genes
72                                                     NAL Call. No.: 450 P699Expression of soybean seed storage protein genes in transgenic plants; theireffects on expression of a neighboring gene and position dependency.Fujiwara, T.; Beachy, R.N.Kyoto : Japanese Society of Plant Physiologists; 1993 Jan.Plant and cell physiology v. 34 (1): p. 13-20; 1993 Jan.  Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Agrobacterium; Genetictransformation; Transgenic plants; Gene expression; Seeds; Plant proteins;Genes; Reporter genes; Beta-glucuronidase; Enzyme activity
Abstract:  The beta-conglycinin genes, which encode the 7S seed storageproteins of soybean, were previously shown to be relatively independent of"position effects" in transgenic plants, i.e., expression levels of the(alpha)' and beta subunit genes of beta-conglycinin were relatively consistenton a per gene basis compared with other plant genes. We tested whether thepromoter region of the (alpha)' subunit gene confers position independency byintroducing a fusion gene comprised of the (alpha)' subunit promoter and theuidA (encoding beta-glucuronidase) coding sequence and found that theresultant gene lost its position independency. We also tested the possibilitythat the beta-conglycinin genes have the ability to neutralize "positioneffects" by placing a position dependent gene adjacent to the beta-conglyciningenes. Genes comprised of the promoter that produces the 35S transcript of thecauliflower mosaic virus (CaMV 35S) and the uidA coding region was employed asa position dependent reporter gene. Neither the (alpha)' nor the beta subunitgenes effectively altered position dependency of the CaMV 35S promoter. Weconclude that the coding sequence of the (alpha)' subunit gene is importantfor its position independency and that the beta-conglycinin genes do notaffect position dependency of the adjacent genes. Nevertheless the (alpha)'subunit gene acts as an enhancer on the CaMV 35S promoter when the promotersare adjacent to each other.
73                                                     NAL Call. No.: 450 P693Expression of soybean-embryo lipoxygenase 2 in transgenic tobacco tissue.Deng, W.; Grayburn, W.S.; Hamilton-Kemp, T.R.; Collins, G.B.; Hildebrand, D.F.Berlin : Springer-Verlag; 1992.Planta v. 187 (2): p. 203-208; 1992.  Includes references.
Language:  English
Descriptors: Nicotiana tabacum; Transgenics; Gene expression; Glycine max;Plant embryos; Lipoxygenase; Enzyme activity; Lipid metabolism; Fatty acids;Peroxidation
Abstract:  To assess the role of lipoxygenase (LOX; EC 1.13.11.12) in plants,we increased the expression of LOX in the tissues of Nicotiana tabacum L. cv.'KY 14' by over-expression of the LOX2 gene from the soybean (Glycine max (L.)Merrill) embryo. The LOX2 cDNA was manipulated by replacing its5'-untranslated sequence with the translational enhancer of the alfalfa mosaicvirus (AMV), and subcloned into a plant expression vector, 3' to a duplicatedcauliflower mosaic virus 35S promoter. The AMV-LOX2 construct was transferredinto tobacco using Agrobacterium tumefaciens strain A281. The LOX2 wasexpressed in transgenic tobacco calli, leaves of transgenic plants, and theirseed progeny at levels up to 0.1-0.2% of the total extracted protein. Theintroduced LOX2 affected fatty-acid oxidative metabolism as evidenced by a50-529% increase in C6-aldehyde production. The impact on C6-aldehydeformation was greater than the effect on production of fatty-acidhydroperoxides. This is consistent with other studies indicating the greaterpropensity of soybean embryo LOX2 in generating C6-aldehydes than that ofother well-characterized LOX isozymes.
74                                                     NAL Call. No.: 450 P692Expression of the soybean (Glycine max) glutamate 1-semialdehydeaminotransferase gene in symbiotic root nodules.Sangwan, I.; O'Brian, M.R.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul.Plant physiology v. 102(3): p. 829-834; 1993 Jul.  Includes references.
Language:  English
Descriptors: Glycine max; Structural genes; Complementary  DNA;Aminotransferases; Nucleotide sequences; Amino acid sequences; Geneexpression; Messenger  RNA; Enzyme activity; Root nodules; Leaves; Etiolation
Abstract:  Extracts of soybean (Glycine max) root nodules and greeningetiolated leaves catalyzed radiolabeled 6-aminolevulinic acid (ALA) formationfrom 3,4-[3H]glutamate but not from 1-[14C]glutamate. Nevertheless, thosetissue extracts expressed the activity of glutamate 1-semialdehyde (GSA)aminotransferase, the C5 pathway enzyme that catalyzes ALA synthesis from GSAfor tetrapyrrole formation. A soybean nodule cDNA clone that conferred ALAprototrophy, GSA aminotransferase activity, and glutamate-dependent ALAformation activity on an Escherichia coli GSA aminotransferase mutant wasisolated. The deduced product of the nodule cDNA shared 79% identity with theGSA aminotransferase expressed in barley leaves, providing, along with thecomplementation data, strong evidence that the cDNA encodes GSAaminotransferase. GSA aminotransferase mRNA and enzyme activity were expressedin nodules but not in uninfected roots, indicating that the Gsa gene isinduced in the symbiotic tissue. The Gsa gene was strongly expressed in leavesof etiolated plantlets independently of light treatment and, to a much lesserextent, in leaves of mature plants. We conclude that GSA aminotransferase, andpossibly the C5 pathway, is expressed in a nonphotosynthetic plant organ fornodule heme synthesis and that Gsa is a regulated gene in soybean.
75                                                  NAL Call. No.: SB732.6.M65Extracellular protein elicitors from Phytophthora: host-specificity andinduction of resistance to bacterial and fungal phytopathogens.Kamoun, S.; Young, M.; Glascock, C.B.; Tyler, B.M.St. Paul, Minn. : APS Press; 1993 Jan.Molecular plant-microbe interactions : MPMI v. 6 (1): p. 15-25; 1993 Jan.Includes references.
Language:  English
Descriptors: Raphanus sativus; Brassica campestris; Nicotiana tabacum; Crops;Leguminosae; Solanaceae; Phytophthora nicotianae var. parasitica; Phytophthoracryptogea; Xanthomonas campestris pv. armoraciae; Proteins; Cell wallcomponents; Induced resistance; Disease resistance; Genetic regulation; Geneexpression; Promoters; Naringenin-chalcone synthase
76                                                    NAL Call. No.: QK710.P62Ferritin (mRNA, protein) and iron concentrations during soybean noduledevelopment.Ragland, M.; Theil, E.C.Dordrecht : Kluwer Academic Publishers; 1993 Feb.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (3): p. 555-560; 1993 Feb.Includes references.
Language:  English
Descriptors: Glycine max; Gene expression; Messenger  RNA; Ferritin; Iron;Nodulation; Root nodules; Nitrogenase; Enzyme activity; Leghemoglobin
Abstract:  To study how iron-rich nodules concentrate and store iron, ferritin(mRNA, protein) was analyzed in developing soybean nodules and compared tonitrogenase (mRNA/activity) and leghemoglobin (mRNA, protein, heme). Bothferritin mRNA and protein concentrations increased early in nodulation. Laterin nodulation ferritin protein declined, in contrast to the mRNA, asnitrogenase (mRNA and activity) increased and leghenioglobin (mRNA andprotein) accumulated. A precursor/product relationship between iron stored inferritin and iron in nitrogenase or leghemoglobin is suggested. Theuncoordinated changes in ferritin mRNA and protein during nodulation contrastwith nitrogenase mRNA and nitrogenase activity suggesting possibletranslational and posttranscriptional effects on ferritin expression.
77                                                    NAL Call. No.: QK710.P62Forcing expression of a soybean root glutamine synthetase gene in tobaccoleaves induces a native gene encoding cytosolic enzyme.Hirel, B.; Marsolier, M.C.; Hoarau, A.; Hoarau, J.; Brangeon, J.; Schafer, R.;Verma, D.P.S.Dordrecht : Kluwer Academic Publishers; 1992 Oct.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (2): p. 207-218; 1992 Oct.Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Multiple genes; Structural genes;Glutamate-ammonia ligase; Promoters; Gene expression; Transgenics; Genetictransformation; Root nodules; Roots; Genetic regulation; Ammonia; Leaves;Cytoplasm; Immunocytochemistry; Cytosol; Messenger  RNA; Nucleotide sequences
Abstract:  Glutamine synthetase (GS; EC 6.3.1.2) is present in differentsubcellular compartments in plants. It is located in the cytoplasm in root androot nodules while generally present in the chloroplasts in leaves. Theexpression of GS gene(s) is enhanced in root nodules and in soybean rootstreated with ammonia. We have isolated four genes encoding subunits ofcytosolic GS from soybean (Glycine max L. cv. Prize). Promoter analysis of oneof these genes (GS15) showed that it is expressed in a root-specific manner intransgenic tobacco and Lotus corniculatus, but is induced by ammonia only inthe legume background. Making the GS15 gene expression constitutive by fusionwith the CaMV-35S promoter led to the expression of GS in the leaves oftransgenic tobacco plants. The soybean GS was functional and was located inthe cytoplasm in tobacco leaves where this enzyme is not normally present.Forcing this change in the location of GS caused concomitant induction of themRNA for a native cytosolic GS in the leaves of transgenic tobacco. Shiftingthe subcellular location of GS in transgenic plants apparently altered thenitrogen metabolism and forced the induction in leaves of a native GS geneencoding a cytosolic enzyme. The latter is normally expressed only in the roottissue of tobacco. This phenomenon may suggest a hitherto uncharacterizedmetabolic control on the expression of certain genes in plants.
78                                                     NAL Call. No.: 450 P699Freezing tolerance and alteration of translatable mRNAs in alfalfa (Medicagosativa L.) Hardened at subzero temperatures.Castonguay, Y.; Nadeau, P.; Laberge, S.Kyoto : Japanese Society of Plant Physiologists; 1993 Jan.Plant and cell physiology v. 34 (1): p. 31-38; 1993 Jan.  Includes references.
Language:  English
Descriptors: Medicago sativa; Cold hardening; Freezing; Cold tolerance; Stressresponse; Gene expression; Messenger  RNA; Translation; Protein synthesis;Glycine; Cultivars; Regulation; Cold
Abstract:  We analyzed changes in populations of translatable mRNAs occurringin crowns of the cold-tolerant alfalfa (Medicago sativa L.) cv. Apica (CT) andthe cold-sensitive cv. CUF-101 (CS) after their acclimation at low nonfreezingtemperatures and at subzero temperatures. Both cultivars showed very similartranslation profiles under all treatments. Low temperatures inducedsignificant changes in the populations of translatable mRNAs. We observed arelationship between the accumulation of cold-regulated (COR) translationproducts and freezing tolerance within cultivars. Moreover, at least three CORtranslation products were specific to the CT and might be related to hardinesspotential in alfalfa. Whereas extension of the cold acclimation period at 2degrees C reduced cold tolerance, incubation at subzero temperatures increasedor maintained freezing tolerance. This increased hardiness was associated withenhanced translation of COR polypeptides and also with the appearance of newtranslatable mRNAs. This is, to our knowledge, the first report of alteredgene expression in plants incubated at subzero temperatures. Marked changes inpopulations of translatable mRNAs at temperatures below freezing might berelated to previous reports that alfalfa achieves maximum hardiness under snowcover when the soil has frozen. Translation in the presence of [3H]glycineshowed that a large proportion of the COR genes encode for glycine-richproteins (GRPs) and that some of the GRPs are specific to the CT.
79                                                     NAL Call. No.: 450 P692Frost, abscisic acid, and desiccation hasten embryo development in Brassicanapus.Johnson-Flanagan, A.M.; Huiwen, Z.; Geng, X.M.; Brown, D.C.W.; Nykiforuk,C.L.; Singh, J.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.Plant physiology v. 99 (2): p. 700-706; 1992 Jun.  Includes references.
Language:  English
Descriptors: Brassica napus; Plant embryos; Seed development; Regulation;Abscisic acid; Frost; Desiccation; Seed germination; Plant proteins;Transcription; Gene expression
Abstract:  Seed development in canola (Brassica napus) following a mildnonlethal freeze was examined with respect to abscisic acid (ABA) levels,desiccation, and expression of LEA.76 and isocitrate lyase (ICL) transcripts.Plants with seed of 70 and 55% moisture contents were frozen to -5 degrees Cfor 3 hours, and seed development followed after thawing. In addition, similarprocesses were compared during induction of extreme desiccation tolerance byapplication of ABA in Brassica microspore-derived haploid embryos in culture.A mild freeze/thaw caused a premature switch in seed developmental directionfrom predesiccation to desiccation as indicated by an immediate andaccelerated loss of seed moisture to levels similar to the mature seed in 7instead of 35 days, and by elevated ABA levels and induction of low levels ofLEA.76 and ICL transcripts. Similarly, addition of ABA to haploid embryos inculture resulted in the induction of desiccation tolerance and low levels oflate embryogenesis-abundant (LEA) but not ICL transcripts. In contrast, normalseed development and desiccation of ABA-treated (desiccation-tolerant) embryosresulted in the induction of ICL and very high levels of LEA.76 transcripts.Similarly, desiccation of control (desiccation-sensitive) embryos resulted invery high levels of LEA.76 transcripts. These results indicate that althoughLEA-type proteins have been implicated in the development of desiccationtolerance, high transcript levels of LEA.76 were not observed in the inductionof desiccation tolerance either by a hastening of the maturation process inthe developing Brassica seed, or by the exogenous application of ABA toBrassica haploid embryos in culture.
80                                               NAL Call. No.: S494.5.B563C87Functional and structural analysis of promoter fragments in soybean nuclearDNA.Dong, J.L.; Xu, X.L.; Sakai, F.; Li, J.L.Dordrecht : Kluwer Academic Publishers; 1993.Current plant science and biotechnology in agriculture v. 15: p. 165-168;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: Glycine max; Glycyrrhiza glabra; Promoters; Recombinant  DNA;Beta-glucuronidase; Genetic transformation; Gene expression; Histoenzymology;Reporter genes
81                                                     NAL Call. No.: 500 N21PGene expression in cotton (Gossypium hirsutum L.) fiber: cloning of the mRNAs.John, M.E.; Crow, L.J.Washington, D.C. : The Academy; 1992 Jul01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 89 (13): p. 5769-5773; 1992 Jul01.  Includes references.
Language:  English
Descriptors: Gossypium hirsutum; Messenger  RNA; Cloning; Gene expression;Nucleotide sequences; Amino acid sequences; Dna libraries; Transgenics
Abstract:  Cotton, an important natural fiber, is a differentiated epidermalcell. The number of genes that are active in fiber cells is similar to thosein leaf, ovule, or root tissues. Through differential screening of a fibercDNA library, we isolated five cDNA clones that are preferentially expressedin fiber. One of the cDNA clones, pCKE6, corresponded to an abundant mRNA infiber. Transcripts for E6 were detected throughout the development of thefiber. Immunoprecipitation of in vitro translation products and Western blotanalysis of fiber proteins showed two polypeptides in the range of 30-32 kDaas the products of E6 mRNA. Sequence analysis and hybrid-selected RNAtranslation also suggest that E6 mRNAs encode two polypeptides. Concentrationsof E6 mRNA and protein are highest during the late primary cell wall and earlysecondary cell wall synthesis stages. Sequence comparison of E6 with otherknown eukaryotic and prokaryotic genes reveals no significant homology(Genbank; December 1991). E6 or a homologous gene(s) is conserved in severalmembers of Malvaceae as well as in one other fiber-producing plant, kapok, butis not found in several other plants examined or in Acetobacter xylinum. Agenomic clone corresponding to pCKE6 was isolated, and the promoter element ofthe E6 gene was shown to direct the expression of a carrot extensin mRNA in atissue-specific and developmentally regulated fashion in transgenic cottonplants.
82                                                     NAL Call. No.: 450 P692A gene that encodes a proline-rich nodulin with limited homology to PsENOD12is expressed in the invasion zone of Rhizobium meliloti-induced alfalfa rootnodules.Lobler, M.; Hirsch, A.M.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Sep.Plant physiology v. 103 (1): p. 21-30; 1993 Sep.  Includes references.
Language:  English
Descriptors: Medicago sativa; Amino acid sequences; Gene expression; Geneticcode; Nucleotide sequences; Nodulins; Proline; Rhizobium meliloti; Rootnodules; Transcription
Abstract:  To define the early stages of the interaction between Rhizobium andhost legumes, we have cloned and characterized three early nodulin-encodingsequences from an alfalfa (Medicago sativa L.) cDNA library by probing with afragment of a cDNA clone for PsENOD12, an infection-related nodulin from pea(Pisum sativum L). Although the coding regions of the three clones are 95 to98% homologous to each other, they are only 43% homologous to the pea clone.However, the putative signal peptide encoded by the alfalfa cDNA clones is100% homologous to the PsENOD12 signal peptide. The spatial and temporalexpression patterns of PsENOD12 and the alfalfa clones were compared. In situhybridization experiments detected RNA transcripts in the invasion zone ofmature nitrogen-fixing nodules, the same site where PsENOD12 mRNAs are found.Transcripts were also found by in situ hybridization in cells of Rhizobiummeliloti exoH mutant-induced nodules penetrated by infection threads, butnorthern analysis did not detect transcripts in Inf- (infection thread minus)nodules elicited by R. meliloti exoB nodules or in pseudonodules elicited bytreatment with the auxin transport inhibitor N-1-(naphthyl)phthalamic acid. Inaddition, the alfalfa gene represented by these cDNA clones exhibited atemporal expression pattern that differed from that of PsENOD12, which istransiently expressed. These data, plus information derived from Southern blotanalysis, indicate that we have isolated cDNA clones for a novel earlynodulin, which we have designated MsENOD10 (Medicago sativa Early Nodulin 10).
83                                                    NAL Call. No.: 450 P5622Genetic and chemical polymorphisms of saponins in soybean seed.Tsukamoto, C.; Kikuchi, A.; Harada, K.; Kitamura, K.; Okubo, K.Oxford ; New York : Pergamon Press, 1961-; 1993 Nov.Phytochemistry v. 34 (5): p. 1351-1356; 1993 Nov.  Includes references.
Language:  English
Descriptors: Glycine max; Seeds; Triterpenoid saponins; Structure; Biochemicalpolymorphism; Genetic polymorphism; Gene expression; Inheritance
Abstract:  The variation in saponin composition in soybean seeds is explainedby different combinations of five genes controlling the utilization ofsoyasapogenol glycosides as substrates. The function of these genes isvariety-specific and organ-specific. Phenotypes of over 1000 soybeans wereclassified into eight saponin types, and the frequency of phenotypes wasdifferent between the cultivated [Glycine max (L.) Merr.] and the wild soybean(G. soja Sieb. & Zucc.). The AaBc saponin type predominated in G. soja (58.4%of test collections), but was only found in 0.3% of G. max. Four unidentifiedarabinoside saponins were detected in the seeds of the AaBc type soybeans.Themode of inheritance of saponin types is explained by a combination ofco-dominant, dominant and recessive acting genes. The combined chemical andgenetic data show that the directed manipulation of soybean saponincomposition is a possibility for the future.
84                                                  NAL Call. No.: 511 P444AEBGenetic transformation of alfalfa using the Ti plasmid system of Agrobacteriumtumefaciens.Deineko, E.V.; Rivkin, M.I.; Komarova, M.L.; Vershinin, A.V.; Shumnyi, A.V.K.New York, N.Y. : Consultants Bureau; 1992 Jan.Doklady : biological sciences - Akademiia nauk SSSR v. 319 (1/6): p. 457-459.ill; 1992 Jan.  Translated from: Doklady Akademii Nauk SSSR, v. 319 (6), 1991,p. 1473-1476. (511 P444A).  Includes references.
Language:  English; Russian
Descriptors: Medicago sativa; Gene expression; Genetic transformation;Plasmids; Transgenics; Agrobacterium tumefaciens
85                                                    NAL Call. No.: QK710.P62The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by agene family.Xue, J.; Lenman, M.; Falk, A.; Rask, L.Dordrecht : Kluwer Academic Publishers; 1992 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (2): p. 387-398; 1992 Jan.Includes references.
Language:  English
Descriptors: Sinapis alba; Brassica napus; Arabidopsis thaliana; Multigenefamilies; Thioglucosidase; Nucleotide sequences; Gene expression; MessengerRNA; Amino acid sequences
Abstract:  A full-length cDNA clone (MB3) and three partial clones (MA1, MB1and MB2) which encode myrosinase (thioglucoside glucohydrolase, EC 3.2.3.1)were isolated from a Sinapis alba (white mustard) cDNA library. Nucleotidesequence analysis of these clones revealed that they are encoded by a genefamily. Southern blot analysis with gene-specific probes showed that the genefamily consists of a least two subfamilies (MA and MB) each with severalmembers both in S. alba and in Brassica napus (oilseed rape). In Arabidopsisthaliana (wall cress) only three myrosinase genes seem to be present. Northernblot analysis indicated that all the myrosinase mRNA species have the samesize, approximately 1.95 kb.
86                                                     NAL Call. No.: 500 N21PGuanine nucleotide binding protein involvement in early steps ofphytochrome-regulated gene expression.Romero, L.C.; Lam, E.Washington, D.C. : The Academy; 1993 Feb15.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (4): p. 1465-1469. ill; 1993 Feb15.  Includes references.
Language:  English
Descriptors: Glycine max; Binding proteins; Gene expression; Guanine;Nucleotides; Phytochrome; Toxins; Transcription
Abstract:  The transmission process of light signals from plant photoreceptorsto target cellular events is largely unknown. In the present work, we showthat treatment of dark-adapted soybean cells (SB-P) with cholera toxin orpertussis toxin uncouples phytochrome-dependent gene expression. Addition ofas little as 10 ng of toxin per ml is sufficient to activate expression ofgenes encoding the major chlorophyll a/b-binding protein (cab) in the dark.Significant levels of cab transcript accumulation are detected within 0.5 hafter addition of the toxins and expression of these genes is desensitized tofurther light treatments. Treatment of SB-P cells with the calmodulinantagonist N-(6-aminobexyl)-5-chloro-1-naphthalenesulfonamide hydrochloride(W-7) prevents induction of the photoregulated gene by phytochrome orbacterial toxins. These results indicate the involvement of guanine nucleotidebinding protein(s) in phytochrome-mediated cab gene activation. A likely siteof action for this step is between the photoreceptor and a downstreamW-7-sensitive effector.
87                                                    NAL Call. No.: 442.8 Z34Haploid and diploid expression of a Brassica campestris anther-specific genepromoter in Arabidopsis and tobacco.Xu, H.; Davies, S.P.; Kwan, B.Y.H.; O'Brien, A.P.; Singh, M.; Knox, R.B.Berlin, W. Ger. : Springer International; 1993 May.Molecular & general genetics : MGG v. 239 (1/2): p. 58-65; 1993 May.  Includesreferences.
Language:  English
Descriptors: Brassica campestris; Promoters; Structural genes; Plant proteins;Anthers; Nucleotide sequences; Amino acid sequences; Multigene families;Recombinant  DNA; Reporter genes; Beta-glucuronidase; Gene expression;Histoenzymology; Genetic transformation; Transgenic plants; Pollen; Nicotianatabacum; Arabidopsis thaliana; Complementary  DNA
Abstract:  The anther-specific cDNA clone Bcp1 from Brassica campestris isexpressed in both the haploid pollen and diploid tapetum, as shown by in situhybridization. We have isolated Bgp1, a genomic clone homologous to Bcp1. Thecoding region and extensive 5' flanking sequences of Bgp1 have been sequenced,and the coding region shows 88% identity with Bcp1. RNA gel blot analysisconfirmed the expression of Bgp1-specific transcripts in B. campestris pollen.A 767 bp 5' DNA fragment was fused to the reporter gene beta-glucuronidase(gus) and introduced into both Arabidopsis thaliana and Nicotiana tabacum bytransformation. This 5' fragment directed high-level expression in the pollenand tapetum of transgenic Arabidopsis. In transgenic tobacco however, the sameconstruct was expressed only in pollen. A series of 5' deletion constructs hasbeen created and used to transform A. thaliana to analyse the 5' region ofBgp1. The results indicate that Bgp1 expression in the tapetum and pollen ofArabidopsis requires the presence of different 5' DNA sequences.
88                                                    NAL Call. No.: 442.8 Z34High frequency, heat treatment-induced inactivation of the phosphinothricinresistance gene in transgenic single cell suspension cultures of Medicagosativa.Walter, C.; Broer, I.; Hillemann, D.; Puhler, A.Berlin, W. Ger. : Springer International; 1992 Nov.M G G : Molecular and general genetics v. 235 (2/3): p. 189-196; 1992 Nov.Includes references.
Language:  English
Descriptors: Medicago sativa; Genetic transformation; Transgenics; Structuralgenes; Acyltransferases; Glufosinate; Herbicide resistance; Gene expression;Cell suspensions; Genetic regulation; Heat; Callus; Regenerative ability;Enzyme activity
Abstract:  One descendant of the Medicago sativa Ra-3 transformant T304 wasanalysed with respect to the somatic stability of the syntheticphosphinothricin-N-acetyltransferase (pat) gene which was used as a selectivemarker and was under the control of the 5'/3' expression signals of thecauliflower mosaic virus (CaMV) gene VI. In order to quantify geneinstability, we developed a system for culturing and regenerating individualcells. Single cell suspension cultures derived from T304 and the ancestralnon-transgenic M. sativa cultivar Ra-3, were established. The cells wereregenerated into monoclonal calli. In transgenic calli, the phosphinothricin(Pt)-resistance phenotype was retained after more than 2 months ofnon-selective growth. In contrast, up to 12% of the suspension culture cellsgrown under non-selective conditions and at constant temperature (25 degreesC) lost the herbicide-resistance phenotype within 150 days. Surprisingly, aheat treatment (37 degrees C), lasting for 10 days, during the culture periodresulted in an almost complete (95%) loss of the Pt resistance of thesuspension culture cells. However, the frequency of cell division wasidentical in cultures grown under normal and heat treatment conditions. Abiochemical test revealed that no phosphinothricin-N-acetyltransferaseactivity was present in heat treated, Pt-sensitive cells. The resistance levelof the Pt-sensitive transgenic cells was equivalent to that of the wild-typecells. A PCR analysis confirmed the presence of the pat gene in heat treated,Pt-sensitive cells. From these results it is concluded that the Pt resistancegene was heat-inactivated at a high frequency in the M. sativa suspensioncultures.
89                                                     NAL Call. No.: 381 J824Histone synthesis and turnover in alfalfa. Fast loss of highly acetylatedreplacement histone variant H3.2.Waterborg, J.H.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1993Mar05.The Journal of biological chemistry v. 268 (7): p. 4912-4917; 1993 Mar05.Includes references.
Language:  English
Descriptors: Medicago varia; Histones; Protein synthesis; Chemical reactions;Chromatin; Gene expression; Structural genes; Transcription
Abstract:  Histone synthesis in alfalfa tissue culture cells was studied bylabeling with tritiated lysine, purification of histone proteins byreversed-phase high pressure liquid chromatography, and fluorography ofacid/urea/Triton X-100 polyacrylamide gels. Minor histone variant H3.2 wassynthesized twice as fast as major variant H3.1. The predicted difference inhistone H3 variant turnover was examined during continued growth. More than50% of newly synthesized histone H3.2 and 20% of new H3.1 were lost fromchromatin over a period of 100 h. This produced a ratio between the stableremaining portions of each new histone H3 variant protein identical to that ofthe steady-state histone H3 variants. The labile portion of new histone H3.2(half-life of 20 h) was rapidly lost specifically from transcriptionallyactive chromatin as judged by the acetylation level of nearly 1.5 acetylatedlysines/histone molecule, a level 50% higher than the acetylation in histoneH3.2 overall and three times that of histone H3.1. These results and theconstitutive level of H3.2 gene expression identify histone H3.2 of alfalfa asa functional replacement histone variant. The extent of its preferentialassembly into active chromatin nucleosomes and the rapid rate of itssubsequent loss indicate significant dissolution of plant nucleosomes duringgene transcription.
90                                                   NAL Call. No.: QK725.P532Identification of a methyl jasmonate-responsive domain in the soybean vspBpromoter.Mason, H.S.; DeWald, D.B.; Mullet, J.E.Rockville, Md. : American Society of Plant Physiologists; 1993 Mar.The Plant cell v. 5 (3): p. 241-251; 1993 Mar.  Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Promoters; Acid phosphatase;Recombinant  DNA; Reporter genes; Beta-glucuronidase; Gene expression; Geneticregulation; Jasmonic acid; Derivatives; Sucrose; Abiotic injuries; Deletions;Nucleotide sequences; Genetic transformation; Transgenic plants;Histoenzymology; Plant
Abstract:  Soybean vspB encodes a highly expressed vegetative storageprotein-acid phosphatase. In soybean, vspB expression is stimulated by methyljasmonate (MeJA) and sugars. The vspB promoter was studied by transformingtobacco with fusions of 5' noncoding vspB DNA and the gene encodingbeta-glucuronidase (GUS). Constructs containing 833 bp of vspB 5' DNA showedhigh expression of GUS in stems, leaf veins and trichomes, sepals, and pollen.Sucrose (0.2 M) and MeJA (10(-5) M) increased gene expression when applied toleaf tissue. Deletion of the region -787 to -520 with respect to thetranscription initiation site rendered the vspB promoter noninducible by MeJAbut still sucrose responsive. This result indicates that DNA elements capableof modulating vspB by MeJA can be separated from carbon response elements.Further 5' end deletion from -520 to -403 or 3' end deletion from -165 to -289removed DNA sequences involved in carbon modulation of gene expression. A DNAdomain that mediates the MeJA response was further localized to a 50-bp regionbetween -535 and -585. This domain when fused to a cauliflower mosaic virus(CaMV) 35S truncated (-88) promoter makes the CaMV promoter responsive toMeJA. The MeJA-responsive domain contains a G-box motif (CACGTG) and a C-richsequence. A similar 50-bp DNA region is present in the putative promoter ofvspA. Related sequences are located in a wound- and MeJA-responsive domain ofthe proteinase inhibitor II gene and a UV-responsive promoter domain of chs,the gene encoding chalcone synthase that is also responsive to MeJA.
91                                                    NAL Call. No.: QK710.P62Identification of two alfalfa early nodulin genes with homology to members ofthe pea Enod12 gene family.Allison, L.A.; Kiss, G.B.; Bauer, P.; Poiret, M.; Pierre, M.; Savoure, A.;Kondorosi, E.; Kondorosi, A.Dordrecht : Kluwer Academic Publishers; 1993 Jan.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (2): p. 375-380; 1993 Jan.Includes references.
Language:  English
Descriptors: Medicago sativa; Structural genes; Multigene families; Nodulins;Nucleotide sequences; Amino acid sequences; Gene expression; Nodulation; Rootnodules
Abstract:  In a search for plant genes expressed during early symbioticinteractions between Medicago sativa and Rhizobium meliloti, we have isolatedand characterized two alfalfa genes which have strong sequence similarity tomembers of the Enod12 gene family of Pisum sativum. The M. sativa genes,MsEnod12A and B, encode putative protein products of 8066 Da and 12849 Da,respectively, each with a signal sequence at the N-terminus followed by arepetitive proline-rich region. Based on their expression during the initialperiod of nodule development, MsEnod12A and B are alfalfa early nodulin genes.
92                                               NAL Call. No.: S494.5.B563C87Induction of genes encoding phenylpropanoid biosynthetic enzymes in soybeanroots inoculated with B. japonicum, requires NOD gene induction and occursindependent of any known host functions.Estabrook, E.; Potenza, C.; Feder, A.I.; Sengupta-Gopalan, C.Dordrecht : Kluwer Academic Publishers; 1993.Current plant science and biotechnology in agriculture v. 14: p. 385-389;1993.  In the series analytic: Advances in molecular genetics of plant-microbeinteractions. 2 / edited by E.W. Nester, and D.P.S. Verma.  Proceedings of the6th International Symposium on Molecular Plant-Microbe Interactions held July1992, Seattle, Washington.  Includes references.
Language:  English
Descriptors: Glycine max; Bradyrhizobium japonicum; Gene expression;Structural genes; Phenylalanine ammonia-lyase; Chalcone isomerase;Naringenin-chalcone synthase; Genetic regulation; Roots; Nodulation; Celldifferentiation; Root nodules; Root hairs; Messenger  RNA
93                                                  NAL Call. No.: SB732.6.M65Isoflavonoid accumulation and expression of defense gene transcripts duringthe establishment of vesicular-arbuscular mycorrhizal associations in roots ofMedicago truncatula.Harrison, M.J.; Dixon, R.A.St. Paul, MN : APS Press, [c1987-; 1993 Sep.Molecular plant-microbe interactions : MPMI v. 6 (5): p. 643-654; 1993 Sep.Includes references.
Language:  English
Descriptors: Medicago truncatula; Medicago sativa; Glomus versiforme;Vesicular arbuscular mycorrhizas; Roots; Gene expression; Messenger  RNA;Phenylalanine ammonia-lyase; Naringenin-chalcone synthase; Oxidoreductases;Medicarpin; Biosynthesis; Isoflavones; Flavonoids
94                                                    NAL Call. No.: QK710.P62The isolation and characterisation of a cDNA clone encoding L-asparaginasefrom developing seeds of lupin (Lupinus arboreus).Lough, T.J.; Reddington, B.D.; Grant, M.R.; Hill, D.F.; Reynolds, P.H.S.;Farnden, K.J.F.Dordrecht : Kluwer Academic Publishers; 1992 Jun.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (3): p. 391-399; 1992 Jun.Includes references.
Language:  English
Descriptors: Lupinus arboreus; Dna; Structural genes; Asparaginase; Nucleotidesequences; Amino acid sequences; Genetic code; Transcription; Gene expression;Messenger  RNA; Seed development
Abstract:  An L-asparaginase cDNA clone, BR4, was isolated from a Lupinusarboreus Sims developing seed expression library by screening with polyclonalantibodies to the seed asparaginase. The cDNA hybridised with anoligonucleotide probe designed from amino acid sequence data and was found onsequencing to be 947 bp in length. Six polypeptide sequences obtainedpreviously could be placed along the longest open reading frame.Computer-aided codon use analysis revealed that the cDNA sequence wasconsistent with other plant genes in terms of codon use. The cDNA insert wasused to analyse asparaginase transcription in various tissues by northern blotanalysis. A transcript size of approximately 1.2 kb was detected in L.arboreus seed total and poly(A)+ RNA. The level of this transcript declinedfrom 30 days after anthesis to an undetectable level by day 55. Furthermore,under the high stringency conditions used, the seed asparaginase cDNA did nothybridise with total or poly(A)+ RNA isolated from root tips, suggesting thatthe asparaginase known to be present in this tissue may be the product of adifferent gene. Southern analysis suggested the seed asparaginase is asingle-copy gene. The plant asparaginase amino acid sequence did not have anysignificant homology with microbial asparaginases but was 23% identical and66% similar (allowing for conservative substitutions) to a humanglycosylasparaginase.
95                                                    NAL Call. No.: 442.8 Z34Isolation and characterization of novel nodulin cDNAs representig genesexpressed at early stages of soybean nodule development.Kouchi, H.; Hata, S.Berlin, W. Ger. : Springer International; 1993 Apr.M G G : Molecular and general genetics v. 238 (1/2): p. 106-119; 1993 Apr.Includes references.
Language:  English
Descriptors: Glycine max; Bradyrhizobium japonicum; Complementary  DNA;Nodulins; Nucleotide sequences; Amino acid sequences; Root nodules; Celldifferentiation; Gene expression; Messenger  RNA; Spatial distribution; Roots;Epidermis; Stems
Abstract:  We took advantage of a subtractive hybridization procedure toisolate a set of cDNA clones of nodule-specific genes (nodulin genes) fromdeveloping soybean root nodules. Single-stranded 32P-labelled cDNA synthesizedfrom nodule poly(A)+ RNA was hybridized with a large excess of uninfected rootpoly(A)+ RNA. Unhybridized cDNA was selected and used to screen nodule cDNAlibraries. By this procedure we isolated several novel nodulin cDNA clonestogether with most of the nodulin cDNAs previously described. Four novelnodulin genes, which were expressed long before the onset of nitrogenfixation, were further characterized. GmN 6 and GmN 3 transcripts appeared inthe roots less than 3 days after sowing and inoculation with Bradyrhizobium,but GmN 6 transcripts were also detected at very low levels in the stems ofuninfected plants. Transcripts of GmN 15 and GmN 0 first appeared at 6-7 days,just before nodule emergence. Amino acid sequences of the predicted productsof GmN 6, GmN 3 and GmN 0 exhibited no significant homology to proteinsidentified so far. The GmN 15 encoded protein has a limited but significanthomology to some plant cyanins, suggesting that it is a metal-bindingglycoprotein. In situ hybridization studies revealed that GmN 6 transcriptsfirst appeared in the pericycle cells of the root stele near the infectedsite. During nodule emergence they were found in a few cell layers surroundingthe vascular strands connecting the nodule meristem with the root stele, andin mature nodules they were present specifically in the pericycle cells invascular bundles. These observations led us to hypothesize that GmN 6 geneproducts play a role in the transport and/or degradation of photosynthate. Onthe other hand, GmN 3 transcripts first appeared in the primary nodulemeristem just below the root epidermis. In mature nodules they were onlypresent in the infected cells.
96                                                    NAL Call. No.: QK710.P62Isolation and characterization of three families of auxin down-regulated cDNAclones.Datta, N.; LaFayette, P.R.; Kroner, P.A.; Nagao, R.T.; Key, J.L.Dordrecht : Kluwer Academic Publishers; 1993 Mar.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 21 (5): p. 859-869; 1993 Mar.Includes references.
Language:  English
Descriptors: Glycine max; Complementary  DNA; Multigene families; Geneexpression; Genetic regulation; Auxins; Nucleotide sequences; Amino acidsequences; Light; Plant proteins; Transcription; Messenger  RNA; Plantdevelopment
Abstract:  Five cDNA clones (ADR6, ADR11-1, ADR11-2, ADR12-1 and ADR12-2),representing three families of auxin down-regulated (ADR) genes were isolatedand characterized. These were isolated by screening a lambdaZap cDNA librarywith the partial cDNA clones p6, p11 and p12, isolated earlier (Baulcombe andKey, J Biol Chem 255: 8907-8913, 1980). Hybrid-select translation of ADR6,ADR11-2 and ADR12-2 clones produced polypeptides of 33 kDa 22.5 kDa and a 6and 7 kDa respectively, when analyzed by SDS-PAGE. ADR6 and ADR12-2 gave oneand two spots, respectively, on an IEF-SDS 2D gel. ADR11-2 probably encodes abasic protein as it was only resolved on non-equilibrium pH gradient gelelectrophoresis (NEPHGE). Genomic Southern blot analysis of ADR6, ADR11 andADR12 suggests that each represents a small multigene family. The RNA levelscorresponding to ADR6, ADR11 and ADR12 decrease in response to applied auxinby 100-, 15- and 10-fold, respectively (Baulcombe and Key, 1980). Runofftranscription, done in the presence and absence of auxin, showed that the rateof transcription of the genes corresponding to ADR6, ADR11-2 and ADR12-2 wasreduced in the presence of auxin, but the decrease was small relative to thedecrease in the cytoplasmic levels of these mRNAs, in response to auxin. Acomparative analysis of the influence of auxin on in vitro transcription andsteady state RNA levels corresponding to these ADR cDNAs suggests that thedecrease in rate of transcription due to auxin is not enough to account forthe auxin-induced decrease in the steady state levels. Northern analysisshowed developmental and organ/tissue-specific response of these ADR genes.Furthermore, the expression of the genes corresponding to ADR6 and ADR12-1appears to be up-regulated by light, whereas the gene corresponding to ADR11appears to be down-regulated by light.
97                                                    NAL Call. No.: QK710.P62Isolation and characterization of two Brassica napus embryo acyl-ACPthioesterase cDNA clones.Loader, N.M.; Woolner, E.M.; Hellyer, A.; Slabas, A.R.; Safford, R.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 769-778; 1993 Nov.  Includes references.
Language:  English
Descriptors: Brassica napus; Complementary  DNA; Multigene families;Thiolester hydrolases; Nucleotide sequences; Amino acid sequences; Geneexpression; Messenger  RNA; Enzyme precursors; Seeds; Plant embryos
Abstract:  Acyl-ACP thioesterases are involved in regulating chain terminationof fatty systems. Previously, acyl-ACP thioesterase purified from Brassicanapus seed tissue has been shown to have a high preference for hydrolysingoleoyl-ACP. Here, oligonucleotides derived from B. napus oleoyl-ACPthioesterase protein sequence data have been used to isolate two acyl-ACPthioesterase clones from a B. napus embryo cDNA library. The two clones, pNL2and pNL3, contain 1642 bp and 1523 bp respectively and differ in the length oftheir 3' non-coding regions. Both cDNAs contain open reading frames of 366amino acids which encode for 42 kDa polypeptides. Mature rape thioesterase hasan apparent molecular weight of 38 kDa on SDS-PAGE and these cDNAs thereforeencode for precursor forms of the enzyme. This latter finding is consistentwith the expected plastidial location of fatty acid synthase enzymes. Northernblot analysis shows thioesterase mRNA size to be ca. 1.6 kb and for thethioesterase genes to be highly expressed in seed tissue coincident with themost active phase of storage lipid synthesis. There is some sequenceheterogeneity between the two cDNA clones, but overall they are highlyhomologous sharing 95.7% identity at the DNA level and 98.4% identity at theamino acid level. Some sequence heterogeneity was also observed between thededuced and directly determined thioesterase protein sequences. Consistentwith the observed sequence heterogeneity was Southern blot data showing B.napus thioesterase to be encoded by a small multi-gene family.
98                                                    NAL Call. No.: QK710.P62The isolation and functional characterisation of a B. napus acyl carrierprotein 5' flanking region involved in the regulation of seed storage lipidsynthesis.Silva, J. de; Robinson, S.J.; Safford, R.Dordrecht : Kluwer Academic Publishers; 1992 Apr.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (6): p. 1163-1172; 1992 Apr.Includes references.
Language:  English
Descriptors: Brassica napus; Nicotiana tabacum; Agrobacterium tumefaciens;Genes; Promoters; Plant proteins; Lipogenesis; Nucleotide sequences; Geneexpression; Seeds; Reporter genes; Beta-glucuronidase; Transgenics; Genetictransformation; Genetic regulation; Seed development; Histoenzymology
Abstract:  Acyl carrier protein (ACP) is a key component of the fatty acidbiosynthetic machinery in plants. A 1.4 kb 5' flanking region of a Brassicanapus ACP gene (ACP05) was transcriptionally fused to the reporter genebeta-glucuronidase (GUS), and expression of the chimaeric gene monitored intransgenic tobacco. GUS activity was found to increase through seeddevelopment reaching a maximum value, coincident with the most active phase ofstorage lipid synthesis that was, on average, 100-fold higher than thatobserved in leaf. In control plants transformed with CaMV 35S-GUS constructs,GUS activity was similar in leaf and all stages of seed development. Based onaverage values, the level of GUS expression obtained via the ACP promoter wascomparable to that obtained from the CaMV 35S promoter. We therefore concludethat the isolated 5' ACP flanking sequence represents a strong promoterelement involved in the developmental regulation of storage lipid synthesis inB. napus seed tissue. Putative regulatory elements in the 5' upstream regionof ACP05 were identified by dot matrix analysis and by sequence comparisonwith the upstream regions from a second seed-expressed rape ACP gene and froman Arabidopsis ACP gene.
99                                                     NAL Call. No.: QK745.J6Jasmonate-induced proteins in cotton: immunological relationship to therespective barley proteins and homology of transcripts to late embryogenesisabundant (Lea) mRNAs.Reinbothe, S.; Machmudova, A.; Wasternack, C.; Reinbothe, C.; Parthier, B.New York, N.Y. : Springer; 1992.Journal of plant growth regulation v. 11 (1): p. 7-14; 1992.  Includesreferences.
Language:  English
Descriptors: Gossypium hirsutum; Cotyledons; Protein synthesis; Induction;Jasmonic acid; Genetic regulation; Gene expression; Messenger  RNA;Transcription; Hordeum vulgare; Plant proteins; Embryogenesis; Plant embryos
100                                                    NAL Call. No.: 500 N21PJasmonic acid/methyl jasmonate accumulate in wounded soybean hypocotyls andmodulate wound gene expression.Creelman, R.A.; Tierney, M.L.; Mullet, J.E.Washington, D.C. : The Academy; 1992 Jun01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 89 (11): p. 4938-4941. ill; 1992 Jun01.  Includes references.
Language:  English
Descriptors: Glycine max; Hypocotyls; Injuries; Jasmonic acid; Cellularbiology; Cell wall components; Gene expression; Plant proteins; Proline
Abstract:  Jasmonic acid (JA) and its methyl ester, methyl jasmonate (MeJA),are plant lipid derivatives that resemble mammalian eicosanoids in structureand biosynthesis. These compounds are proposed to play a role in plant woundand pathogen responses. Here we report the quantitative determination ofJA/MeJA in planta by a procedure based on the use of [13C,2H3]MeJA as aninternal standard. Wounded soybean (Glycine max [L] Merr. cv. Williams) stemsrapidly accumulated MeJA and JA. Addition of MeJA to soybean suspensioncultures also increased mRNA levels for three wound-responsive genes (chalconesynthase, vegetative storage protein, and proline-rich cell wall protein)suggesting a role for MeJA/JA in the mediation of several changes in geneexpression associated with the plants' response to wounding.
101                                                   NAL Call. No.: QK710.P62The legumin boxes and the 3' part of a soybean beta-conglycinin promoter areinvolved in seed gene expression in transgenic tobacco plants.Chamberland, S.; Daigle, N.; Bernier, F.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 937-949; 1992 Sep.Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana; Agrobacterium tumefaciens; Promoters;Plant proteins; Seeds; Nucleotide sequences; Controlling elements; Reportergenes; Beta-glucuronidase; Genetic transformation; Transgenics; Geneexpression; Transcription; Mutants; Induced mutations; Genetic regulation;Plant embryos; Histoenzymology; Roots; Leaves
Abstract:  beta-conglycinin is one of the major seed storage proteins insoybean. It is composed of three subunits, namely alpha, alpha' and beta. Theexpression of beta-conglycinin is highly regulated, being restricted to theembryo during the mid-maturation phase of embryogeny. Two series of constructswere made with the 2' subunit promoter and the GUS reporter gene toinvestigate the cis-acting elements involved in the regulated expression ofthis promoter. The activity of each construct was tested in transgenic tobaccoplants. In the first series of constructs, we checked if the 'legumin box', asequence found in most legume seed storage protein genes as well as in otherseed-specific genes, is involved in the regulated expression of the alpha'subunit of the beta-conglycinin gene in tobacco. To this end, both copies ofthe alpha' subunit promoter legumin boxes were mutagenized in vitro. Thetranscriptional activity of the single mutants and the double mutant werecompared with that of the wild-type promoter. Our results show that thelegumin boxes act together to increase transcription of the beta-conglycininalpha' subunit gene by about a factor of ten. This is the first demonstrationof a function for the legumin box in transcriptional regulation. In the secondseries of experiments, we wished to determine if the 3' part of the promoter(the CCAAT and TATAA region) contains important regulatory elements. We foundthat this small fragment (-82 to +13 bp) can confer by itself a low level ofseed-specific gene expression. Chimaeric promoters constructed from parts ofthe alpha' subunit promoter and of the constitutive CaMV 35S promoter werealso analysed. These constructs also revealed the importance of the CCAAT andTATAA region of the alpha' subunit promoter in seed-specific gene expression.
102                                                   NAL Call. No.: QK710.P68Light- and sucrose-dependent gene expression in photomixotrophic cellsuspension cultures and protoplasts of rape (Brassica napus L.).Harter, K.; Talke-Messerer, C.; Barz, W.; Schafer, E.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. 507-516; 1993Sep.  Includes references.
Language:  English
Descriptors: Brassica napus; Cell suspensions; Chlorophyll a/b bindingprotein; Gene expression; Growth; Light; Protoplasts; Sucrose
103                                                  NAL Call. No.: QD341.A2N8Metal-regulated transcription in eukaryotes.Thiele, D.J.Oxford : IRL Press; 1992 Mar25.Nucleic acids research v. 20 (17): p. 1183-1191; 1992 Mar25.  Includesreferences.
Language:  English
Descriptors: Saccharomyces cerevisiae; Torulopsis glabrata; Chlamydomonasreinhardtii; Glycine max; Phanerochaete chrysosporium; Mice; Rats;Transcription; Genetic regulation; Metal ions; Gene expression
104                                                   NAL Call. No.: QK710.P62Minimal enhancer elements of the leghemoglobin lba and lbc3 gene promotersfrom Glycine max L. have different properties.She, Q.; Lauridsen, P.; Stougaard, J.; Marcker, K.A.Dordrecht : Kluwer Academic Publishers; 1993 Sep.Plant molecular biology v. 22 (6): p. 945-956; 1993 Sep.  Includes references.
Language:  English
Descriptors: Glycine max; Lotus corniculatus; Promoters; Deletions;Leghemoglobin; Recombinant  DNA; Reporter genes; Chloramphenicolacetyltransferase; Beta-glucuronidase; Gene expression; Genetic regulation;Genetic transformation; Transgenic plants; Histoenzymology; Roots; Rootnodules
Abstract:  The characteristics of the soybean leghemoglobin lba gene promoterwere analyzed and important promoter elements from the lba and lbc3 promoterswere compared using transgenic Lotus corniculatus plants. A 5' deletionanalysis of the lba promoter delimited two cis-acting elements controllingexpression: a distal positive element (-1254, -884) required for expressionand a proximal element (-285, -60) essential for full-level activity. Incontrast to the corresponding region of the lbc3 promoter, the lba proximalelement is unable to control expression from the heterologous CaMV 35Senhancer. The upstream positive element of the lba gene contains a positionand orientation-independent enhancer between positions (-1091, -788). Thesequence of this enhancer region is conserved in the lbc3 gene upstream -1333,-1132) of the previously assigned strong positive element (SPE; -1090, -947).The present analysis revealed some of the properties of this extended lbc3 SPEelement. The extended element (-1364, -947) functions in both orientationsfrom 5' locations whereas the SPE2 subcomponent (-1364, -1154) containing theconserved sequence is only active in the correct orientation. Removal of theSPE2 by internal deletion demonstrates that the SPE2 subcomponent isindispensable for the activity of the lbc3 upstream positive element. Theseresults indicate that the upstream positive elements of the lba and lbc3 genespossess different properties although their conserved minimal enhancersequence has similar function. This may reflect the differential expression ofthe two lb genes of Glycine max L.
105                                                    NAL Call. No.: 500 N21PModification of Brassica seed oil by antisense expression of a stearoly-acylcarrier protein desaturase gene.Knutzon, D.S.; Thompson, G.A.; Radke, S.E.; Johnson, W.B.; Knauf, V.C.; Kridl,J.C.Washington, D.C. : The Academy; 1992 Apr01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 89 (7): p. 2624-2628; 1992 Apr01.  Includes references.
Language:  English
Descriptors: Brassica campestris; Brassica napus; Gene expression; Geneticengineering; Lipid metabolism; Molecular genetics; Rapeseed oil; Saturatedfatty acids; Biosynthesis
Abstract:  Molecular gene transfer techniques have been used to engineer thefatty acid composition of Brassica rapa and Brassica napus (canola) oil.Stearoyl-acyl carrier protein (stearoyl-ACP) desaturase (EC 1.14.99.6)catalyzes the first desaturation step in seed oil biosynthesis, convertingstearoyl-ACP to oleoyl-ACP. Seed-specific antisense gene constructs of B. rapastearoyl-ACP desaturase were used to reduce the protein concentration andenzyme activity of stearoyl-ACP desaturase in developing rapeseed embryosduring storage lipid biosynthesis. The resulting transgenic plants showeddramatically increased stearate levels in the seeds. A continuous distributionof stearate levels from 2% to 40% was observed in seeds of a transgenic B.napus plant, illustrating the potential to engineer specialized seed oilcompositions.
106                                                   NAL Call. No.: 442.8 Z34Modulation of glutamine synthetase gene expression in tobacco by theintroduction of an alfalfa glutamine synthetase gene in sense and antisenseorientation: molecular and biochemical analysis.Temple, S.J.; Knight, T.J.; Unkefer, P.J.; Sengupta-Gopalan, C.Berlin, W. Ger. : Springer International; 1993 Jan.M G G : Molecular and general genetics v. 236 (2/3): p. 315-325; 1993 Jan.Includes references.
Language:  English
Descriptors: Medicago sativa; Nicotiana tabacum; Structural genes;Complementary  DNA; Glutamate-ammonia ligase; Genetic transformation;Transgenics; Antisense  RNA; Genetic regulation; Gene expression;Transcription; Enzyme activity; Messenger  RNA; Translation
Abstract:  A glutamine synthetase (GS) cDNA isolated from an alfalfa cellculture cDNA library was found to represent a cytoplasmic GS. The full-lengthalfalfa GS1 coding sequence, in both sense and antisense orientation and underthe transcriptional control of the cauliflower mosaic virus 35S promoter, wasintroduced into tobacco. Leaves of tobacco plants transformed with the senseconstruct contained greatly elevated levels of GS transcript and GSpolypeptide which assembled into active enzyme. Leaves of the plantstransformed with the antisense GS1 construct showed a significant decrease inthe level of both GS1 and GS2 polypeptides and GS activity, but did not showany significant decrease in the level of endogenous GS mRNA. We have proposedthat antisense inhibition using a heterologous antisense GS RNA occurs at thelevel of translation. Our results also suggest that the post-translationalassembly of GS subunits into a holoenzyme requires an additional factor(s) andis under regulatory control.
107                                              NAL Call. No.: QK725.P56 1993Molecular analysis of cytoplasmic male sterility in sunflower (Helianthusannuus).Zetsche, K.; Horn, R.Weinheim ; New York : VCH; 1993.Plant mitochondria : with emphasis on RNA editing and cytoplasmic malesterility /. p. 411-422; 1993.  Includes references.
Language:  English
Descriptors: Helianthus annuus; Mitochondrial  DNA; Cytoplasmic malesterility; Mitochondrial genetics; Inversion; Structural genes; Transcription;Gene expression; Molecular mapping
Abstract:  The most thoroughly investigated CMS type in sunflower is the PET1(or Leclercq) cytoplasm. The mtDNAs of male-sterile and fertile lines differonly in an area of about 17 kb. The rearranged region which is framed by theatpA gene and the cob gene includes an 11 kb inversion and an about 5 kbinsertion. Due to the 5 kb insertion a new open reading frame (orfH522) iscreated downstream of the atpA gene. Northern hybridizations revealed thatorfH522 is co-transcribed with the atpA gene on an additional largertranscript which can be observed only in the male-sterile lines. The 11 kbinversion seems to be also present in a minor subpopulation of mitochondrialDNA molecules of fertile H. petiolaris plants. The inversion may involve the261 bp inverted repeat. Southern analyses indicate that the 5 kb insertionseems to be composed of sequences from the mitochondrial DNA, the nucleargenome and of sequences of yet unknown origin. Interesting in this connectionis that a homology to the 5 kb insertion could also be detected in anothermale-sterile cytoplasm in sunflower, MAX1, although it is still unclearwhether it plays a role in creating the CMS phenotype in this type ofcytoplasm. Comparing the mitochondrially encoded in organello translationproducts of male-sterile and fertile lines, a 16 kD polypeptide could only beobserved in the male-sterile lines. This protein which is membrane-bound wasnot detectable in fertile H. annuus and H. petiolaris.
108                                                  NAL Call. No.: QK865.A1R4Molecular biology of stress-induced phenylpropanoid and isoflavonoidbiosynthesis in alfalfa.Dixon, R.A.; Choudhary, A.D.; Dalkin, K.; Edwards, R.; Fahrendorf, T.; Gowri,G.; Harrison, M.J.; Lamb, C.J.; Loake, G.J.; Maxwell, C.A.New York, N.Y. : Plenum Press; 1992.Recent advances in phytochemistry v. 26: p. 91-138; 1992.  In the seriesanalytic: Phenolic Metabolism in Plants / edited by H.A. Stafford and R.K.Ibrahim. Proceedings of the Thirty-first Annual Meeting of the PhytochemicalSociety of North America, June 1991, Fort Collins, Colorado.  Literaturereview.  Includes references.
Language:  English
Descriptors: Medicago sativa; Propionic acid; Biosynthesis; Flavonoids;Biochemical pathways; Ligases; Transferases; Hydro-lyases; Enzyme activity;Genetic regulation; Transcription; Plant breeding; Literature reviews;Nucleotide sequences; Gene expression
109                                                   NAL Call. No.: QK710.P68Molecular characterization and expression of alfalfa isoliquiritigenin2'-O-methyltransferase, an enzyme specifically involved in the biosynthesis ofan inducer of Rhizobium meliloti nodulation genes.Maxwell, C.A.; Harrison, M.J.; Dixon, R.A.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. 971-981; 1993Dec.  Includes references.
Language:  English
Descriptors: Medicago sativa; Nodulation; Roots; Transcription; Amino acidsequences; Gene expression; Genetic code; Molecular biology; Nucleotidesequences; Protein synthesis; Rhizobium meliloti
110                                                   NAL Call. No.: QK710.P62Molecular characterization and expression of an isocitrate dehydrogenase fromalfalfa (Medicago sativa L.).Shorrosh, B.S.; Dixon, R.A.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (5): p. 801-808; 1992 Dec.Includes references.
Language:  English
Descriptors: Medicago sativa; Structural genes; Isocitrate dehydrogenase; Dna;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Multigene families; Plant development
Abstract:  A putative isocitrate dehydrogenase (IDH) cDNA from alfalfa hasbeen cloned and sequenced. The derived amino acid sequence of 433 residuescontains the isocitrate and isopropylmalate dehydrogenase signatures, is 63%identical to yeast mitochondrial NADP-IDH and shares high sequence identitywith peptides of pig heart NADP-IDH. The sequence contains a potentialN-terminal leader with similarities to a thylakoid transit peptide. IDHtranscripts and NADP-IDH activity were detected in all alfalfa tissuesexamined, their levels depending upon the tissue type and its developmentalstage. Transcripts and enzymatic activity were not induced on exposure of cellsuspension cultures to a fungal elicitor. IDH is encoded by a small genefamily in alfalfa.
111                                                   NAL Call. No.: QK710.P62Molecular characterization of a pea beta-1,3-glucanase induced by Fusariumsolani and chitosan challenge.Chang, M.M.; Hadwiger, L.A.; Horovitz, D.Dordrecht : Kluwer Academic Publishers; 1992 Nov.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (4): p. 609-618; 1992 Nov.Includes references.
Language:  English
Descriptors: Pisum sativum; Fusarium solani f.sp. phaseoli; Fusarium solanif.sp. pisi; Structural genes; Beta-glucanase; Dna; Nucleotide sequences; Aminoacid sequences; Disease resistance; Defense mechanisms; Fungal diseases;Chitosan; Gene expression; Messenger  RNA; Stems; Roots; Pods; Geneticregulation
Abstract:  beta-glucanases are prominent proteins in pea endocarp tissueresponding to fungal infection. We have cloned and sequenced a partial peacDNA clone, pPIG312, corresponding to a beta-1,3-glucanase in pea podschallenged with the incompatible pathogen Fusarium solani f. sp. phaseoli. Theinsert from the partial pea cDNA was used to probe a genomic library derivedfrom pea leaves of the same cultivar. One of the genomic clones, pPIG4-3,contained the complete coding sequence for a mature beta-1,3-glucanaseprotein. The predicted amino acid sequence of the pea beta-1,3-glucanase has78% identity to bean beta-1,3-glucanase, 62% and 60% to two tobaccobeta-1,3-glucanases, 57% to soybean beta-1,3-glucanase, 51% to barleybeta-1,3-glucanase, and 48% to barley beta-1,3-1,4-glucanase. Genomic Southernanalysis indicates that the pea genome contains only one beta-1,3-glucanasegene corresponding to the probe used in this study. Accumulation ofbeta-1,3-glucanase mRNA homologous with the pPIG312 probe was detected in peapods within 4 to 8 h after challenge with F. solani f. sp. phaseoli, f. sp.pisi, a compatible strain, or the elicitor, chitosan. In the incompatiblereaction, mRNA accumulation remained high for 48h, whereas it rapidlydecreased in the compatible reaction. After fungal inoculation of whole peaseedlings, the enhanced mRNA accumulation occurred mainly in the basal region(lower stem and root). This beta-1,3-glucanase mRNA was constitutivelyexpressed in the roots of pea seedlings. The sustained levels ofbeta-glucanase mRNA expression induced by the incompatible pathogen in theresistance response suggests that the enzyme contributes to the pea plant'sgeneral defense.
112                                                    NAL Call. No.: 450 P699Molecular characterization of a rapidly and transiently wound-induced soybean(Glycine max L.) gene encoding 1-aminocyclopropane-1-carboxylate synthase.Liu, D.; Li, N.; Dube, S.; Kalinski, A.; Herman, E.; Mattoo, A.K.Kyoto, Japan : Japanese Society of Plant Physiologists; 1993 Oct.Plant and cell physiology v. 34 (7): p. 1151-1157; 1993 Oct.  Includesreferences.
Language:  English
Descriptors: Glycine max; Lyases; Acc; Auxins; Ethylene; Gene expression;Genetic code; Healing; Molecular genetics; Amino acid sequences; Nucleotidesequences
Abstract:  A complementary DNA clone, designated GMACS1, encoding an mRNA forsoybean 1-aminocyclopropane-1-carboxylate (ACC) synthase was isolated from aleaf cDNA library, and its nucleotide sequence was determined. TheGMACS1-specific transcript was found to rapidly but transiently accumulateupon wounding in soybean leaf, pod and seed, and was not induced by 2,4-D, orby ethylene. However, the transcript level increased 37-fold in the presenceof cycloheximide.
113                                                  NAL Call. No.: QK725.P532Molecular characterization of NADH-dependent glutamate synthase from alfalfanodules.Gregerson, R.G.; Miller, S.S.; Twary, S.N.; Gantt, J.S.; Vance, C.P.Rockville, Md. : American Society of Plant Physiologists; 1992 Feb.The Plant cell v. 5 (2): p. 215-226; 1992 Feb.  Includes references.
Language:  English
Descriptors: Medicago sativa; Glutamate-ammonia ligase; Nadh; ComplementaryDNA; Nucleotide sequences; Amino acid sequences; Gene expression; MessengerRNA; Genetic regulation; Nitrogen fixation; Bacteroids; Root nodules;Rhizobium meliloti; Enzyme activity
Abstract:  Alfalfa NADH-dependent glutamate synthase (NADH-GOGAT), togetherwith glutamine synthetase, plays a central role in the assimilation ofsymbiotically fixed nitrogen into amino acids in root nodules. Antibodiespreviously raised against purified NADH-GOGAT were employed to screen a cDNAlibrary prepared using RNA isolated from nodules of 20-day-old alfalfa plants.A 7.2-kb cDNA clone was obtained that contained the entire protein codingregion of NADH-GOGAT. Analysis of this cDNA and determination of theamino-terminal amino acids of the purified protein revealed that NADH-GOGAT issynthesized as a 2194-amino acid protein that includes a 101-amino acidpresequence. The deduced amino acid sequence shares significant identity withmaize ferredoxin-dependent GOGAT, and with both large and small subunits ofEscherichia coli NADPH-GOGAT. DNA gel blot analysis of alfalfa genomic DNAsuggests the presence of a single NADH-GOGAT gene or a small gene family. Theexpression of NADH-GOGAT mRNA, enzyme protein, and enzyme activity wasdevelopmentally regulated in root nodules. A dramatic increase in geneexpression occurred coincidentally with the onset of nitrogen fixation in thebacteroid, and was absent in both ineffective plants that were nodulated witheffective Rhizobium meliloti and effective plants that had been nodulated withineffective R. meliloti strains. Maximum NADH-GOGAT expression, therefore,appears to require an effective, nitrogen-fixing symbiosis.
114                                                    NAL Call. No.: 450 P692Molecular cloning and evidence for osmoregulation of thedelta1-pyrroline-5-carboxylate reductase (proC) gene in pea (Pisum sativumL.).Williamson, C.L.; Slocum, R.D.Rockville, MD : American Society of Plant Physiologists, 1926-; 1992 Nov.Plant physiology v. 100 (3): p. 1464-1470; 1992 Nov.  Includes references.
Language:  English
Descriptors: Pisum sativum; Complementary  DNA; Structural genes;Oxidoreductases; Nucleotide sequences; Amino acid sequences; Gene expression;Messenger  RNA; Genetic regulation; Osmotic pressure; Osmoregulation; Roots;Leaves; Seedlings; Greening; Salinity; Sodium chloride
Abstract:  Several cDNA clones encoding delta 1-pyrroline-5-carboxylatereductase (P5CR, L-proline:NAD[P]+ 5-oxidoreductase, EC 1.5.1.2), whichcatalyzes the terminal step in proline biosynthesis, were isolated from a pealeaf library screened with a 32P-labeled Aval fragment of a soybean noduleP5CR cDNA (A.J. Delauney, D.P.S. Verma [1990) Mol Gen Genet 221: 299-305). DNAsequence analysis of one full-length 1.3-kb clone (PPPS3) indicated that thepea P5CR gene contains a single major open reading frame encoding apolypeptide of 28,242 Da. Genomic analysis suggested that two to three copiesof the P5CR gene are present per haploid genome in pea. The primary structureof pea P5CR is 85% identical with that of soybean and exhibits significanthomology to human, yeast, and Escherichia coli P5CR. The sequence of one offour highly conserved domains found in all prokaryotic and eukaryotic P5CRS issimilar to the consensus sequence for the NAD(P)H-binding site of otherenzymes. The pea P5CR cDNA hybridized to two transcripts, 1.3 and 1.1 kb insize, in polyadenylated RNA purified from leaf tissues of mature, light-grownplants (4 weeks old). Only the 1.3-kb transcript was detected in younger (1week old) greened seedlings or in etiolated seedlings. In greened seedlings,steady-state levels of this 1.3-kb mRNA increased approximately 5-fold in roottissues within 6 h after plants were irrigated with 0.4 m NaCl, suggestingthat expression of the P5CR gene is osmoregulated.
115                                                    NAL Call. No.: 450 P692Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an enzymeinvolved in the resistance response of soybean (Glycine max L.) againstpathogen attack.Uhlmann, A.; Ebel, J.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug.Plant physiology v. 102 (4): p. 1147-1156; 1993 Aug.  Includes references.
Language:  English
Descriptors: Glycine max; Complementary  DNA; Ligases; Isoenzymes; Nucleotidesequences; Amino acid sequences; Multigene families; Messenger  RNA; Geneexpression; Genetic regulation; Beta-glucan; Cell wall components;Phytophthora megasperma; Defense mechanisms
Abstract:  We have isolated three classes of cDNAs that probably encode three4-coumarate:coenzyme A ligase (4CL) isoenzymes in soybean (Glycine max L.).The deduced amino acid sequences reveal several regions of extended sequenceidentity among 4CLs of all plants analyzed to date. The sequences of two ofthese regions are consistent with a domain structure proposed for a group ofenzymes catalyzing the ATP-dependent covalent binding of AMP to theirsubstrates during the reaction sequence. By using two cDNA fragments that donot cross-hybridize under the conditions used, we demonstrate that 4CL insoybean is very likely encoded by a small gene family. Members of this familyare differentially expressed in soybean cell cultures treated with beta-glucanelicitors of Phytophthora megasperma f. sp. glycinea or in soybean rootsinfected with either an incompatible or compatible race of the fungus. Theseresults are in agreement with our previous observation that elicitor treatmentof soybean cells caused a preferential enhancement in the activity level ofone of the 4CL isoenzymes. In soybean, 4CL isoenzymes possessing differentsubstrate affinities for substituted cinnamic acids, and showing differentialregulation to environmental stress, may play a pivotal role in distributingsubstituted cinnamate intermediates at a branch point of generalphenylpropanoid metabolism into subsequent specific pathways.
116                                                  NAL Call. No.: QH431.G452Molecular cloning and expression of a cDNA encoding the proliferating cellnuclear antigen from Brassica napus (oilseed rape).Markley, N.A.; Bonham-Smith, P.C.; Moloney, M.M.Ottawa, Ontario, Canada : National Research Counci l Canada; 1993 Jun.Genome / v. 36 (3): p. 459-466; 1993 Jun.
Language:  English
Descriptors: Brassica napus; Complementary  DNA; Plant proteins; Antigens;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Immunochemistry; Dna replication; Dna polymerase
Abstract:  A cDNA clone encoding the proliferating cell nuclear antigen (PCNA)has been isolated from a Brassica napus apical meristem cDNA library. Theputative full-length cDNA contains an open reading frame of 1004 nucleotides,which predicts a protein of 263 amino acids (Mr = 29 231). Sequence analysishas revealed that the plant PCNA exhibits 81.6% amino acid similarity with thehuman PCNA. Genomic Southern blot analysis indicates the presence of at leasttwo copies of PCNA per genome. The B. napus PCNA mRNA (1.0 kb) was expressedin rapidly dividing tissues such as flower buds, apical meristems, and youngleaves, while mature stem and fully expanded leaves showed significantly lowerlevels of PCNA transcript. The B. napus PCNA cDNA was expressed in Escherichiacoli as a fusion protein with glutathione-S-transferase (GST) in the bacterialexpression vector pGEX-2T. A broad specificity monoclonal antibody raisedagainst rabbit PCNA cross-reacted with the GST-PCNA fusion peptide but notwith the GST moiety alone. This antibody also recognized the human PCNA (36kDa) polypeptide, confirming the structural similarities between the human andplant PCNA. The high degree of structural conservation of PCNA from suchdiverse organisms as humans and higher plants suggests that the plant PCNA mayfunction in a manner analogous to that found in mammals with respect to plantcell DNA replication. Such conservation suggests that PCNA is also a criticalcomponent of the plant cell DNA replication complex.
117                                                   NAL Call. No.: QK710.P62Molecular cloning and sequencing analysis of a beta-tubulin gene from Lupinusalbus.Vassilevskaia, T.D.; Ricardo, C.P.; Rodrigues-Pousada, C.Dordrecht : Kluwer Academic Publishers; 1993 Jul.Plant molecular biology v. 22 (4): p. 716-718; 1993 Jul.  Includes references.
Language:  English
Descriptors: Lupinus albus; Structural genes; Complementary  DNA; Tubulin;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Roots; Leaves; Flowers; Multigene families
Abstract:  Genomic lambda-dash library constructed from Lupinus albus nuclearDNA was screened using a fragment of the beta-tubulin cDNA (beta 8-31) cloneof Chlamydomonas reinhardtii as probe. One of the positive recombinant phageswas isolated, subcloned and analysed by sequencing. We present here nucleotideand derived amino acid sequences of the beta-tubulin gene, designated as Lbeta 1 and identified by similarity with other beta-tubulins. The L beta1-encoded protein reveals a very high degree of similarity with other planttubulins and contains consensus sequences for binding guanine base, phosphateand Mg2+. Northern analysis of total RNA isolated from roots, leaves, flowersand pools revealed that Lupinus albus beta-tubulin genes are constitutivelyexpressed in all studied plant tissues.
118                                                    NAL Call. No.: 450 P692Molecular cloning of abscisic acid-responsive mRNAs expressed during theinduction of freezing tolerance in bromegrass (Bromus inermis Leyss)suspension culture.Lee, S.P.; Chen, T.H.H.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Mar.Plant physiology v. 101 (3): p. 1089-1096; 1993 Mar.  Includes references.
Language:  English
Descriptors: Bromus inermis; Messenger  RNA; Plant proteins; Alcoholoxidoreductases; Cloning; Complementary  DNA; Gene expression; Geneticregulation; Abscisic acid; Freezing; Tolerance; Cell suspensions; Nucleotidesequences; Amino acid sequences; Cold; Acclimatization
Abstract:  Abscisic acid (ABA) increases the freezing tolerance of bromegrass(Bromus inermis Leyss) cell-suspension cultures at 23 degrees C and elicitsmany metabolic changes similar to those observed during cold acclimation.Induction and maintenance of freezing tolerance by ABA is accompanied by theexpression of novel polypeptides and translatable RNAs. The objective of thisstudy was to isolate and characterize ABA-responsive cDNAs associated withABA-induced freezing tolerance in bromegrass cell cultures. Among the 16ABA-responsive cDNA clones isolated, 9 were expressed only with ABA treatment,7 showed increased transcript level, and 1 was transiently expressed. Coldresponsiveness was determined in three clones with increased transcript levelsand in the transiently expressed clone. Deacclimation of ABA-hardened cellswas a relatively slow process, because all of the novel transcripts persistedfor at least 7 d after cells were cultured in ABA-free medium. Preliminarysequencing of cDNAs has identified several clones that share high sequencehomology with genes associated with sugar metabolism, osmotic stress, andprotease activity. Clone pBGA61 was fully sequenced and tentatively identifiedas an NADPH-dependent aldose reductase. The predicted amino acid sequence ofthe coding region shared 92% similarity with that predicted for barley aldosereductase cDNA. It is proposed that expression of genes related to sugarmetabolism and osmotic stress may be required for ABA-induced hardening.
119                                                   NAL Call. No.: QK710.P68The MsK family of alfalfa protein kinase genes encodes homologues ofshaggy/glycogen synthase kinase-3 and shows differential expression patternsin plant organs and development.Pay, A.; Jonak, C.; Bogre, L.; Meskiene, I.; Mairinger, T.; Szalay, A.;Heberle-Bors, E.; Hirt, H.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Jun.The plant journal v. 3 (6): p. 847-856; 1993 Jun.  Includes references.
Language:  English
Descriptors: Medicago sativa; Structural genes; Multigene families; Proteinkinase; Nucleotide sequences; Amino acid sequences; Complementary  DNA; Geneexpression; Messenger  RNA; Cell suspensions; Leaves; Petioles; Stems; Roots;Flowering; Plant embryos
120                                                   NAL Call. No.: QK710.P68Multiple functions of promoter sequences involved in organ-specific expressionand ammonia regulation of a cytosolic soybean glutamine synthetase gene intransgenic Lotus corniculatus.Marsolier, M.C.; Carrayol, E.; Hirel, B.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Mar.The plant journal v. 3 (3): p. 405-414; 1993 Mar.  Includes references.
Language:  English
Descriptors: Lotus corniculatus; Glycine max; Genes; Promoters; Geneexpression; Gene transfer; Transgenics; Glutamate-ammonia ligase; Enzymeactivity; Regulation; Ammonia; Histochemistry; Plant morphology; Plant anatomy
121                                                  NAL Call. No.: QK725.P532A mutant lectin gene is rescued from an insertion element that blocks itsexpression.Okamuro, J.K.; Goldberg, R.B.Rockville, Md. : American Society of Plant Physiologists; 1992 Sep.The Plant cell v. 4 (9): p. 1141-1146; 1992 Sep.  Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Structural genes; Lectins;Alleles; Mutations; Genetic regulation; Gene expression; Transcription;Controlling elements; Genetic transformation; Transgenics; Promoters;Embryogenesis
Abstract:  The soybean lectin gene Le1 encodes a prevalent seed protein and ishighly regulated during the life cycle. The mutant lectin gene allele le1 isnot transcribed detectably, contains a 3.5-kb Tgm1 insertion element withinits coding region 0.6 kb 3' to the transcription start site, and leads to alectinless phenotype. To determine whether the Tgm1 element or a secondarymutation was responsible for repressing le1 gene transcription, we eliminatedthe insertion element by constructing a chimeric lectin gene (le1/Le1) thatcontained the 5' half of the le1 gene and its promoter region and the 3' halfof the wild-type Le1 gene. Transformed tobacco seed containing the le1/Le1gene produced both lectin mRNA and protein, demonstrating that the mutantlectin gene control region is transcriptionally competent. By contrast,transformed seed containing the le1 gene produced no detectable lectin mRNA.We conclude that the absence of detectable transcription from the le1 gene isdue to transcriptional inhibition by the Tgm1 insertion element and that thiselement acts at a distance to block transcription from an upstream promoterregion.
122                                                   NAL Call. No.: 450 J8224A mutation in Vicia faba results in ineffective nodules with impairedbacteroid differentiation and reduced synthesis of late nodulins.Haser, A.; Robinson, D.L.; Duc, G.; Vance, C.P.Oxford : Oxford University Press; 1992 Nov.Journal of experimental botany v. 43 (256): p. 1397-1407; 1992 Nov.  Includesreferences.
Language:  English
Descriptors: Vicia faba; Rhizobium; Root nodules; Nodulation; Bacteroids; Celldifferentiation; Mutants; Recessive genes; Mutations; Nodulins; Proteinsynthesis; Nitrogen fixation; Acetylene reduction; Enzymes; Enzyme activity;Gene expression; Messenger  RNA
Abstract:  Although numerous reports have documented the effect ofbacterially-induced ineffectiveness on root nodule structure, function, andplant gene expression, few studies have detailed the effect of the plantgenome on similar parameters. In this report effective (N2-fixing) broadbean(Vicia faba L.) and plant-controlled ineffective (non-N2-fixing) broadbeanrecessive for the sym-1 gene were compared for nodule structure, developmentalexpression of nodule enzyme activities, enzyme proteins, and mRNAs involved inN assimilation, leghemoglobin (Lb) synthesis, and acetylene reduction activity(ARA). During development of effective wild-type nodules, glutamine synthetase(GS), aspartate aminotransferase (AAT), phosphoenolpyruvate carboxylase (PEPC)and NADH-glutamate synthase (GOGAT) activities and enzyme proteins increasedcoincident with nodule ARA. The increases in GS, AAT, and PEPC were associatedwith increased synthesis of mRNAs for these proteins. Synthesis of Lbpolypeptides and mRNAs during development of effective nodules was similar tothat of GS, AAT, and PEPC. By contrast, ineffective sym-1 nodules displayedlittle or no ARA and had neither the increases in enzyme activities nor enzymeproteins and mRNAs as seen for effective nodules. The effect of the sym-1 geneappeared to occur late in nodule development at either the stage of bacterialrelease from infection threads or differentiation of bacteria into bacteroids.High in vitro enzyme activities, enzyme polypeptides, and mRNA levels inparental effective nodules were dependent upon a signal associated witheffective bacteroids that was lacking in sym-1 nodules. Nodule organogenesisdid not appear to be a signal for the induction of GS, PEPC, AAT, and Lbexpression in sym-1 nodules.
123                                                    NAL Call. No.: 442.8 Z8NADP+ glyceraldehyde-3-phosphate dehydrogenase in soybeans [glycine max (L.)Merr.]: genetics and developmental expression.Delorme, R.M.; Skorupska, H.T.Berlin, W. Ger. : Springer International; 1993 Feb.Theoretical and applied genetics v. 85 (6/7): p. 851-856; 1993 Feb.  Includesreferences.
Language:  English
Descriptors: Glycine max; Inheritance; Loci; Alleles; Genetic variation;Glyceraldehyde-3-phosphate dehydrogenase; Nadp; Electrophoresis; Enzymepolymorphism; Gene expression; Plant development; Linkage; Linkage groups;Cultivars; Pedigree; Line differences; Lines; Chloroplasts; Genetic change
Abstract:  Chloroplastic (NADP+) glyceraldehyde-3-phosphate dehydrogenase(E.C. 1.2.1.9) catalyzes the second reaction in photosynthesis after thefixation of carbon by Rubisco. Chloroplast-bound (NADP+) G3PDH was resolved insoybean by starch gel electrophoresis using L-histidine-citrate buffer (pH5.7). Histochemical staining revealed zymogram patterns indicative of atetramer. A survey of soybean genotypes revealed differences in zymogrampatterns between the principal cytoplasmic sources of the northern andsouthern US germplasms. In the soybean pedigree, an allelic frequency shifttoward a five-banded pattern was observed. G3PDH polymorphism was due toallele associated with gene expression at the slow locus. No linkage was foundbetween the slow locus of (NADP+) G3PDH and ACO2, ACO3, ACO4, ACP, DIA1, IDH1,IDH2, PGM1, and PGM3. Developmental expression in the above-ground tissues wasidentical, whereas roots as a rule did not express (NADP+) G3PDH activity. Theimportance of chloroplast-bound (NADP+) G3PDH in photo-synthesis and itsinteresting mode of inheritance warrants further exploration of this enzyme insoybean.
124                                                    NAL Call. No.: 450 P692New cold- and drought-regulated gene from Medicago sativa.Laberge, S.; Castonguay, Y.; Vezina, L.P.Rockville, Md. : American Society of Plant Physiologists; 1993 Apr.Plant physiology v. 101 (4): p. 1411-1412; 1993 Apr.  Includes references.
Language:  English
Descriptors: Medicago sativa; Complementary  DNA; Multigene families; Plantproteins; Nucleotide sequences; Amino acid sequences; Gene expression;Messenger  RNA; Genetic regulation; Cold stress; Water stress; Drought;Acclimatization
125                                                    NAL Call. No.: 450 P692A new cold-induced alfalfa gene is associated with enhanced hardening atsubzero temperature.Monroy, A.F.; Castonguay, Y.; Laberge, S.; Sarhan, F.; Vezina, L.P.; Dhindsa,R.S.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Jul.Plant physiology v. 102(3): p. 873-879; 1993 Jul.  Includes references.
Language:  English
Descriptors: Medicago sativa; Complementary  DNA; Structural genes; Plantproteins; Nucleotide sequences; Amino acid sequences; Cold hardening;Freezing; Tolerance; Gene expression; Messenger  RNA; Genetic regulation; Cold
Abstract:  When alfalfa (Medicago sativa L. cv Apica) plants grown at roomtemperature are transferred to 2 degrees C, the temperature at which 50% ofthe plants fail to survive (LT50) decreases from -6 to -14 degrees C duringthe first 2 weeks but then increases to 9 degrees C during the subsequent 2weeks. However, when plants are kept for 2 weeks at 2 degrees C and thentransferred to 2 degrees C for another two weeks, the LT50 declines to 16degrees C. These changes in freezing tolerance are paralleled by changes intranscript levels of cas15 (cold acclimation-specific gene encoding a 14.5-kDprotein), a cold-induced gene. Cold-activation of cas15 occurs even whenprotein synthesis is inhibited by more than 90%, suggesting thatcold-initiated events up to and including the accumulation of cas15transcripts depend on preexisting gene products. cas15 shows little homologyto any known gene at the nucleotide or amino acid level. The deducedpolypeptide (CAS15) of 14.5 kD contains four repeats of a decapeptide motifand possesses a bipartite sequence domain at the carboxy terminus withhomology to the reported nuclear-targeting signal sequences. Although therelative amount of cas15 DNA as a fraction of the total genomic DNA is similarin cultivars with different degrees of freezing tolerance, its organization inthe genome is different. The possible role of cas15 in the development ofcold-induced freezing tolerance is discussed.
126                                                    NAL Call. No.: QK710.A9Nodulation and nodulin gene expression in an interspecific hybrid betweenGlycine max and Glycine tomentella.Shen, B.; Davis, L.C.East Melbourne : Commonwealth Scientific and Industrial Research Organization;1992.Australian journal of plant physiology v. 19 (6): p. 693-707; 1992.  Includesreferences.
Language:  English
Descriptors: Glycine tomentella; Glycine max; Interspecific hybridization;Gene expression; Hybrids; Nodulins; Nodulation; Nitrogen fixation; Rhizobiumfredii; Bradyrhizobium japonicum
127                                                 NAL Call. No.: SB732.6.M65Pathological and molecular characterizations of alfalfa interactions withcompatible and incompatible bacteria, Xanthomonas campestris pv. alfalfae andPseudomonas syringae pv. pisi.Esnault, R.; Buffard, D.; Breda, C.; Sallaud, C.; El Turk, J.; Kondorosi, A.St. Paul, MN : APS Press, [c1987-; 1993 Sep.Molecular plant-microbe interactions : MPMI v. 6 (5): p. 655-664; 1993 Sep.Includes references.
Language:  English
Descriptors: Medicago sativa; Xanthomonas campestris pv. alfalfae; Pseudomonassyringae pv. pisi; Disease resistance; Defense mechanisms; Gene expression;Messenger  RNA; Oxidoreductases; Chalcone isomerase; Naringenin-chalconesynthase; Roots; Leaves; Pathogenesis-related proteins; Nucleotide sequences;Amino acid sequences; Complementary  DNA
128                                                  NAL Call. No.: QK725.P532Patterns of soybean proline-rich protein gene expression.Wyatt, R.E.; Nagao, R.T.; Key, J.L.Rockville, Md. : American Society of Plant Physiologists; 1992 Jan.The Plant cell v. 4 (1): p. 99-100; 1992 Jan.  Includes references.
Language:  English
Descriptors: Glycine max; Multigene families; Plant proteins; Proline; Geneexpression; Messenger  RNA; Cell wall components; Hypocotyls; Xylem; Phloem;Testas; Seeds; Epidermis; Leaves; Cotyledons
Abstract:  The expression patterns of three members of a gene family thatencodes proline-rich proteins in soybean (SbPRPs) were examined using in situhybridization experiments. In most instances, the expression of SbPRP geneswas intense in a limited number of cell types of a particular organ. SbPRP1RNA was localized in several cell types of soybean hypocotyls, including cellswithin the phloem and xylem. SbPRP1 expression increased within epidermalcells in the elongating and mature regions of the hypocotyl; expression wasdetected also in lignified cells surrounding the hilum of mature seeds. SbPRP2RNA was present in cortical cells and in the vascular tissue of the hypocotyl,especially cells of the phloem. This gene was expressed also in the innerinteguments of the mature seed coat. SbPRP3 RNA was localized specifically tothe endodermoid layer of cells surrounding the stele in the elongating regionof the hypocotyl, as well as in the epidermal cells of leaves and cotyledons.These data show that members of this gene family exhibit cell-specificexpression. The members of the SbPRP gene family are expressed in differenttypes of cells and in some cell types that also express the glycine-richprotein or hydroxyproline-rich glycoprotein classes of genes.
129                                                   NAL Call. No.: QK710.P68The plant homologue of MAP kinase is expressed in a cell cycle-dependent andorgan-specific manner.Jonak, C.; Pay, A.; Bogre, L.; Hirt, H.; Heberle-Bors, E.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers; 1993Apr.The plant journal v. 3 (4): p. 611-617; 1993 Apr.  Includes references.
Language:  English
Descriptors: Medicago sativa; Medicago varia; Clones; Genetic analysis;Nucleotide sequences; Amino acid sequences; Genetic code; Dna; Kinases;Microtubules; Plant proteins; Gene expression; Transcription
130                                                  NAL Call. No.: QK725.P532Pollen-stigma signaling in the sporophytic self-incompatibility response.Nasrallah, J.B.; Nasrallah, M.E.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Oct.The Plant cell v. 5 (10): p. 1325-1335; 1993 Oct.  In the special issue:Special review issue on plant reproduction.  Includes references.
Language:  English
Descriptors: Brassica campestris; Brassica napus; Brassica oleracea; Selfincompatibility; Pollen; Stigma; Pollen tubes; Loci; Multigene families;Glycoproteins; Protein kinase; Gene expression; Literature reviews
131                                                   NAL Call. No.: QK710.P68Prediction of germ-line transformation events in chimeric R0 transgenicsoybean plantlets using tissue-specific expression patterns.Christou, P.; McCabe, D.E.Oxford : Blackwell Scientific Publishers and BIOS Scientific Publishers inassociation with the Society for Experimental Biology, c1991-; 1992 May.The Plant journal : for cell and molecular biology v. 2 (3): p. 283-290; 1992May.  Includes references.
Language:  English
Descriptors: Glycine max; Genetic transformation; Germ line; Chimeras;Transgenic plants; Gene expression; Genetic markers; Beta-glucuronidase;Enzyme activity; Genetic improvement; Phenotypes; Developmental stages; Plantanatomy; Plant morphology
132                                                    NAL Call. No.: 450 P692Proteolysis during development and senescence of effective and plantgene-controlled ineffective alfalfa nodules.Pladys, D.; Vance, C.P.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Oct.Plant physiology v. 103 (2): p. 379-384; 1993 Oct.  Includes references.
Language:  English
Descriptors: Medicago sativa; Root nodules; Plant composition; Nodulins;Senescence; Genetic regulation; Proteolysis; Cysteine; Proteinases; Enzymeactivity; Ph; Genotypes; Genetic variation; Plant development; Proteincomposition; Symbiosis; Gene expression; Phosphoenolpyruvate carboxylase;Leghemoglobin
Abstract:  Plant-controlled ineffective root nodules, conditioned by the in1gene in medicago sativa L. cv Saranac, undergo premature senescence and havereduced levels of many late nodulins. To ascertain which factors contribute topremature senescence, we have evaluated proteolysis as it occurs throughoutthe development of ineffective Saranac (in1Sa) and effective Saranac nodules.Cysteine protease activities with acidic pH optimum and enzyme proteins werepresent in both genotypes. We found that acidic protease activity was low ineffective Saranac nodules throughout their development. In contrast, by 2weeks after inoculation, acid protease activity of in1Sa nodules wasseveralfold higher than that of Saranac nodules and remained high until theexperiment was terminated 8 weeks later. This increase in protease enzymeactivity correlated with an increase in protease protein amounts. Increasedprotease activity and amount in in1Sa nodules was correlated with a decreasein nodule soluble protein. The time at which in1Sa nodules initially showedincreased protease activity corresponded to when symbiosis deteriorated. Highlevels of phosphoenolpyruvate carboxylase (PEPC) protein were expressed ineffective nodules by 12 d after inoculation and expression was associated withlow proteolytic enzyme activity. In contrast, although PEPC was expressed inin1Sa nodules, PEPC protein was not found 12 d after inoculation andthereafter. Acidic protease from in1Sa nodules could also degrade purifiedleghemoglobin. These data indicate that premature senescence and low levels oflate nodulins in in1Sa nodules can be correlated in part with increasedproteolysis.
133                                                 NAL Call. No.: SB732.6.M65pSym nod gene influence on elicitation of peroxidase activity from whiteclover and pea roots by rhizobia and their cell-free supernatants.Salzwedel, J.L.; Dazzo, F.B.St. Paul, Minn. : APS Press; 1993 Jan.Molecular plant-microbe interactions : MPMI v. 6 (1): p. 127-134; 1993 Jan.Includes references.
Language:  English
Descriptors: Trifolium repens; Pisum sativum; Rhizobium trifolii; Rhizobiumleguminosarum; Peroxidase; Enzyme activity; Roots; Root hairs; Geneexpression; Plasmids; Plant; Nodulation; Peroxidases
134                                                    NAL Call. No.: 450 P692Regenertion of transgenic soybean (Glycine Max) plants from electroporatedprotoplasts.Dhir, S.K.; Dhir, S.; Savka, M.A.; Belanger, F.; Kriz, A.L.; Farrand, S.K.;Widholm, J.M.Rockville, Md. : American Society of Plant Physiologists; 1992 May.Plant physiology v. 99 (1): p. 81-88; 1992 May.  Includes references.
Language:  English
Descriptors: Glycine max; Transgenics; Protoplasts; Callus; Regenerativeability; Genetic transformation; Gene transfer; Gene expression
Abstract:  Transgenic soybean (Glycine max [L.] Merr.) plants were regeneratedfrom calli derived from protoplasts electroporated with plasmid DNA-carryinggenes for a selectable marker, neomycin phosphotransferase (NPTII), under thecontrol of the cauliflower mosaic virus 35-Svedberg unit promoter, linked witha nonselectable mannityl opine synthesis marker. Following electroporation andculture, the protoplast-derived colonies were subjected to kanamycin selection(50 micrograms per milliliter) beginning on day 15 for 6 weeks. Approximately,370 to 460 resistant colonies were recovered from 1 X 10(6) electroporatedprotoplasts, giving an absolute transformation frequency of 3.7 to 4.6 X10(-4). More than 80% of the kanamycin-resistant colonies showed NPTIIactivity, and about 90% of these also synthesized opines. This indicates thatthe linked marker genes were co-introduced and co-expressed at a very highfrequency. Plants were regenerated from the transformed cell lines. Southernblot analysis of the transformed callus and leaf DNA demonstrated theintegration of both genes. Single-plant assays performed with different plantparts showed that both shoot and root tissues express NPTII activity andaccumulate opines. Experiments with NPTII and mannityl opine synthesis markergenes on separate plasmids resulted in a co-expression rate of 66%. Theseresults indicate that electroporation can be used to introduce both linked andunlinked genes into the soybean to produce transformed plants.
135                                                   NAL Call. No.: QK710.P62Regulatable endogenous production of cytokinins up to 'toxic' levels intransgenic plants and plant tissues.Ainley, W.M.; McNeil, K.J.; Hill, J.W.; Lingle, W.L.; Simpson, R.B.; Brenner,M.L.; Nagao, R.T.; Key, J.L.Dordrecht : Kluwer Academic Publishers; 1993 Apr.Plant molecular biology v. 22 (1): p. 13-23; 1993 Apr.  Includes references.
Language:  English
Descriptors: Glycine max; Nicotiana tabacum; Agrobacterium tumefaciens; Geneexpression; Structural genes; Acyltransferases; Isopentenyladenosine;Recombinant  DNA; Promoters; Heat shock proteins; Genetic regulation; Heatshock; Transgenic plants; Genetic transformation; Shoots; Organogenesis
Abstract:  The effects of expressing a chimeric gene consisting of a soybeanheat shock gene promoter and a sequence that encodes an enzyme catalyzing thesynthesis of a potent phytohormone, the cytokinin iPMP, have been analyzed intransgenic tobacco plants. The production of cytokinin endogenously producedseveral effects previously undocumented. The differentiation of shootsindependent of exogenous cytokinin from heat-treated transgenic plant leafexplants demonstrates that long-term heat treatments do not interfere withcomplex developmental processes. This extends the potential usefulness of heatshock gene promoters to conditionally express genes during windows ofdevelopment that span several weeks.
136                                                    NAL Call. No.: 450 P692Regulation of expression of proteinase inhibitor genes by methyl jasmonate andjasmonic acid.Farmer, E.E.; Johnson, R.R.; Ryan, C.A.Rockville, Md. : American Society of Plant Physiologists; 1992 Mar.Plant physiology v. 98 (3): p. 995-1002; 1992 Mar.  Includes references.
Language:  English
Descriptors: Lycopersicon esculentum; Medicago sativa; Nicotiana tabacum;Proteinases; Enzyme inhibitors; Protein synthesis; Gene expression;Regulation; Jasmonic acid; Derivatives; Messenger  RNA; Induction
Abstract:  Gel electrophoretic analysis of the proteinase inhibitor proteinsinduced in tomato leaves by airborne methyl jasmonate (EE Farmer, CA Ryan[1990] Proc Natl Acad Sci USA 87: 7713-7716) revealed the new appearance ofinhibitors I and II and two other, higher molecular mass proteins (63.5 and 87kilodaltons). Northern analysis of methyl jasmonate-induced inhibitors I andII mRNAs in tomato (Lycopersicon esculentum) leaves, and of alfalfa trypsininhibitor (a Bowman-Birk family inhibitor) mRNA in alfalfa (Medicago sativa)leaves, indicated that nascent inhibitor mRNAs were regulated in a mannersimilar to wounding, that is, at the transcriptional level. In tobacco(Nicotiana tabacum), transformed with a fused gene composed of the 5' and 3'regions of a wound-inducible potato inhibitor II and a chloramphenicol acetyltransferase (CAT) gene coding region, CAT activity was induced in leaves bymethyl jasmonate, consistent with a transcriptional regulation of theinhibitor II gene. In tomato leaves, inhibitor I and II mRNAs and proteinsaccumulated in leaves distal to those exposed to methyl jasmonate or jasmonicacid to similar levels as in exposed leaves. We suggest that in response towound signals generated by insect or pathogen attacks, linolenic acid isreleased into the cytoplasm from plant cell membrane lipids and is rapidlyconverted in cells to jasmonic acid (or perhaps a closely related derivativesuch as methyl jasmonate), which serves as a signal to regulate the expressionof proteinase inhibitor genes.
137                                                  NAL Call. No.: QK725.P532Rhizobium meliloti elicits transient expression of the early nodulin geneENOD12 in the differentiating root epidermis of transgenic alfalfa.Pichon, M.; Journet, E.P.; Dedieu, A.; Billy, F. de; Truchet, G.; Barker, D.G.Rockville, Md. : American Society of Plant Physiologists; 1992 Oct.The Plant cell v. 4 (10): p. 1199-1211; 1992 Oct.  Includes references.
Language:  English
Descriptors: Medicago truncatula; Rhizobium meliloti; Gene expression;Structural genes; Nodulins; Nodulation; Roots; Epidermis; Root nodules;Transgenics; Genetic transformation; Transcription; Genetic regulation;Nucleotide sequences; Amino acid sequences; Restriction mapping
Abstract:  To study the molecular responses of the host legume during earlystages of the symbiotic interaction with Rhizobium, we have cloned andcharacterized the infection-related early nodulin gene MtENOD12 from Medicagotruncatula. in situ hybridization experiments have shown that, within theindeterminate Medicago nodule, transcription of the MtENOD12 gene begins incell layers of meristematic origin that lie ahead of the infection zone,suggesting that these cells are undergoing preparation for bacterialinfection. Histochemical analysis of transgenic alfalfa plants that express anMtENOD12 promoter-beta-glucuronidase gene fusion has confirmed this result andfurther revealed that MtENOD12 gene transcription occurs as early as 3 to 6 hrfollowing inoculation with R. meliloti in a zone of differentiating rootepidermal cells which lies close to the growing root tip. It is likely thatthis transient, nodulation (nod) gene-dependent activation of the ENOD12 genealso corresponds to the preparation of the plant for bacterial infection. Weanticipate that this extremely precocious response to Rhizobium will provide avaluable molecular marker for studying early signal exchange between the twosymbiotic organisms.
138                                                    NAL Call. No.: 450 P692RNA editing of cytochrome oxidase subunit III in sunflower mitochondria.Saiardi, A.; Quagliariello, C.Rockville, Md. : American Society of Plant Physiologists; 1992 Apr.Plant physiology v. 98 (4): p. 1261-1263; 1992 Apr.  Includes references.
Language:  English
Descriptors: Helianthus annuus; Mitochondria; Messenger  RNA; Transcription;Cytochrome-c oxidase; Nucleotide sequences; Gene expression; Genome analysis
Abstract:  Direct sequencing of cytochrome oxidase subunit III (coxIII) mRNAwith a specific primer confirms RNA editing in sunflower (Helianthus annus)mitochondria. Six instances of mRNA editing could be verified, one of thesespecific to this species. All the editing events involve C to U transitions inthe coxIII mRNA causing codon changes that lead to amino acids betterconserved in evolution than those encoded in the genomic DNA. This observationconfirms RNA editing to be widespread in higher plant mitochondria.
139                                                   NAL Call. No.: QH506.E46Roles of plant homologs of Rab1p and Rab7p in the biogenesis of theperibacteroid membrane, a subcellular compartment formed de novo during rootnodule symbiosis.Cheon, C.I.; Lee, N.G.; Siddique, A.B.M.; Bal, A.K.; Verma, D.P.S.Oxford, Eng. : Oxford University Press; 1993 Nov.The EMBO journal v. 12 (11): p. 4125-4135; 1993 Nov.  Includes references.
Language:  English
Descriptors: Glycine max; Vigna aconitifolia; Bradyrhizobium japonicum; Plantproteins; Binding proteins; Guanosine triphosphate; Cell membranes; Celldifferentiation; Root nodules; Complementary  DNA; Nucleotide sequences; Aminoacid sequences; Gene expression; Messenger  RNA; Nodulation; Geneticregulation; Antisense  RNA; Transgenic plants; Genetic transformation
Abstract:  The peribacteroid membrane (PBM) in legume root nodules is derivedfrom plasma membrane following endocytosis of Rhizobium by fusion of newlysynthesized vesicles. We studied the roles of plant Rab1p and Rab7p homologs,the small GTP-binding proteins involved in vesicular transport, in thebiogenesis of the PBM. Three cDNAs encoding legume homologs of mammalian Rab1pand Rab7p were isolated from soybean (sRab1p, sRab7p) and Vigna aconitifolia(vRab7p). sRab1p was confirmed to be a functional counterpart of yeast Ypt1p(Rab1p) by complementation of a yeast ypt1-1 mutant. Both srab1 and vrab7genes are induced during nodulation with the level of vrab7 mRNA being 12times higher than that in root meristem and leaves. This induction directlycorrelates with membrane proliferation in nodules. Antisense constructs ofsrab1 and vrab7, under a nodule-specific promoter (leghemoglobin, Lbc3), weremade in a binary vector and transgenic nodules were developed on soybean hairyroots obtained through Agrobacterium rhizogenes-mediated transformation. Bothantisense srab1 and vrab7 nodules were smaller in size and showed lowernitrogenase activity than controls. The antisense srab1 nodules showed lack ofexpansion of infected cells, fewer bacteroids per cell and their frequentrelease into vacuoles. In contrast, antisense vrab7 expressing nodules showedaccumulation of late endosomal structures and multivesicular bodies in theperinuclear region. These data suggest that both Rab1p and Rab7p are essentialfor the development of the PBM compartment in effective symbiosis.
140                                                    NAL Call. No.: 450 P564Root nodule development: origin, function and regulation of nodulin genes.Verma, D.P.S.; Hu, C.A.; Zhang, M.Copenhagen : The Scandinavian Society for Plant Physiology; 1992 Jun.Physiologia plantarum v. 85 (2): p. 253-265; 1992 Jun.  Includes references.
Language:  English
Descriptors: Leguminosae; Rhizobium; Gene expression; Nodulins; Structuralgenes; Nodulation; Root nodules; Cell differentiation; Bacteroids
Abstract:  The symbiotic root nodule, an organ formed on leguminous plants, isa product of successful interactions between the host plant and the soilbacteria, Rhizobium spp. Plant hormones play an important role in the genesisof this organ. The hormonal balance appears to be modulated by the signalsproduced by bacteria. Many host genes induced during nodule organogenesis andthe symbiotic state have been identified and characterized from severallegumes. These genes encode nodule-specific proteins (nodulins) which performdiverse functions in root nodule development and metabolism. Formation of asubcellular compartment housing the bacteria is essential to sustain thesymbiotic state, and several nodulins arc involved in maintaining theintegrity and function of this compartment. The bacteroid enclosed in theperibacteroid membrane behaves as an 'organelle,' completely dependent on thehost for all its requirements for carbon, nitrogen and other essentialelements. Thus it seems likely that the nodulins in the peribacteroid membraneperform specific transport functions. While the function of a few othernodulins is known (e.g. nodulin-100, nodulin-35), a group of uncharacterizednodulins exists in soybean root nodules. These nodulins share structuralsimilarities and seem to have been derived from a common ancestor. Inductionof nodulin genes occurs prior to and independent of nitrogen fixation, andthus is a prelude to symbiosis. Although some of the early nodulin genes areinduced prior to or during infection, induction of late nodulins requiresendocytotic release of bacteria.
141                                                   NAL Call. No.: QK710.P62Seed-specific repression of GUS activity in tobacco plants by antisense RNA.Fujiwara, T.; Lessard, P.A.; Beachy, R.N.Dordrecht : Kluwer Academic Publishers; 1992 Dec.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 20 (6): p. 1059-1069; 1992 Dec.Includes references.
Language:  English
Descriptors: Nicotiana tabacum; Transgenics; Genetic transformation;Beta-glucuronidase; Reporter genes; Recombinant  DNA; Promoters; Plantproteins; Gene expression; Genetic regulation; Antisense  RNA; Seeds;Messenger  RNA; Enzyme activity
Abstract:  beta-Conglycinin, the 7S storage protein of soybean, is expressedonly in seeds and is regulated predominantly by gene transcription. We appliedan antisense strategy to modify expression of a beta-glucuronidase (uidA orgusA) gene in seeds using a promoter from a beta-conglycinin gene. Transgenictobacco plants harboring the gusA gene under the control of the CaMV 35Spromoter were retransformed with a gene construct comprising thebeta-conglycinin promoter fused to the gusA gene in the antisense orientation.Double transformants were regenerated and transformation was confirmed bySouthern blot hybridization. Seed-specific repression of GUS activity wasobserved in lines containing high copy numbers of the antisense gusAtransgene. Suppression of GUS activity was correlated with the amounts of (-)sense gusA transcript detected and concomitantly with a decrease in gusAtranscript levels. Furthermore, the amount of suppression of GUS activity wasgreatest during mid to late stages of seed development, when expression of thealpha' promoter is high. These results indicate that suppression of GUSactivity is due to expression of the antisense gene.
142                                                   NAL Call. No.: QK710.P62Sequence analysis and developmental expression of an alfalfa protein disulfideisomerase.Shorrosh, B.S.; Dixon, R.A.Dordrecht : Kluwer Academic Publishers; 1992 May.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (2): p. 319-321; 1992 May.Includes references.
Language:  English
Descriptors: Medicago sativa; Structural genes; Dna; Isomerases; Nucleotidesequences; Amino acid sequences; Gene expression; Messenger  RNA; Plantdevelopment
143                                                   NAL Call. No.: QK710.P62Sequence and transcription analysis of mitochondrial plasmids isolated fromcytoplasmic male-sterile lines of Vicia faba.Flamand, M.C.; Goblet, J.P.; Duc, G.; Briquet, M.; Boutry, M.Dordrecht : Kluwer Academic Publishers; 1992 Sep.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (6): p. 913-923; 1992 Sep.Includes references.
Language:  English
Descriptors: Vicia faba; Mitochondrial  DNA; Plasmids; Cytoplasmic malesterility; Nucleotide sequences; Transcription; Gene expression; MessengerRNA; Southern blotting; Dna; Nuclei
Abstract:  Three mitochondrial plasmids (1704, 1695 and 1478 bp) were isolatedfrom sterile cytoplasms of Vicia faba L. and cloned into a bacterial plasmidvector. Their nucleotide sequence was found to be 99 to 100% homologous totheir counterparts isolated from a fertile cytoplasm (J.A. Wahleithner andD.R. Wolstenholme, Curr Genet 12 (1987) 55-76). Several overlappingtranscripts were localized in the region which is unique to each of the threeplasmids. S1 nuclease mapping indicated for all of them several 3' termini buta unique 5' boundary which was located downstream of the consensus sequenceCNTAAGTGANNNNNGAA also found at the transcript 5' boundary of other plantmitochondrial plasmids. Southern blot hybridization with nuclear DNA indicatedthe presence of nuclear sequences homologous to each plasmid.
144                                                    NAL Call. No.: 450 P692Sequence of a Brassica campestris myrosinase gene.Machlin, S.; Mitchell-Olds, T.; Bradley, D.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Aug.Plant physiology v. 102 (4): p. 1359-1360; 1993 Aug.  Includes references.
Language:  English
Descriptors: Brassica campestris; Structural genes; Thioglucosidase;Nucleotide sequences; Amino acid sequences; Introns; Multigene families; Geneexpression; Messenger  RNA
145                                                   NAL Call. No.: QK710.P62Sequence of cab-151, a gene encoding a photosytem II type II chlorophylla/b-binding protein in cotton.Sagliocco, F.; Kapazoglou, A.; Dure L. IIIDordrecht : Kluwer Academic Publishers; 1992 Feb.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 18 (4): p. 841-842; 1992 Feb.Includes references.
Language:  English
Descriptors: Gossypium hirsutum; Genes; Chlorophyll a/b binding protein;Nucleotide sequences; Amino acid sequences; Photosystem ii; Introns; Geneexpression; Messenger  RNA; Leaves; Cotyledons
146                                                 NAL Call. No.: SB732.6.M65Sequential expression of two late nodulin genes in the infected cells ofalfalfa root nodules.Allen, T.; Raja, S.; Ganter, G.; Dunn, K.St. Paul, Minn. : APS Press; 1992 Sep.Molecular plant-microbe interactions : MPMI v. 5 (5): p. 430-434; 1992 Sep.Includes references.
Language:  English
Descriptors: Medicago sativa; Root nodules; Nodulation; Symbiosis; Genes;Nodulins; Gene expression; Leghemoglobin; Nitrogen fixation
147                                                   NAL Call. No.: QK725.I43A short histone H3 promoter from alfalfa specifies expression in S-phase cellsand meristems.Kapros, T.; Stefanov, I.; Magyar, Z.; Ocsovszky, I.; Dudits, D.Columbia, MD : Tissue Culture Association; 1993 Jan.In vitro cellular & developmental biology : plant v. 29P (1): p. 27-32; 1993Jan.  Includes references.
Language:  English
Descriptors: Medicago sativa; Nicotiana tabacum; Medicago varia; Promoters;Histones; Recombinant  DNA; Beta-glucuronidase; Reporter genes; Transgenicplants; Genetic transformation; Gene expression; Cell division; Shootmeristems; Histoenzymology
148                                              NAL Call. No.: QK756.A28 1992Signal transduction and gene expression during cold acclimation of alfalfa.Dhindsa, R.S.; Monroy, A.; Wolfraim, L.; Dong, G.Boca Raton : CRC Press; 1992.Advances in plant cold hardiness / edited by Paul H. Li, Lars Christersson. p.57-71; 1992.  Key papers presented at the "4th International Plant ColdHardiness Seminar" and the invitational papers at the Swedish University ofAgricultural Sciences, July 1 to 5, 1991, Uppsala.  Includes references.
Language:  English
Descriptors: Medicago sativa; Cold tolerance; Gene expression; Transduction
149                                                   NAL Call. No.: QH506.E46Silent mitochondrial and active nuclear genes for subunit 2 of cytochrome coxidase (cox2) in soybean: evidence for RNA-mediated gene transfer.Covello, P.S.; Gray, M.W.Oxford, Eng. : IRL Press; 1992 Nov.The EMBO journal - European Molecular Biology Organization v. 11 (11): p.3815-3820; 1992 Nov.  Includes references.
Language:  English
Descriptors: Glycine max; Mitochondrial  DNA; Structural genes; Cytochrome-coxidase; Nuclei; Mitochondrial genetics; Gene expression; Transcription;Nucleotide sequences; Introns; Amino acid sequences; Rna editing; Evolution
Abstract:  In most plants and other eukaryotes investigated, the mitochondrialgenome carries the gene encoding subunit 2 of cytochrome c oxidase (cox2). Inthis paper, we show that the previously reported mitochondrial cox2 of soybeanis actually silent, and that there is an expressed, single-copy,nucleus-encoded cox2. Molecular cloning and sequence analysis of cox2 cDNA andgenomic clones show that the soybean nuclear gene encodes an N-terminalextension that resembles a signal sequence for mitochondrial import and whosecoding sequence is separated by an intron from that corresponding tomtDNA-encoded cox2. Comparison of soybean mitochondrial and nuclear cox2sequences clearly indicates that in an ancestor of soybean, cox2 wastransferred from the mitochondrion to the nucleus via a C-to-U edited RNAintermediate.
150                                                   NAL Call. No.: QK710.P68Site-directed mutagenesis of the organ-specific element in the soybeanleghemoglobin lbc3 gene promoter.Ramiov, K.B.; Laursen, N.B.; Stougaard, J.; Marcker, K.A.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. 577-580; 1993Sep.  Includes references.
Language:  English
Descriptors: Glycine max; Lotus corniculatus; Gene expression; Genetictransformation; Leghemoglobin; Mutagenesis; Nucleotide sequences; Promoters
151                                                   NAL Call. No.: QK710.P62A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules.Madsen, O.; Sandal, L.; Sandal, N.N.; Marcker, K.A.Dordrecht : Kluwer Academic Publishers; 1993 Oct.Plant molecular biology v. 23 (1): p. 35-43; 1993 Oct.  Includes references.
Language:  English
Descriptors: Glycine max; Complementary  DNA; Structural genes;Oxidoreductases; Nucleotide sequences; Amino acid sequences; Gene expression;Messenger  RNA; Root nodules; Leaves
Abstract:  In plants the enzyme coproporphyrinogen oxidase catalyzes theoxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IXin the heme and chlorophyll biosynthesis pathway(s). We have isolated asoybean coproporphyrinogen oxidase cDNA from a cDNA library and determined theprimary structure of the corresponding gene. The coproporphyrinogen oxidasegene encodes a polypeptide with a predicted molecular mass of 43 kDa. Thederived amino acid sequence shows 50% similarity to the corresponding yeastamino acid sequence. The main difference is an extension of 67 amino acids atthe N-terminus of the soybean polypeptide which may function as a transitpeptide. A full-length coproporphyrinogen oxidase cDNA clone complements ayeast mutant deleted of the coproporphyrinogen oxidase gene, thusdemonstrating the function of the soybean protein. The soybeancoproporphyrinogen oxidase gene is highly expressed in nodules at the stagewhere several late nodulins including leghemoglobin appear. Thecoproporphyrinogen oxidase mRNA is also detectable in leaves but at a lowerlevel than in nodules while no mRNA is detectable in roots. The high level ofcoproporphyrinogen oxidase mRNA in soybean nodules implies that the plantincreases heme production in the nodules to meet the demand for additionalheme required for hemoprotein formation.
152                                                    NAL Call. No.: 450 P699Soybean lipoxygenase L-4, a component of the 94-kilodalton storage protein invegetative tissues: expression and accumulation in leaves induced by podremoval and by methyl jasmonate.Kato, T.; Shirano, Y.; Iwamoto, H.; Shibata, D.Kyoto, Japan : Japanese Society of Plant Physiologists; 1993 Oct.Plant and cell physiology v. 34 (7): p. 1063-1072; 1993 Oct.  Includesreferences.
Language:  English
Descriptors: Glycine max; Leaves; Plant tissues; Pods; Amino acid sequences;Lipoxygenase; Nucleotide sequences; Plant proteins; Cloning; Gene expression;Genetic code; Jasmonic acid
Abstract:  A lipoxygenase L-4 gene was isolated from a soybean genomiclibrary. The amino acid sequence of lipoxygenase L-4 is highly homologous withthe partial amino acid sequence of the 94-kDa vegetative storage protein,vsp94, found in paraveinal mesophyll cells in the leaves of depodded soybeanplants. No L4 expression was observed in maturing seeds. The L4 gene is highlyexpressed in the vegetative tissues of young seedlings, including cotyledons,hypocotyls, roots and primary leaves. L-4 expression followed the same patternas lipoxygenase activity in cotyledons peaking 3 to 5 days after germination,and returning to a basal level by 9 days after germination. L-4 geneexpression was low in the roots, stems and leaves of 10-week-old plants.Exposure of 4-week-old plants to atmospheric methyl jasmonate increased L-4mRNA in leaves. Continuous pod removal from 7-week-old plants over a 2 weekperiod resulted in dramatic accumulation of L-4 mRNA in leaves. Accumulationof the L-4 protein and three other lipoxygenase fractions in the leaves ofdepodded plants was demonstrated by ion exchange chromatography. These resultsindicate that lipoxygenase L-4 is a component of vsp94.
153                                                  NAL Call. No.: QK725.P532Soybean nodulin-26 gene encoding a channel protein is expressed only in theinfected cells of nodules and is regulated differently in roots of homologousand heterologous plants.Miao, G.H.; Verma, D.P.S.Rockville, MD : American Society of Plant Physiologists, c1989-; 1993 Jul.The Plant cell v. 5 (7): p. 781-794; 1993 Jul.  Includes references.
Language:  English
Descriptors: Glycine max; Multigene families; Structural genes; Nodulins;Nucleotide sequences; Amino acid sequences; Gene expression; Messenger  RNA;Root nodules; Roots; Introns; Exons; Promoters; Transgenic plants; Genetictransformation; Nicotiana tabacum; Lotus corniculatus; Root meristems;Complementary  DNA
Abstract:  Nodulin-26 (N-26) is a major peribacteroid membrane protein insoybean root nodules. The gene encoding this protein is a member of an ancientgene family conserved from bacteria to humans. N-26 is specifically expressedin root nodules, while its homolog, soybean putative channel protein, isexpressed in vegetative parts of the plant, with its highest level in the rootelongation zone. Analysis of the soybean N-26 gene showed that its fourintrons mark the boundaries between transmembrane domains and the surfacepeptides, suggesting that individual transmembrane domains encoded by a singleexon act as functional units. The number and arrangement of introns betweenN-26 and its homologs differ, however. Promoter analysis of N-26 was conductedin both homologous and heterologous transgenic plants. The cis-acting elementsof the N-26 gene are different from those of the other nodulin genes, and nonodule-specific cis-acting element was found in this gene. in transgenicnodules, the expression of N-26 was detected only in the infected cells; noactivity was found in nodule parenchyma and uninfected cells of the symbioticzone. The N-26 gene is expressed in root meristem of transgenic Lotuscorniculatus and tobacco but not in untransformed and transgenic soybeanroots, suggesting the possibility that this nodulin gene is controlled by atrans-negative regulatory mechanism in homologous plants. This studydemonstrates how a preexisting gene in the root may have been recruited forsymbiotic function and brought under nodule-specific developmental control.
154                                                    NAL Call. No.: 450 P692Soybean seed coat peroxidase: a comparison of high-activity and low-activitygenotypes.Gijzen, M.; Van Huystee, R.; Buzzell, R.I.Rockville, MD : American Society of Plant Physiologists, 1926-; 1993 Dec.Plant physiology v. 103 (4): p. 1061-1066; 1993 Dec.  Includes references.
Language:  English
Descriptors: Glycine max; Testas; Plant composition; Peroxidase; Enzymeactivity; Genetic regulation; Genotypes; Genetic variation; Cultivars; Roots;Gene expression; Alleles; Histochemistry; Plant anatomy
Abstract:  Peroxidase activity in the seed coats of soybean (Glycine max [L.]Merr.) is controlled by the Ep locus. We compared peroxidase activity incell-free extracts from seed coat, root, and leaf tissues of three EpEpcultivars (Harosoy 63, Harovinton, and Coles) to three epep cultivars (Steele,Marathon, and Raiden). Extracts from the seed coats of EpEp cultivars were100-fold higher in specific activity than those from epep cultivars, but therewas no difference in specific activity in crude root or leaf extracts.Isoelectric focusing of root tissue extracts and staining for peroxidaseactivity showed that EpEp cultivars had a root peroxidase of identicalisoelectric point to the seed coat peroxidase, whereas roots of the epep typeswere lacking that peroxidase, indicating that the Ep locus may also affectexpression in the root. In seed coat extracts, peroxidase was the mostabundant soluble protein in EpEp cultivars, whereas this enzyme was presentonly in trace amounts in epep genotypes, as determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis. Histochemical localization ofperoxidase activity inseed coats of EpEp cultivars shows that the enzymeoccurs predominately in the cytoplasm of hourglass cells of the subepidermis.No obvious difference in the gross or microscopic structure of the seed coatwas observed to be associated with the Ep locus. These results suggest thatsoybean seed coat peroxidase may be involved in processes other than seed coatbiosynthesis.
155                                                    NAL Call. No.: 381 J824A soybean vacuolar protein (P34) related to thiol proteases is synthesized asa glycoprotein precursor during seed maturation.Kalinski, A.; Melroy, D.L.; Dwivedi, R.S.; Herman, E.M.Baltimore, Md. : American Society for Biochemistry and Molecular Biology; 1992Jun15.The Journal of biological chemistry v. 267 (17): p. 12068-12076; 1992 Jun15.Includes references.
Language:  English
Descriptors: Glycine max; Seeds; Seed maturation; Thiols; Proteinases; Geneexpression; Protein synthesis; Glycoproteins; Precursors; Organelles
Abstract:  We have examined the synthesis, posttranslational processing, andlocalization of soybean P34, a member of the papain superfamily. P34 has beenidentified as a constituent of oil storage organelles or oil bodies isolatedfrom seed lysates and has been assumed to be one of the oil body proteins.Electron microscopic immunocytochemistry with a monoclonal antibodydemonstrated that P34 is localized in the protein storage vacuoles but not inthe oil bodies. Immunocytochemical observations of partially disrupted seedcells showed that the association of P34 with oil bodies appears to occur as aconsequence of cell lysis. In vitro synthesis of P34 results in the formationof a 46-kDa polypeptide that increases to 47 kDa due to core glycosylation bycanine microsomes. In vivo synthesis studies in the presence and absence oftunicamycin, an inhibitor of N-linked glycosylation, indicate that pro-P34 is47 kda. Since the cDNA sequence of prepro-P34 contains a single putativeglycosylation site in the precursor domain, we conclude that P34, like a fewother vacuolar proteins, is synthesized as a glycoprotein precursor.Pulse-chase experiments showed that the processing of pro-P34 to mature P34occurs in a single step and that this posttranslational cleavage occurs on thecarboxyl side of an Asn, which is typical of seed vacuolar proteins. Pro-P34(47 kDa) is detected in immunoblots of maturing seeds. Analysis of RNAindicates that the P34 genes are expressed only during seed maturation andthat the P34 mRNA is related to other thiol protease mRNAs detectable in otherorgans and plants. Unlike other seed thiol proteases that are synthesized onlyafter seed germination, P34 accumulates during seed maturation.
156                                                    NAL Call. No.: 450 P693Spatial and temporal expression of Cab mRNAs in cotyledons of the developingsoybean seedling.Chang, Y.C.; Walling, L.L.Secaucus, N.J. : Springer-Verlag; 1992.Planta v. 186 (2): p. 262-272; 1992.  Includes references.
Language:  English
Descriptors: Glycine max; Seedlings; Developmental stages; Cotyledons;Messenger  RNA; Gene expression; Genetic code; Chlorophyll a/b bindingprotein; Spatial distribution; Plant anatomy
Abstract:  Changes in the temporal and spatial distribution of the mRNAs forthe chlorophyll-a/b-binding-protein gene (Cab) in cotyledons from developingsoybean (Glycine max (L.) Merr.) seedlings were studied. Cab mRNAs could bedetected in the polysomal polyadenylated poly(A)+ mRNA population ofcotyledons within 3 d after start of imbibition, prior to their emergence fromsoil, and declined prior to the onset of cotyledonary senescence. The Cab mRNAlevels were compared to the levels of rbcS (ribulose-1,5-bisphosphatecarboxylase small subunit) mRNAs in cotyledons and distinct differences intheir expression programs were noted. Quantitative analyses with S1 nucleasewere used to monitor the accumulation of the mRNAs of individual members ofthe Cab gene family. Cab 3, Cab 4, and Cab 5 mRNAs were differentiallyregulated in the cotyledons during post-germinative development. Cab 4 was themost abundant Cab gene mRNA representing approx. 4.3% of the cotyledonarypolysomal poly(A)+ mRNA population. In-situ hybridizations usingmethacrylate-imbedded tissue and 3H-antisense- and -sense-strand RNA probeswere used to determine the qualitative and quantitative distribution of CabRNAs in cotyledonary cells. Cab RNAs were most abundant in the palisade cells.These results indicate an interaction of both developmental and environmentalcues in modulating the expression of the Cab gene family in soybeancotyledons.
157                                                   NAL Call. No.: QK710.P62Stress response in alfalfa (Medicago sativa L.). 15. Characterization andexpression patterns of members of a subset of the chalcone synthase multigenefamily.Junghans, H.; Dalkin, K.; Dixon, R.A.Dordrecht : Kluwer Academic Publishers; 1993 May.Plant molecular biology v. 22 (2): p. 239-253; 1993 May.  Includes references.
Language:  English
Descriptors: Medicago; Multigene families; Structural genes;Naringenin-chalcone synthase; Complementary  DNA; Nucleotide sequences; Aminoacid sequences; Messenger  RNA; Gene expression; Roots; Root nodules; Stems;Leaves; Flowers; Genetic regulation; Abiotic injuries; Cell wall components;Fungal diseases; Phoma medicaginis; Cell suspensions
Abstract:  We have identified five different full length chalcone synthase(CHS) cDNA clones from a cDNA library produced from transcripts isolated froman elicitor-treated alfalfa cell suspension culture. Nucleotide sequencesimilarity between the clones varied from 88-93%. Oligonucleotides based ondivergent se- quences in the 5'-untranslated regions of the clones coulddistinguish individual genes, or groups of genes and their correspondingtranscripts. Developmentally regulated expression of the CHS transcripts waspredominantly in roots and root nodules; other unidentified members of the CHSgene family are expressed in stems, leaves and nodules. One of the CHStranscripts was strongly expressed in floral tissue. All the CHS transcriptsstudied were induced in elicitor-treated cell suspension cultures. Transcriptswere also induced in roots in response to wounding or spraying with variouselicitors, and in leaves infected with Phoma medicaginis (but not in woundedleaves). The induction kinetics of CHS2 transcripts were more rapid and/ortransient than those of other members of the CHS family in CuCl2-treated rootsand Phoina-infected leaves. The results are discussed in terms of theevolution and functions of the CHS gene family in legumes.
158                                                     NAL Call. No.: 381 Ar2Stress responses in alfalfa (Medicago sativa L.) XVII: molecular cloning andexpression of the elicitor-inducible cinnamic acid 4-hydroxylase cytochromeP450.Fahrendorf, T.; Dixon, R.A.Orlando, Fla. : Academic Press; 1993 Sep.Archives of biochemistry and biophysics v. 305 (2): p. 509-515; 1993 Sep.Includes references.
Language:  English
Descriptors: Medicago sativa; Cell suspensions; Cytochrome p-450; Stress;Phytoalexins; Gene expression; Cloning; Nucleotide sequences; Amino acidsequences
Abstract:  We have isolated cDNA clones encoding a novel class of plantcytochrome P450 by screening an alfalfa cDNA expression library with anantibody against an avocado P450 (CYP73A1) that is expressed during fruitripening but that has not yet been ascribed an in vivo activity. The cDNAsencode a polypeptide of Mr 58,000, pI 9.3, containing sequence similarity (25to 31% overall at the amino acid level) to the avocado P450 and mammalian,yeast, and bacterial P450s, particularly in the presumed heme binding region.Expression studies in yeast confirmed that the P450 clones encode cinnamicacid 4-hydroxylase (CA4H), a key enzyme of the phenylpropanoid pathway inplants. CA4H is encoded by a small gene family in alfalfa, which does notappear to contain homologs of the avocado P450. CA4H transcripts are stronglyinduced by fungal elicitor at the onset of accumulation of isoflavonoidphytoalexins in alfalfa cell suspension cultures.
159                                                    NAL Call. No.: 450 P692Subcellular location of delta-1-pyrroline-5-carboxylase reductase inroot/nodule and leaf of soybean.Szoke, A.; Miao, G.H.; Hong, Z.; Verma, D.P.S.Rockville, Md. : American Society of Plant Physiologists; 1992 Aug.Plant physiology v. 99 (4): p. 1642-1649; 1992 Aug.  Includes references.
Language:  English
Descriptors: Glycine max; Roots; Root nodules; Leaves; Chemical composition;Oxidoreductases; Enzyme activity; Proline; Biosynthesis; Genetic regulation;Gene expression; Escherichia coli; Gene transfer; Nicotiana tabacum;Transgenics; Genetic transformation; Carboxylic acids
Abstract:  The expression of delta-1-pyrroline-5-carboxylate reductase (P5CR)gene was found to be higher in soybean root nodules than in leaves and roots,and its expression in roots appeared to be osmoregulated (AJ Delauney, DPSVerma [1990] Mol Gen Genet 221: 299-305). P5CR was purified to homogeneity asa monomeric protein of 29 kilodaltons by overexpression of a soybean P5CR cDNAclone in Escherichia coli. The pH optimum of the purified P5CR was altered byincreasing the salt concentration, and maximum enzyme activity was attainableat a lower pH under high salt (0.2-1 molar NaCl). Kinetic studies of thepurified enzyme suggested that nicotinamide adenine dinucleotide phosphate+inhibited P5CR activity, whereas nicotinamide adenine dinucleotide+ did not.Subcellular fractionation and antibodies raised against purified soybean P5CRwere used to investigate location of the enzyme in different parts of soybeanas well as in leaves of transgenic tobacco plants synthesizing soybean P5CR.P5CR activity was present in cytoplasm of soybean roots and nodules as well asin leaves, but in leaves, about 15% of the activity was detected in theplastid fraction. The location of P5CR was further confirmed by western blotassay of the proteins from cytosol and plastid fractions of different parts ofthe plant. Expression of soybean nodule cytosolic P5CR in transgenic tobaccounder the control of cauliflower mosaic virus 35S promoter led to theaccumulation of this protein exclusively in the cytoplasm, suggesting that thechloroplastic activity may be due to the presence of a plastid form of theenzyme. The different locations of P5CR in root and leaf suggested thatproline may be synthesized in different subcellular compartments in root andleaf. Proline concentration was not significantly increased in transgenicplants exhibiting high level P5CR activity, indicating that reduction of P5Cis not a rate-limiting step in proline production.
160                                                 NAL Call. No.: SB732.6.M65The sucrose synthase gene is predominantly expressed in the root nodule tissueof Vicia faba.Kuster, H.; Fruhling, M.; Perlick, A.M.; Puhler, A.St. Paul, Minn. : APS Press; 1993 Jul.Molecular plant-microbe interactions : MPMI v. 6 (4): p. 507-514; 1993 Jul.Includes references.
Language:  English
Descriptors: Vicia faba; Structural genes; Complementary  DNA; Sucrosesynthase; Nucleotide sequences; Amino acid sequences; Gene expression; Rootnodules; Messenger  RNA
161                                                    NAL Call. No.: 450 P693A sucrose-synthase gene of Vicia faba L.: Expression pattern in developingseeds in relation to starch synthesis and metabolic regulation.Heim, U.; Weber, H.; Baumlein, H.; Wobus, U.Berlin ; New York : Springer-Verlag, 1925-; 1993.Planta v. 191 (3): p. 394-401; 1993.  Includes references.
Language:  English
Descriptors: Vicia faba; Seed development; Starch; Biosynthesis; Metabolism;Sucrose synthase; Genetic regulation; Genetic code; Gene expression; Proteinsynthesis; Nucleotide sequences; Amino acid sequences; Plant composition
Abstract:  Copy-DNA clones encoding a single class of sucrose-synthase (SUCS;EC 2.4.1.13) subunit have been isolated and sequenced from a Vicia faba L.seed cotyledonary library. Southern analyses indicated the existence of onlyone gene. Transcript levels determined by Northern blot hybridisation steadilyincreased until the middle of development [25-35 days after flowering (DAF)]and declined thereafter. Sucrose levels approximately paralleled levels ofSUCS mRNA. The activity of SUCS increased with decreasing fructose and glucoseconcentrations and peaked about 10 d later than mRNA levels. In-vitro cultureexperiments demonstrated that increasing the sucrose concentration leads toincreased levels of SUCS mRNA. The SUCS mRNA was also synthesised in seed-coattissue, but in lower amounts than in cotyledons and with a differentdevelopmental profile. The early peak level of SUCS mRNA (20 DAF) in seedcoats coincided with the peak in the amount of sucrose and with a peak oftransiently synthesised starch.
162                                                   NAL Call. No.: QK710.P62Suppression of gene expression in plant cells utilizing antisense sequencestranscribed by RNA polymerase III.Bourque, J.E.; Folk, W.R.Dordrecht : Kluwer Academic Publishers; 1992 Jul.Plant molecular biology : an international journal on molecular biology,biochemistry and genetic engineering v. 19 (4): p. 641-647; 1992 Jul.Includes references.
Language:  English
Descriptors: Glycine max; Daucus carota; Antisense  DNA; Recombinant  DNA;Transfer  RNA; Methionine; Reporter genes; Chloramphenicol acetyltransferase;Regulation; Gene expression; Rna polymerase; Enzyme activity; Transcription;Rna
Abstract:  Inverted sequences of the chloramphenicol acetyltransferase (CAT)reporter gene were fused to a soybean tRNA(met(i)) gene lacking a terminatorsuch that the tRNA(met(i)) sequences caused the co-transcription of CATantisense sequences by RNA polymerase III. When electroporated into carrotprotoplasts, these antisense DNA constructs suppressed CAT enzyme activityexpressed from co-electroporated DNAs containing the CAT gene downstream ofthe cauliflower mosaic virus (CaMV) 35S RNA promoter. Our most effectiveconstruct, an antisense sequence complementary to the 3' portion of the CATgene, inhibited CAT activity five-fold greater than an antisense constructexpressed by RNA polymerase II from the cauliflower mosaic virus 35S RNApromoter. These results indicate that antisense sequences transcribed by RNApolymerase III should efficiently suppress gene expression in plants.
163                                                   NAL Call. No.: QK710.P62A survey of transcripts expressed specifically in root nodules of broadbean(Vicia faba L.).Perlick, A.M.; Puhler, A.Dordrecht : Kluwer Academic Publishers; 1993 Sep.Plant molecular biology v. 22 (6): p. 957-970; 1993 Sep.  Includes references.
Language:  English
Descriptors: Vicia faba; Messenger  RNA; Transcription; Root nodules; Geneexpression; Complementary  DNA; Dna libraries; Nodulins; Leghemoglobin; Plantproteins; Sucrose synthase; Aspartate-ammonia ligase; Lipoxygenase
Abstract:  More than 600 potentially nodule-specific clones have been detectedby differential hybridization of a broadbean cDNA library constructed fromroot nodule poly(A)(+) RNA. These isolated cDNAs belong to at least 28different clone groups containing cross-hybridizing sequences. The number ofclones within a clone group varies from about 200 to only one single clone.Northern hybridization experiments revealed nodule-specific transcripts for 14clone groups and markedly nodule-enhanced transcripts for another 7 clonegroups. Sequence homologies indicate that three transcript sequences code fordifferent leghemoglobins. Two other transcripts encode a nodule-specificsucrose synthase and a nodule-enhanced asparagine synthetase, respectively.Four deduced gene products are proline-rich, two of them being the homologuesof PsENOD2 and PsENOD12. The third proline-rich protein (PRP) is composed ofsimilar amino acid repeats as the nodule-specific PsENOD12 but is expressed innodules and roots in comparable amounts. The fourth PRP is a nodule-enhancedextensin-type protein built up by Ser-Pro4 repeats. Two furthernodule-specific transcripts encode gene products showing some similarity tostructural glycine-rich proteins. Additionally, transcripts could beidentified for broadbean homologues of the nodulins MsNOD25, PsENOD3 andPsENOD5 and transcripts specifying a nodule-enhanced lipoxygenase and atranslation elongation factor EF-1alpha, which is expressed in all broadbeantissues tested.
164                                                    NAL Call. No.: QD415.F4Thermal injury and ozone stress affect soybean lipoxygenases expression.Maccarrone, M.; Veldink, G.A.; Vliegenthart, J.F.G.Amsterdam, Netherlands : Elsevier Science Publishers; 1992 Sep14.F E B S letters : Federation of European Biochemical Societies v. 309 (3): p.225-230; 1992 Sep14.  Includes references.
Language:  English
Descriptors: Glycine max; Structural genes; Lipoxygenase; Isoenzymes; Geneexpression; Transcription; Messenger  RNA; Genetic regulation; Ozone; Heatshock; Cold shock; Enzyme activity; Seedlings; Cold stress; Heat stress;Translation
Abstract:  The effects of thermal injury (cold and heat shock) and ozonetreatment on lipoxygenases 1 (LOX-1) and 2 (LOX-2) of soybean seedlings havebeen investigated. Cold stress led to a decrease of the specific activities ofboth isoenzymes, attributable at least in part to a down-regulation of geneexpression at the translational level. Both heat shock and ozone treatmentenhanced lipoxygenases-specific activities, acting at the level oftranscription of the genes. It is proposed that LOX-1 and LOX-2 are involvedin the thermotolerance of soybeans and in the precocious aging induced byozone.
165                                                   NAL Call. No.: QK710.P68Tissue-specific expression of sunflower heat shock proteins in response towater stress.Almoguera, C.; Coca, M.A.; Jordano, J.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. 947-958; 1993Dec.  Includes references.
Language:  English
Descriptors: Helianthus annuus; Gene expression; Genetic code; Heat shockproteins; Messenger  RNA; Protein synthesis; Responses; Water stress
166                                                    NAL Call. No.: 450 P692Tissue-specific expression of the alternative oxidase in soybean and siratro.Kearns, A.; Whelan, J.; Young, S.; Elthon, T.E.; Day, D.A.Rockville, Md. : American Society of Plant Physiologists; 1992 Jun.Plant physiology v. 99 (2): p. 712-717; 1992 Jun.  Includes references.
Language:  English
Descriptors: Glycine max; Macroptilium atropurpureum; Bradyrhizobiumjaponicum; Bradyrhizobium; Shoots; Roots; Root nodules; Oxidoreductases;Enzyme activity; Respiration; Mitochondria; Gene expression; Geneticregulation; Protein synthesis
Abstract:  Alternative oxidase activity (cyanide-insensitive respiration) wasmeasured in mitochondria from the shoots, roots, and nodules of soybean(Glycine max L.) and siratro (Macroptilium atropurpureum) plants. Activity washighest in the shoots and lowest in the nodules. Alternative oxidase activitywas associated with one (roots) or two (shoots) proteins between 30 and 35kilodaltons that were detected by western blotting with a monoclonal antibodyagainst Sauromatum guttatum alternative oxidase. No such protein was detectedin nodule mitochondria. Measurements of oxygen uptake by isolated soybean rootand nodule cells in the presence of cyanide and salicylhydroxamic acidindicated that alternative oxidase activity was confined to the uninfectedcortex cells of the nodule. Immunoprecipitation of translation products ofmRNA isolated from soybean shoots revealed a major band at 43 kilodaltons thatis assumed to be the precursor of an alternative oxidase protein. This bandwas not seen when mRNA from nodules was treated in the same fashion. Theresults indicate that tissue-specific expression of the alternative oxidaseoccurs in soybean and siratro.
167                                              NAL Call. No.: S494.5.B563C87Transcriptional regulation of auxin-responsive genes.Gulfoyle, T.J.; Hagen, G.; Li, Y.; Gee, M.A.; Martin, G.; Ulmasov, T.N.Dordrecht : Kluwer Academic Publishers; 1992.Current plant science and biotechnology in agriculture v. 13: p. 129-135;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: Glycine max; Structural genes; Multigene families; Promoters;Plant proteins; Gene expression; Messenger  RNA; Genetic regulation; Auxins
168                                              NAL Call. No.: S494.5.B563C87Transcriptional regulation of phytoalexin biosynthetic genes.Dixon, R.A.; Bhattacharyya, M.K.; Harrison, M.J.; Faktor, O.; Lamb, C.J.;Loake, G.J.; Ni, W.; Oommen, A.; Paiva, N.; Stermer, B.Dordrecht : Kluwer Academic Publishers; 1993.Current plant science and biotechnology in agriculture v. 14: p. 497-509;1993.  In the series analytic: Advances in molecular genetics of plant-microbeinteractions. 2 / edited by E.W. Nester, and D.P.S. Verma.  Proceedings of the6th International Symposium on Molecular Plant-Microbe Interactions held July1992, Seattle, Washington.  Includes references.
Language:  English
Descriptors: Medicago sativa; Structural genes; Naringenin-chalcone synthase;Oxidoreductases; Hydroxymethylglutaryl-coa reductase; Promoters; Dna bindingproteins; Transcription; Gene expression; Genetic regulation; Phytoalexins;Biosynthesis
169                                                    NAL Call. No.: QH426.M6Transformation and foreign gene expression.Moloney, M.M.; Holbrook, L.A.New York : Springer-Verlag; 1993.Monographs on theoretical and applied genetics v. 19: p. 148-167; 1993.  Inthe series analytic: Breeding oilseed brassicas / edited by K.S. Labana, S.S.Banga and S.K. Banga.  Literature review.  Includes references.
Language:  English
Descriptors: Brassica napus; Brassica campestris; Brassica juncea; Genetictransformation; Agrobacterium tumefaciens; Plasmid vectors; Direct  DNAuptake;Transgenic plants; Gene transfer; Genetic vectors; Cauliflower mosaiccaulimovirus; Literature reviews; Gene expression
170                                                    NAL Call. No.: SB249.N6Transient expression of beta-glucuronidase gene in new hybrid of fineextra-long staple Egyptian cotton seedlings following biolistic particlebombardment.Momtaz, O.A.; Madkour, M.A.Memphis, Tenn. : National Cotton Council of America, 1991-; 1993.Proceedings / v. 2: p. 624-627; 1993.  Meeting held on January 10-14, 1993,New Orleans, Louisiana.  Includes references.
Language:  English
Descriptors: Egypt; Cabt; Gossypium barbadense; Beta-glucuronidase; Hybrids;Direct  DNAuptake; Genetic transformation; Gene expression
171                                                   NAL Call. No.: QK710.P62A tRNA Val(GAC) gene of chloroplast origin in sunflower mitochondria is nottranscribed.Ceci, L.R.; Saiardi, A.; Siculella, L.; Quagliariello, C.Dordrecht : Kluwer Academic Publishers; 1993 Nov.Plant molecular biology v. 23 (4): p. 727-736; 1993 Nov.  Includes references.
Language:  English
Descriptors: Helianthus annuus; Structural genes; Transfer  RNA; Valine;Mitochondrial  DNA; Gene expression; Transcription; Genomes; Chloroplasts;Mitochondrial genetics; Nucleotide sequences; Amino acid sequences;Chloroplast genetics; Repetitive  DNA; Molecular conformation; Promoters
Abstract:  A tRNA(Val) (GAC) gene is located in opposite orientation 552nucleotides (nt) down-stream of the cytochrome oxidase subunit III (coxIII)gene in sunflower mitochondria. The comparison with the homologous chloroplastDNA revealed that the tRNA(Val) gene is part of a 417 nucleotides DNAinsertion of chloroplast origin in the mitochondrial genome. No tRNA(Val) isencoded in monocot mitochondrial DNA (mtDNA), whereas two tRNA(Val) speciesare coded for by potato mtDNA. The mitochondrial genomes of different plantspecies thus seem to encode unique sets of tRNAs and must thus be competent inimporting the missing differing sets of tRNAs.
172                                                   NAL Call. No.: QK710.P62Two classes of differentially regulated glutamine synthetase genes areexpressed in the soybean nodule: a nodule-specific class and a constitutivelyexpressed class.Roche, D.; Temple, S.J.; Sengupta-Goplan, C.Dordrecht : Kluwer Academic Publishers; 1993 Sep.Plant molecular biology v. 22 (6): p. 971-983; 1993 Sep.  Includes references.
Language:  English
Descriptors: Glycine max; Multigene families; Complementary  DNA;Glutamate-ammonia ligase; Nucleotide sequences; Amino acid sequences; Geneexpression; Genetic regulation; Root nodules; Cotyledons; Plant tissues;Messenger  RNA
Abstract:  We have characterized two sets of cDNA clones representing theglutamine synthetase (GS) mRNA in soybean nodules. Using the 3'-untranslatedregions of a representative member of each set, as gene member(s) specificprobes, we have shown that one set of the GS genes are expressed in anodule-specific manner, while the other set is expressed in other tissues,besides the nodules. The nodule-specific GS genes are expressed in adevelopmentally regulated manner in the nodules, independent of the onset ofnitrogen fixation. The other class of GS genes is expressed constitutively inall tissues tested, but its expression level is dramatically enhanced innodules following onset of N2 fixation. The latter set of genes is alsoexpressed in cotyledons of germinating seedlings in a developmentallyregulated manner. Analysis of hybrid select translation products and genomicSouthern blots suggests that multiple gene members in each class are expressedin the nodules.
173                                                    NAL Call. No.: 500 N21PTwo functional soybean genes encoding p34cdc2 protein kinases are regulated bydifferent plant developmental pathways.Miao, G.H.; Hong, Z.; Verma, D.P.S.Washington, D.C. : The Academy; 1993 Feb01.Proceedings of the National Academy of Sciences of the United States ofAmerica v. 90 (3): p. 943-947; 1993 Feb01.  Includes references.
Language:  English
Descriptors: Glycine max; Amino acid sequences; Gene expression; Genetic code;Genetic regulation; Meristems; Nodules; Nucleotide sequences; Plantdevelopment; Protein kinase; Rhizobium; Saccharomyces cerevisiae
Abstract:  We have isolated two cDNA clones (cdc2-S5 and cdc2-S6) encodingp34cdc2 protein kinases, homologs of yeast cdc2/CDC28 genes, from a soybeannodule cDNA library. The two sequences share 90% sequence homology in thecoding regions. The 5' and 3' noncoding regions are distinct from each other,however, indicating that at least two genes encode p34cdc2 protein kinases insoybean. Both sequences can rescue the cdc28 mutation in Saccharomycescerevisiae but rescue it with different efficiency. Genomic Southern analysisshowed the existence of two copies for each of these genes, which are notclosely linked and are nonallelic. The relative expression level of the twosoybean p34cdc2 genes varies in different tissues. Expression of cdc2-S5 ishigher in roots and root nodules, whereas cdc2-S6 is more actively expressedin aerial tissues, indicating that regulation of these two p34cdc2 gene.9 iscoupled with plant developmental pathways. Expression of cdc2-S5 is,furthermore, enhanced after Rhizobium infection, whereas cdc2-S6 fails torespond, suggesting that cdc2-S5 plays a role in nodule initiation andorganogenesis. This latter gene preferentially responds to auxin(alpha-naphthaleneacetic acid) treatment, indicating that phytohormones may beinvolved in the control of cell division mediated by Rhizobium infection.Thus, different p34cdc2 protein kinases may control cell division in differenttissues in a multicellular organism and respond to different signals--e.g.,phytohormones.
174                                                   NAL Call. No.: 442.8 Z34Use of the polymerase chain reaction to isolate an S-locus glycoprotein cDNAintrogressed from Brassica campestris into B. napus ssp. oleifera.Goring, D.R.; Banks, P.; Beversdorf, W.D.; Rothstein, S.J.Berlin, W. Ger. : Springer International; 1992 Aug.M G G : Molecular and general genetics v. 234 (2): p. 185-192; 1992 Aug.Includes references.
Language:  English
Descriptors: Brassica napus var. oleifera; Brassica campestris; Introgression;Structural genes; Dna; Glycoproteins; Loci; Self incompatibility; Nucleotidesequences; Gene expression; Alleles; Segregation; Polymerase chain reaction;Amino acid sequences; Inheritance
Abstract:  A self-incompatible canola-quality Brassica napus ssp. oleiferaline (W1) was generated by introgressing the S-locus from a self-incompatibleB. campestris plant into the Westar cultivar. Using the polymerase chainreaction (PCR) with primers derived from conserved regions in S-locusglycoprotein (SLG) alleles, the central region of the active SLG gene (910)was obtained. The remaining portions of the cDNA for this 910 gene weresubsequently cloned using the PCR-rapid amplification of cDNA ends (RACE)procedure. Sequence analysis revealed that the 910 cDNA show a high degree ofsequence similarity to SLG alleles associated with Class I self-incompatiblelines. The 910 gene was found to be absent in the original self-compatible cv.Westar (B. napus) and segregated with self-incompatibility in a mixedpopulation generated from a cross between self-incompatible W1 andself-compatible Westar. RNA blot analysis indicated that high levels of 910mRNAs were present in the stigma as buds approached anthesis. Thus, the SLGallele of W1 transferred from B. campestris via backcrosses to a line of cv.Westar has been identified.
175                                                  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.
Abbott, L.K.  3  Ainley, W.M.  135  Allen, T.  146  Allison, L.A.  91  Almoguera, C.  52, 165  Altenbach, S.B.  2  Amasino, R.M.  28  Anderson, D.M.  33  Anderson, E.J.  24  Arahira, M.  35  Arias, J.A.  59  Axelos, M.  6  Axelrod, B.  43  Bagga, S.  45� Baird, W.V.  61  Baker, M.E.  62  Bako, L.  7, 55  Bal, A.K.  139  Baltz, R.  27  Banks, P.  174  Banks, S.W.  11  Barker, D.G.  58, 137  Barz, W.  102  Bauer, P.  91  Baumlein, H.  36, 41, 161  Beachy, R.N.  72, 141  Bedinger, P.A.  175  Belanger, F.  134  Bergman, J.W.  10  Bernier, F.  101  Beversdorf, W.D.  174  Bewley, J.D.  46  Bhattacharyya, M.K.  168  Billy, F. de  137  Bisseling, T.  29, 31  Blank, C. de  31  Bogre, L.  7, 12, 19, 55, 119, 129  Boller, T.  32  Bonham-Smith, P.C.  50, 116  Bourque, J.E.  162  Boutry, M.  143  Bradley, D.  144  Brangeon, J.  77  Breda, C.  56, 127  Brenner, M.L.  135  Briquet, M.  143  Broadwater, A.H.  175  Broer, I.  88  Brown, D.C.W.  79  Brussel, A.N.A. van  4, 5  Buffard, D.  56, 127  Burkard, G.  54  Buzzell, R.I.  154  Caredda, S.  8  Carrayol, E.  120  Castonguay, Y.  78, 124, 125  Ceci, L.R.  171  Chamberland, S.  101  Chang, M.M.  111  Chang, Y.C. p34, 156  Chanut, F.A.  42  Chay, C.H.  175  Chen, T.H.H.  118  Cheon, C.I.  139  Chino, M.  64  Choudhary, A.D.  108  Christou, P.  131  Clark, D.C.  68  Clemens, J.C.  43  Clouse, S.D.  62  Coca, M.A.  165  Cocks, P.S.  8  Collins, G.B.  73  Covello, P.S.  149  Creelman, R.A.  47, 100  Crow, L.J.  81  Crowell, D.N.  28  Cullimore, J.V.  58  Cummins, I.  22  Curie, C.  6  Curry, J.  37  Czarnecka, E.  16  Daigle, N.  101  Dalkin, K.  108, 157  Datta, N.  120, 96  Davies, S.P.  87  Davis, L.C.  126  Day, D.A.  166  Dazzo, F.B.  158, 133  Dedeoglu, D.  7  Dedieu, A.  137  Deineko, E.V.  84  Delorme, R.M.  123  Deng, W.  73  DeWald, D.B.  47, 90  Dhindsa, R.S.  21, 39, 125, 148  Dhir, S.  134  Dhir, S.K.  134  Dickstein, R.  66  Didierjean, L.  54  Dietrich, R.A.  60  Dixon, J.E.  43  Dixon, R.A.  40, 59, 93, 108, 109, 110, 142, 157, 158, 168  Domon, C.  27  Dong, G.  148  Dong, J.L.  80  Donoho, G.P.  43  Dube, S.  112  Duc, G.  122, 143  Dudits, D.  7, 12, 55, 147  Dunn, K.  146  Dure L. III  145  Dwivedi, R.S.  155  Dyer, W.E.  10  Ebel, J.  115  Edwards, R.  108  El Turk, J.  127  Elthon, T.E.  166  Esnault, R.  56, 127  Estabrook, E.  92  Fahrendorf, T.  108, 158  Faktor, O.  40, 168  Falk, A.  85  Farmer, E.E.  136  Farnden, K.J.F.  94  Farrand, S.K.  134  Feder, A.I.  92  Fiedler, U.  41  Filistein, R.  41  Flamand, M.C.  143  Folk, W.R.  162  Fowler, T.J.  51  Franceschi, V.R.  1, 67  Franssen, H.  29, 31  Fruhling, M.  160  Fujiwara, T.  64, 72, 141  Fukazawa, C.  35  Ganter, G.  146  Gantt, J.S.  13, 113  Gartner, A.  12  Gee, M.  17  Gee, M.A.  70, 167  Geng, X.M.  79  Georgescu, A.  2  Gesteland, R.F.  42  Gidamis, A.B.  48, 63  Gijzen, M.  154  Glascock, C.B.  79, 75  Goblet, J.P.  143  Goldberg, R.B.  121  Goldmark, P.J.  37  Gonsalves, D.  38  Gordon, A.J.  23  Goring, D.R.  174  Gossett, D.R.  11  Gowri, G.  108  Grabau, E.A.  42  Grant, M.R.  94  Gray, M.W.  149  Grayburn, W.S.  73  Gregerson, R.G.  113  Grimes, H.D.  1, 67  Grula, J.W.  33  Guilfoyle, T.J.  14, 17, 70  Gulfoyle, T.J.  167  Gurley, W.B.  16  Gyorgyey, J.  12, 55  Hadwiger, L.A.  111  Hagen, G.  14, 17, 70, 167  Hamilton-Kemp, T.R.  73  Harada, J.J.  60  Harada, K.  83  Harrison, M.J.  93, 108, 109, 168  Harter, K.  102  Haser, A.  122  Hata, S.  119, 95  Heberle-Bors, E.  12, 19, 119, 129  Heim, U.  161  Hellyer, A.  97  Hendriks, P.  29  Herman, E.  112  Herman, E.M.  155  Hildebrand, D.F.  73  Hill, D.F.  94  Hill, J.W.  135  Hillemann, D.  88  Hilu, K.  61  Hirai, M.Y.  64  Hirel, B.  77, 120  Hirsch, A.M.  18, 82E Hirt, H.  12, 19, 119, 129  Hitz, W.D.  1  Hoarau, A.  77  Hoarau, J.  77  Hobbs, S.L.  33  Holbrook, L.A.  169  Hong, Z.  159, 173  Horn, R.  107  Horovitz, D.  111  Howieson, J.G.  3, 8  Hu, C.A.  140  Hu, J.S.  38  Hu, W.H.  25  Hudspeth, R.L.  33  Huet, J.C.  26  Huiwen, Z.  79  Huystee, R.B. van  56  Ingersoll, J.C.  16  Inze, D.  36  Itoh, Y. E35  Iwamoto, H.  152  James, C.L.  23  John, M.E.  28, 81  Johnson, R.R.  136  Johnson, W.B.  105  Johnson-Flanagan, A.M.  79  Jonak, C.  12, 119, 129  Jordano, J.  52, 165  Journet, E.P.  137  Junghans, H.  157  Kalinski, A.  112, 155  Kammen, A. van  29  Kamoun, S.  79, 75  Kanamori, J.  63  Kandasamy, M.K.  71  Kang, I.J.  63  Kapazoglou, A.  145  Kapros, T.  7, 55, 147  Katinakis, P.  29, 31  Kato, T.  15, 20, 152  Kawamura, Y.  20  Kawasaki, T.  20  Kearns, A.  166  Keddie, J.S.  68  Kemp, J.D.  45  Kennedy, R.A.  44  Key, J.L.  120, 96, 128, 135  Kijne, J.W.  4, 5  Kikuchi, A.  83  Kiss, G.B.  91  Kitamura, K.  83  Kitamura, Y.  35  Kito, M.  48, 63  Klapper, D.G.  175  Knauf, V.C.  105  Knight, T.J.  106  Knox, R.B.  87  Knutzon, D.S.  105  Komarova, M.L.  84  Komeda, Y.  64  Kondorosi, A.  91, 127  Kondorosi, E.  91  Kouchi, H.  119, 95  Kridl, J.C.  105  Kriz, A.L.  134  Krochko, J.E.  46R Kroner, P.A.  120, 96  Kuo, C.C.  2  Kuster, H.  160  Kwan, B.Y.H.  87  Laberge, S.  78, 124, 125  LaCelle, M.G.  11  LaFayette, P.R.  120, 96  Lam, E.  86  Lamb, C.J.  40, 59, 108, 168  Langis, R.  21  Langner, C.A.  61  Larsen, K.  58  Lauridsen, P.  104  Laursen, N.B.  150  Leaver, C.J.  49  Lee, N.G.  139  Lee, S.P.  118  Lenman, M.  85  Lescure, B.  6 Lessard, P.A.  141  Li, J.L.  80  Li, M.  68  Li, N.  112  Li, Y.  14, 17, 70, 167  Liboz, T.  6  Lin, J.J.  44  Lingle, W.L.  135  Liu, D.  112  Liu, Z.  17  Loader, N.M.  97  Loake, G.J.  40, 108, 168  Lobler, M.  18, 82  Loi, A.  8  Lough, T.J.  94  Lucas, M.C.  11  Lugtenbergh, B.J.J.  4, 5  Maccarrone, M.  164  Machlin, S.  144  Machmudova, A. I99  Madkour, M.A.  170  Madsen, O.  151  Magyar, Z.  7, 147  Mairinger, T.  119  Marcker, K.A.  104, 150, 151  Margis-Pinheiro, M.  54  Markley, N.A.  116  Marsolier, M.C.  77, 120  Martin, C.  54  Martin, G.  70, 167  Mason, H.S.  47, 90  Mattoo, A.K.  112  Maxwell, C.A.  108, 109  McCabe, D.E.  131  McHughen, A.  9  McKhann, H.I.  18  McMorris, T.C.  62  McNeil, K.J.  135  Mellor, R.B.  32  Melroy, D.L.  155  Meskiene, I.  19, 119  Miao, G.H.  153, 159, 173  Mikami, B.  48  Milhollon, E.P.  11  Miller, S.S.  13, 113  Mink, M.  12  Mitchell-Olds, T.  144  Moloney, M.M.  50, 116, 169  Momtaz, O.A.  170  Moneger, F.  49  Monroy, A.  148  Monroy, A.F.  39, 125  Montane, M.H.  6  Morris, C.F.  37  Mujer, C.V.  44  Muller, J.  32  Mullet, J.E.  47, 90, 100  Mur, L.A.  4, 5  Murphy, D.J.  22, 68  Mylona, P.  31  Nadeau, P.  78  Nagao, R.T.  120, 96, 128, 135  Nagpala, P.G.  38  Nagy, I.  36  Naito, S.  64  Narvaez-Vasquez, J.  53  Nasrallah, J.B.  71, 130  Nasrallah, M.E.  71, 130  Nemeth, K.  55  Ngo, W.  66  Ni, W.  168  Nishio, T.  71  Nugent, J.M.  30  Nykiforuk, C.L.  79  O'Brian, M.R.  74  O'Brien, A.P.  87  Oancia, T.L.  50  Ocsovszky, I.  147  Ohta, H.  15  Okamuro, J.K.  121  Okubo, K.  83  Oommen, A.  168  Orozco-Cardenas, M.L.  53  Ougham, H.J.  23  Overvoorde, P.J.  1  Paiva, N.  168  Palmer, J.D.  30  Pang, S.Z.  38  Paolillo, D.J.  71  Parthier, B.  99  Pathirana, S.M.  13  Pay, A.  19, 119, 129  Pearson, K.W.  2  Peng, T.  66  Perlick, A.M.  160, 163  Pernollet, J.C.  26  Pfosser, M.  12  Pichon, M.  137  Pierre, M.  91  Pillay, D.T.N.  27  Pladys, D.  132  Poiret, M.  91  Potenza, C.  92  Pramanik, S.K.  46  Prusty, R.  66  Puhler, A.  88, 160, 163  Quagliariello, C.  138, 171  Radke, S.E.  60, 105  Ragland, M.  76  Raja, S.  146  Ramiov, K.B.  150  Rask, L.  85  Recourt, K.� 4, 5  Reddington, B.D.  94  Reinbothe, C.  99  Reinbothe, S.  99  Reviron, M.P.  26  Reynolds, P.H.S.  94  Ricardo, C.P.  117  Ripp, K.  1  Rivkin, M.I.  84  Robinson, D.L.  122  Robinson, S.J.  98  Robson, A.D.  3  Roche, D.  172  Rodrigues-Pousada, C.  117  Romero, L.C.  86  Rothstein, S.J.  174  Rouan, D.  6  Rubinstein, A.L.  175  Rumpho, M.E.  44  Russell, D.  28  Ryan, C.A.  53, 136  Safford, R.  97, 98  Sagliocco, F.  145  Saiardi, A.  138, 171  Sakai, F.  80  Sallantin, M.  26  Sallaud, C.  127  Salzwedel, J.L.  158, 133  Sandal, L.  151  Sandal, N.N.  151  Sangwan, I.  74  Sarhan, F.  39, 125  Sato, T.  71  Savka, M.A.  134  Savoure, A.  91  Schafer, E.  102  Schafer, R.  77  Schoelz, J.E.  24  Schroder, J.  69  Sehgal, O.P.  24  Sengupta-Gopalan, C.  45, 92, 106  Sengupta-Goplan, C.  172  She, Q.  104  Shen, B.  126  Shen, S.C.  25  Shen, W.  25  Shibata, D.  15, 20, 152  Shirano, Y.  152  Shorrosh, B.S.  110, 142  Shumnyi, A.V.K.  84  Siculella, L.  171  Siddique, A.B.M.  139  Siemieniak, D.R.  38  Silva, J. de  98  Simpson, R.B.  135  Singh, J.  79  Singh, M.  87  Skorupska, H.T.  123  Slabas, A.R.  97  Slightom, J.L.  38  Slocum, R.D.  114  Smart, C.J.  49  Smith, L.J.  68  Smith, M.E.  66  Smolders, A.  29  Spee, J.  29  Staehelin, C.  32  Stanford, A.C.  58  Staraci, L.C.  2  Steczko, J.  43  Stefanov, I.  147  Steinmetz, A.  27  Stermer, B.  168  Stougaard, J.  104, 150  Strabala, T.  17  Sugimoto, T.  20� Sutton, D.  45  Suzuki, H.  51, 57  Szalay, A.  119  Szoke, A.  159  Talke-Messerer, C.  102  Tanaka, K.  15  Taylor, M.G.  65  Temple, S.J.  106, 172  Theil, E.C.  76  Thiele, D.J.  103  Thompson, G.A.  105  Tierney, M.L.  51, 57, 100  Toriyama, K.  71  Townsend, J.  2  Tranbarger, T.J.  67  Trese, A.T.  24  Truchet, G.  137  Tsukamoto, C.  83  Tunen, A.J. van  4, 5  Twary, S.N.  113  Tyler, B.M.  79, 75  Tyson, H.  21  Uhlmann, A.  115  Ulmasov, T.  17  Ulmasov, T.N.  70, 167  Unkefer, P.J.  106  Utsumi, S.  48, 63  Van Huystee, R.  154  Vance, C.P.  13, 113, 122, 132  Vartanian, N.  26  Vasil, I.K.  65  Vasil, V.  65  Vassilevskaia, T.D.  117  Veldink, G.A.  164  Verma, D.P.S.  77, 139, 140, 153, 159, 173  Vershinin, A.V. '84  Vezina, L.P.  124, 125  Vienne, D. de  26  Villarroel, R.  36  Vliegenthart, J.F.G.  164  Vries, F. de  29  Wagner, T.  57  Wainwright, C.  2  Walker-Simmons, M.K.  37  Walling, L.L.  34, 156  Walter, C.  88  Warkentin, T.D.  9  Wasternack, C.  99  Waterborg, J.H.  89  Weber, H.  161  Welle, R.  69  Werth, C.R.  61  Whelan, J.  166  Whittier, R.F.  20  Widholm, J.M.  134  Wiemken, A.  32  Williamson, C.L.  114  Wobus, U.  36, 41, 161  Wolfraim, L.  148  Wolfraim, L.A.  21  Woolner, E.M.  97  Wu, S.C.  55  Wyatt, R.E.  128  Xu, H.  87  Xu, X.L.  25, 80  Xue, J.  85  Xue, Z.T.  25  Yang, W.C.  29, 31  Ying, M.C.  10  Young, M.  79, 75  Young, S.  166  Zetsche, K.  107  Zhang, M.  140  Zhuang, N.L.  25  Zurek, D.M.  62  2,4-d  7, 57, 62  Abiotic injuries  28, 57, 90, 157  Abscisic acid  37, 52, 79, 118  Acc  112  Acclimatization  21, 39, 118, 124  Acetylene reduction  122  Acid phosphatase  90  Acidity  3  Active transport  1  Acyltransferases  88, 135  Adaptation  8, 26  Aerobic treatment  44  Agrobacterium  11, 72  Agrobacterium rhizogenes  51  Agrobacterium tumefaciens  9, 10, 14, 16, 18, 35, 45, 51, 71, 84,98, 101,135, 169  Albumins  2  Alcohol dehydrogenase  16  Alcohol oxidoreductases  118  Alfalfa mosaic virus  54  Alleles  61, 121, 123, 154, 174  Allergens  175  Amino acid sequences  1, 12, 13, 15, 17, 19-22, 25-28, 30, 31, 33,37, 38,42, 43, 50, 54, 66, 74, 81, 82, 85, 87, 91, 94-97, 109-120,124, 125, 127, 129, 137, 139, 142, 144, 145, 149, 151-153, 157,158,160, 161, 171-175  Amino acids  2, 67  Aminotransferases  74  Ammonia  77, 120  Anaerobic conditions  44  Anthers  87  Antigens  116  Antisense  DNA  162  Antisense  RNA  106, 139, 141  Apical meristems  50  Arabidopsis  17  Arabidopsis thaliana  6, 85, 87  Arachis hypogaea  56  Asparaginase  94  Aspartate-ammonia ligase  163  Auxins  17, 70, 120, 96, 112, 120, 96, 167  Bacterial proteins  4, 5  Bacteroids  113, 122, 140  Bertholletia excelsa  2  Beta-glucan  115  Beta-glucanase  111  Beta-glucuronidase  9, 10, 11, 14, 17, 33, 35, 41, 51, 60, 65, 72,80, 87,90, 98, 101, 104, 131, 141, 147, 170  Binding proteins  1, 86, 139  Binding site  16, 27, 35, 43  Biochemical pathways  108  Biochemical polymorphism  83  Biosynthesis  4, 5, 69, 93, 105, 108, 159, 161, 168  Bradyrhizobium  166  Bradyrhizobium japonicum  31, 32, 92, 95, 119, 126, 139, 166  Brassica campestris  6, 30, 71, 75, 79, 87, 105, 130, 144, 169, 174 
Brassica campestris var. rapa  24  Brassica juncea  169  Brassica napus  2, 50, 60, 71, 79, 85, 97, 98, 102, 105, 116, 130,169  Brassica napus var. oleifera  26, 174  Brassica oleracea  71, 130  Brassinolide  62  Bromus inermis  118  Bromus secalinus  37  Buds  10, 12, 50  Cabt  170  Calcium  3  Calcium ions  39  Callus  7, 10, 88, 134  Carboxylic acids  159  Carthamus tinctorius  10  Cauliflower mosaic caulimovirus  24, 45, 53, 169  Cell differentiation  18, 60, 92, 119, 95, 119, 95, 122, 139, 140 
Cell division  7, 12, 19, 29, 147  Cell growth  55  Cell membranes  139  Cell suspensions  7, 21, 39, 56, 65, 88, 102, 118, 119, 157, 158  Cell ultrastructure  71  Cell wall components  51, 57, 75, 79 100, 115, 128, 157  Cellular biology  100  Chalcone isomerase  92, 127  Chemical composition  159  Chemical reactions  16, 89  Chimeras  2, 24, 131  Chitinase  32, 54  Chitosan  111  Chlamydomonas reinhardtii  103  Chloramphenicol acetyltransferase  104, 162  Chlorophyll a/b binding protein  33, 34, 102, 145, 156  Chloroplast genetics  171  Chloroplasts  123, 171  Chromatin  89  Clones  55, 129  Cloning  37, 38, 43, 50, 54, 69, 81, 118, 152, 158  Coat proteins  38  Cold  21, 39, 78, 118, 125  Cold hardening  78, 125  Cold shock  164  Cold stress  124, 164  Cold tolerance  78, 148  Comparisons  175  Complementary  DNA  19, 21, 27, 31, 54, 66, 74, 87, 95-97,106, 113-120, 124, 125, 127, 139, 151, 153, 157, 160, 163, 172, 175 
Complementation  19  Controlling elements  6, 60, 101, 121  Cortex  32, 60  Cotyledons  1, 15, 34, 99, 128, 145, 156, 172  Crops  75, 79  Crystallization  48  Crystals  48  Cultivars  25, 78, 123, 154  Culture media  10  Cysteine  63, 132  Cytochrome p-450  158  Cytochrome-c oxidase  138, 149  Cytokinins  14, 17  Cytoplasm  77  Cytoplasmic male sterility  49, 107, 143  Cytosol  77  Dark  23  Daucus carota  162  Defense mechanisms  54, 111, 115, 127  Deletions  35, 41, 51, 63, 90, 104  Derivatives  90, 136  Desiccation  79  Developmental stages  29, 131, 156  Diploidy  61  Direct  DNAuptake  65, 169, 170  Disease resistance  32, 75, 79, 111, 127  Dna  1, 12, 13, 20, 24, 36, 52, 69, 94, 110, 111, 129, 142, 143,174  Dna binding proteins  6, 16, 27, 35, 168  Dna libraries  81, 163  Dna polymerase  116  Dna replication  116  Dna sequencing  38  Drought  26, 124  Dwarfing  24  Echinochloa  44  Echinochloa crus-galli  44  Echinochloa crus-pavonis  44  Echinochloa muricata  44  Echinochloa oryzoides� 44  Edaphic factors  8  Egypt  170  Electrophoresis  123  Eleusine  61  Embryogenesis  34, 35, 52, 60, 99, 121  Environmental factors  8  Enzyme activity  4, 5, 7, 11, 13, 23, 43, 56, 67, 69, 72-74, 76,88,106, 108, 113, 120, 122, 131-133, 141, 154, 158, 159, 162, 164, 166 
Enzyme inhibitors  39, 136  Enzyme polymorphism  123  Enzyme precursors  97  Enzymes  122  Epicotyls  62  Epidermis  51, 119, 95, 119, 95, 128, 137  Escherichia coli  3, 14, 48, 63, 68, 159  Ethylene  56, 112  Etiolation  74  Evolution  6, 149  Exons  25, 45, 153  Explants  10  Extracts  9  Fatty acids  73  Ferritin  76  Flavonoids  4, 5, 93, 108  Flowering  119  Flowers  12, 50, 53, 117, 157  Freezing  39, 78, 118, 125  Frost  79  Fructose  47  Fungal diseases  111, 157  Fusarium solani f.sp. phaseoli  111  Fusarium solani f.sp. pisi  111  Gelation  63  Gels  63  Gene expression  1-69, 71-175  Gene transfer  2, 11, 53, 63, 64, 68, 120, 134, 159, 169  Genes  2, 3, 14, 24, 38, 56, 62, 71, 72, 98, 120, 145, 146  Genetic analysis  24, 61, 129  Genetic change  123  Genetic code  11, 15, 29, 58, 61, 82, 94, 109, 112, 129, 152, 156,161, 165,173  Genetic engineering  69, 105  Genetic improvement  131  Genetic markers  131  Genetic polymorphism  83  Genetic regulation  3, 7, 13, 15, 16, 21, 29, 31, 34-37, 40, 41,44,46, 51, 52, 54, 55, 59-62, 64, 67, 71, 75, 77, 79, 88, 90, 92,96, 98, 99, 101, 103, 104, 106, 108, 111, 113-115, 118, 120,121, 124, 125, 132, 135, 137, 139, 141, 154, 157, 159, 161, 164,166-168, 172, 173  Genetic transformation  2, 6, 9-11, 14, 16, 18, 35, 41, 45, 51, 53,60,63, 65, 71, 72, 77, 80, 84, 87, 88, 90, 98, 101, 104, 106, 121,131, 134, 135,137, 139, 141, 147, 150, 153, 159, 169, 170  Genetic variation  61, 123, 132, 154  Genetic vectors  169  Genome analysis  138  Genomes  171  Genotypes  8, 132, 154  Germ line  131  Globulins  35, 48  Glomus versiforme  93  Glucose  47  Glufosinate  88  Glutamate-ammonia ligase  23, 77, 106, 113, 120, 172  Glyceraldehyde-3-phosphate dehydrogenase  123  Glycine  78  Glycine max  1, 15-17, 20, 23, 25, 28, 29, 31, 32, 34, 35, 42, 43,47,48, 51, 57, 59, 62-64, 67, 69, 70, 72-74, 76, 77, 80, 83, 86, 90,92,95, 96, 100, 101, 103, 104, 112, 115, 119-121,123, 126, 128, 131, 134, 135, 139, 149-156, 159, 162, 164, 166,167, 172,173  Glycine tomentella  126  Glycoproteins  71, 130, 155, 174  Glycyrrhiza glabra  80  Gossypium barbadense  170  Gossypium hirsutum  33, 81, 99, 145  Greening  114  Growth  8, 102  Growth promoters  40  Guanine  86  Guanosine triphosphate  139  Healing  112  Heat  88  Heat shock  52, 135, 164  Heat shock proteins  16, 52, 135, 165  Heat stress  164  Helianthus annuus  16, 22, 27, 49, 52, 68, 107, 138, 165, 171  Herbicide resistance  88  Hibiscus cannabinus  11  Histidine  43  Histochemistry  14, 120, 154  Histoenzymology  33, 41, 51, 80, 87, 90, 98, 101, 104, 147  Histones  7, 55, 89, 147  Homologous recombination  42  Hordeum vulgare  99  Hybrids  126, 170  Hydro-lyases  108  Hydroxymethylglutaryl-coa reductase  168  Hypocotyls  57, 100, 128  Iaa  57  Imbibition  37  Immunoblotting  53  Immunochemistry  116  Immunocytochemistry  71, 77  Immunohistochemistry  175  In vitro  38, 59  In vitro culture  9  Induced mutations  63, 101  Induced resistance  75, 79  Induction  44, 99, 136  Infection p4, 5  Infections  54  Inheritance  83, 123, 174  Injuries  47, 56, 100  Interspecific hybridization  126  Introgression  174  Introns  6, 25, 27, 45, 144, 145, 149, 153  Inversion  107  Iron p76  Isocitrate dehydrogenase  61, 110  Isoenzymes  61, 115, 164  Isoflavones  93  Isomerases  142  Isopentenyladenosine  135  Jasmonic acid  47, 90, 99, 100, 136, 152  Kinases  129  Laboratory methods  10  Leaves  12, 20, 26, 28, 33, 45, 50, 53, 54, 56, 57, 74, 77, 101,114, 117,119, 127, 128, 145, 151, 152, 157, 159  Lectins  121  Leghemoglobin  23, 76, 104, 132, 146, 150, 163  Legumin  36  Leguminosae  75, 79, 140  Length  62  Lens culinaris  9  Life cycle  67  Ligases  45, 108, 115  Light  120, 96, 102, 120, 96  Line differences  123  Lines  123  Linkage  123  Linkage groups  123p Lipid bodies  68  Lipid metabolism  73, 105  Lipogenesis  98  Lipoxygenase  15, 43, 67, 73, 152, 163, 164  Literature reviews  108, 130, 169  Loci  42, 123, 130, 174  Lolium perenne  175  Lotus corniculatus  104, 120, 150, 153  Lupinus albus  117  Lupinus arboreus  94  Lyases  112  Lycopersicon esculentum  6, 53, 136  Macroptilium atropurpureum  166  Medicago  3, 157  Medicago falcata  21  Medicago littoralis  3  Medicago polymorpha  3, 8  Medicago sativa  7, 12, 13, 18, 19, 39, 40, 45, 46, 53, 55, 66, 78,82, 84,88, 91, 93, 106, 108, 109, 110, 113, 119, 124, 125, 127, 129, 132,136, 142,146, 147, 148, 158, 168  Medicago truncatula  3, 58, 93, 137  Medicago varia  12, 89, 129, 147  Medicarpin  93  Mercuric chloride  54  Meristems  18, 173  Mesophyll  1, 7  Messenger  RNA  1, 4, 5, 7, 12, 13, 17, 19, 20-23, 25-27, 33,34, 37, 39, 42, 46, 47, 50-55, 57, 62, 66, 67, 74, 76-78,81, 85, 92-97, 99, 106, 110, 111, 113-120, 122, 124, 125, 127, 128,136,138, 139, 141-145, 151, 153, 156, 157, 160, 163-165, 167, 172  Metabolic inhibitors  39  Metabolism  161  Metal ions  103  Methionine  2, 64, 162  Mice  103  Microtubules  129  Mitochondria  138, 166  Mitochondrial  DNA  30, 42, 49, 107, 143, 149, 171  Mitochondrial genetics  42, 49, 107, 149, 171  Molecular biology  24, 109  Molecular conformation  25, 48, 68, 171  Molecular genetics  105, 112  Molecular mapping  49, 59, 107  Multigene families  6, 13, 16, 25, 27, 28, 31, 34, 45, 50, 51, 57,59, 85,87, 91, 96, 97, 110, 115, 117, 119, 120, 124, 128, 130, 144, 153,157,167, 172, 175  Multiple genes  42, 77  Mutagenesis  150  Mutants  18, 19, 66, 101, 122  Mutations  6, 43, 121, 122  Naa  7, 57  Nadh  113  Nadh dehydrogenase  30  Nadp  123  Naringenin-chalcone synthase  4, 5, 40, 59, 69, 75, 79, 92, 93,127,157, 168  Nicotiana  101  Nicotiana tabacum  6, 14, 35, 36, 41, 51, 53, 59, 70, 72, 73, 75,77, 79,87, 90, 98, 106, 121, 135, 136, 141, 147, 153, 159  Nitrogen  67  Nitrogen fixation  18, 113, 122, 126, 146  Nitrogenase  76  Nodulation  3, 4, 5, 8, 18, 31, 66, 76, 91, 92, 109, 122, 126, 133,137, 139, 140, 146, 158, 133  Nodules  173  Nodulins  31, 66, 82, 91, 95, 119, 122, 126, 132, 137, 140, 146,153, 163  Nuclei  143, 149  Nucleic acids  58  Nucleotide sequences  1, 6, 12, 13, 16, 19-22, 25, 27-31,33, 36-38, 40, 42, 50, 52, 54, 66, 74, 77, 81, 82, 85, 87, 90, 91,94-98,101, 108-120, 124, 125, 127, 129, 137-139, 142-145,149-153, 157, 158, 160, 161, 171-175  Nucleotides  86  Nutrient availability  67  Nutrient deficiencies  67  Nutrient requirements  64  Ontogeny  29  Organelles  155  Organogenesis  135  Oryza sativa  44  Osmoregulation  114  Osmotic pressure  52, 114  Oxidoreductases  69, 93, 114, 127, 151, 159, 166, 168  Ozone  164  P-coumaric acidp 40  Panicum maximum  65  Pathogenesis-related proteins  127  Pedigree  123  Pennisetum Americanum  65  Pennisetum purpureum  65  Peroxidase  32, 56, 133, 154, 158  Peroxidases  133, 158  Peroxidation  73  Petioles  119  Petunia  64  Ph  3, 132  Phanerochaete chrysosporium  103  Phaseolin  45  Phaseolus vulgaris  40, 45, 54, 59  Phenotypes  24, 61, 131  Phenylalanine ammonia-lyase  4, 5, 92, 93  Phloem  128  Phloem companion cells  1  Phoma medicaginis  157  Phosphoenolpyruvate carboxylase  13, 20, 132  Phosphogluconate dehydrogenase  61  Phosphoproteins  39  Phosphorylation  7, 39  Phosphotransferases  45  Photosynthesis  47  Photosystem ii  145  Phytoalexins  69, 158, 168  Phytochrome  86  Phytophthora cryptogea  75, 79  Phytophthora megasperma  115  Phytophthora nicotianae var. parasitica  75, 79  Pisum sativum  29, 111, 114, 133, 158  Plant  90, 133, 158  Plant anatomy  29, 120, 131, 154, 156  Plant breeding  108  Plant composition  15, 32, 61, 67, 132, 154, 161  Plant development  14, 17, 34, 58, 96, 110, 120, 123, 132, 142, 173 
Plant embryos  22, 35, 37, 46, 52, 60, 73, 79, 97, 99, 101, 119  Plant morphology  14, 120, 131  Plant organs  14  Plant pathogens  32  Plant physiology  17  Plant proteins  1, 2, 12, 21, 22, 25, 26, 28, 39, 41, 42, 46, 51,52, 57,63,68, 72, 79, 87, 96, 98-101, 116, 118, 120, 124, 125, 128,129, 139, 141, 152, 163, 167, 175  Plant tissues  14, 152, 172  Plants  30  Plasma membranes  1  Plasmid vectors  65, 169  Plasmids  3, 84, 133, 143, 158  Pods  111, 152  Pollen  27, 87, 130, 175  Pollen tubes  130  Polymerase chain reaction  174  Precursors  48, 63, 155  Proline  57, 82, 100, 128, 159  Promoters  6, 14, 16, 33, 35, 36, 41, 45, 51, 53, 59, 65, 75, 7980, 87, 90, 98, 101, 104, 120, 121, 135, 141, 147, 150, 153, 167,168,171  Propionic acid  108  Protein composition  132  Protein content  67  Protein kinase  7, 19, 39, 119, 130, 173  Protein synthesis  36, 44, 46, 47, 64, 67, 71, 78, 89, 99, 109,122, 136,155, 161, 165, 166  Protein value  2  Proteinase inhibitors  53  Proteinases D132, 136, 155  Proteins  6, 50, 79, 75, 79, 75  Proteolysis  132  Protoplasts  7, 38, 102, 134  Pseudogenes  42  Pseudomonas syringae pv. pisi  127  Purification  69  Rapeseed oil  105  Raphanus sativus  75, 79  Rats  103  Recessive genes  122  Recombinant  DNA  18, 33, 35, 45, 48, 53, 60, 65, 68, 80, 87, 90,104, 135,141, 147, 162  Regenerative ability  10, 11, 88, 134  Regulation  39, 47, 78, 79, 120, 136, 162  Repetitive  DNA  25, 42, 171  Reporter genes  10, 14, 33, 35, 41, 45, 51, 60, 65, 72, 80, 87, 90,98, 101,104, 141, 147, 162  Respiration  166  Responses  165  Restriction mapping  25, 42, 49, 137  Rhizobium  31, 122, 140, 173  Rhizobium fredii  126  Rhizobium leguminosarum  3, 4, 5, 158, 133, 158, 133  Rhizobium meliloti  3, 8, 18, 66, 82, 109, 113, 137  Rhizobium trifolii  158, 133, 158, 133  Ribosomes  50  Ribulose-bisphosphate carboxylase  34  Rna  24, 162  Rna editing  30, 149  Rna polymerase  162  Root exudates  3  Root hairs  18, 92, 158, 133, 158, 133  Root meristems  60, 153  Root nodules  3, 13, 18, 23, 29, 32, 45, 66, 74, 76, 77, 82, 91,92, 119,95,104, 113, 119, 95, 122, 132, 137, 139, 140, 146, 151, 153, 157,159, 160, 163,166, 172  Roots  4, 5, 7, 12, 18, 20, 28, 29, 32, 34, 45, 51, 56, 57, 60, 77,92, 93,95, 101, 104, 109, 111, 114, 117, 119, 127, 133, 137, 153, 154,157-159,166  Saccharomyces cerevisiae  19, 103, 173  Saccharum officinarum  65  Salinity  26, 114  Sardinia  8  Saturated fatty acids  105  Seed development  2, 46, 79, 94, 98, 161  Seed dormancy  37  Seed germination  15, 79  Seed maturation  155  Seedling growth  62  Seedlings  28, 52, 57, 60, 114, 156, 164  Seeds  2, 20, 22, 35, 36, 37, 41, 45, 48, 52, 64, 72, 83, 97, 98,101, 128,141, 155  Segregation  174  Self compatibility  71  Self incompatibility  71, 130, 174  Senescence  28, 132  Shoot meristems  147  Shoots  10, 135, 166  Sinapis alba  85  Sodium chloride  114  Soil acidity  8  Solanaceae  75, 79  Solanum nigrum  53  Somatic embryogenesis  46, 55  Southern blotting  143  Spatial distribution  71, 95, 119, 156  Squash mosaic comovirus  38  Stability  24  Starch  161  Stems  12, 20, 33, 34, 45, 56, 95, 111, 119, 157  Stigma  130  Strain differences  24  Strains  24  Stress  8, 23, 28, 52, 158  Stress response  44, 56, 78  Structural genes  1, 7, 12, 13, 16, 19-22, 27, 30, 33-35, 41,42, 45, 51-54, 57, 60, 66, 74, 77, 87-89, 91, 92, 94, 106, 107,110, 111, 114, 117, 119, 121, 125, 135, 137, 140, 142, 144, 149,151, 153,157, 160, 164, 167, 168, 171, 174, 175  Structure  83  Sucrose  1, 47, 90, 102  Sucrose synthase  23, 160, 161, 163  Sulfhydryl groups  63  Sulfur  64  Symbiosis  3, 32, 132, 146  Symptoms  24  Synergism  24  Targeted mutagenesis  63  Testas  128, 154  Thioglucosidase  85, 144  Thiolester hydrolases  97  Thiols  155  Tissue culture  11  Tobacco  38  Tolerance  3, 39, 118, 125  Torulopsis glabrata  103  Toxins  86  Transcription  3, 6, 7, 16, 17, 30, 34, 41, 42, 49, 55, 56, 59, 62,79, 82,86, 89, 94, 96, 99, 101, 103, 106-109, 120, 121, 129, 137,138, 143, 149, 162-164, 168, 171  Transduction  148  Transfer  RNA  162, 171  Transferases  4, 5, 108  Transformation  69  Transgenic plants  35, 41, 65, 72, 87, 90, 104, 131, 135, 139, 147,153,169  Transgenics  2, 6, 14, 45, 51, 53, 60, 64, 70, 71, 73, 77, 81, 84,88, 98,101, 106, 120, 121, 134, 137, 141, 159  Translation  6, 78, 106, 164  Transposable elements  25  Trifolium repens  133, 158  Triterpenoid saponins  83  Triticum aestivum  65  Tubulin  117  Ubiquitin  65  Ultraviolet radiation  16, 54  Vacuoles  53  Valine  171  Vesicular arbuscular mycorrhizas  93  Vicia faba  36, 41, 122, 143, 160, 161, 163  Vicia sativa subsp. nigra  4, 5  Vigna aconitifolia  51, 139  Viral antigens  24  Virulence  24  Water deficit  26  Water stress  26, 124, 165  X ray diffraction  48  Xanthomonas campestris pv. alfalfae  127  Xanthomonas campestris pv. armoraciae  75, 79  Xylem  128  Zea mays  6, 16, 65, 175  Zeatin riboside  7  Zinc  27  Zygotes  46                                    BULLET 15
       ELECTRONIC MAIL ACCESS FOR INTERLIBRARY LOAN (ILL) REQUESTS
                                                                  June 1993
The National Agricultural Library (NAL), Document Delivery Services Branchaccepts ILL requests from libraries via several electronic services.  Allrequests must comply with established routing and referral policies andprocedures.  The transmitting library will pay all fees incurred duringthe creation of requests and communication with NAL.  A sample format forILL requests is printed below along with a list of the required data/formatelements.
ELECTRONIC MAIL  -  (Sample form below)     SYSTEM            ADDRESS CODE     ====================================================     INTERNET. . . . . LENDING@NALUSDA.GOV     EASYLINK. . . . . 62031265     ONTYME. . . . . . NAL/LB     TWX/TELEX . . . . Number is 710-828-0506 NAL LEND.                       This number may only be used for                       ILL requests.     FTS2000 . . . . . A12NALLEND      OCLC  . . . . . . NAL's symbol AGL need only be entered                       once, but it must be the last entry in                       the Lender string.  Requests from USDA                       and Federal libraries may contain AGL                       anywhere in the Lender String.
SAMPLE ELECTRONIC MAIL REQUEST| AG University/NAL    ILLRQ 231     4/1/93     NEED BY:  6/1/93 ||                                                                || Interlibrary Loan Department                                   || Agriculture University                                         || Heartland, IA  56789                                           ||                                                                || Dr. Smith   Faculty   Ag School                                ||                                                                || Canadian Journal of Soil Science 1988 v 68(1):  17-27          || DeJong, R.  Comparison of two soil-water models under          || semi-arid growing conditions                                   || Ver:  AGRICOLA                                                 || Remarks:  Not available at IU or in region.                    || NAL CA:  56.8 C162                                             ||                                                                || Auth:  C. Johnson      CCL     Maxcost: $15.00                 ||                                                                || MORE                                                           ||                                                                |
TELEFACSIMILE - Telephone number is 301-504-5675.  NAL accepts ILL requestsvia telefacsimile.  Requests should be created on standard ILL forms andthen faxed to NAL.  NAL does not fill requests via Fax at this time.
REQUIRED DATA ELEMENTS/FORMAT-  Borrower's address must be in block format with at least two blank      lines above and below so form may be used in window envelopes.   Provide complete citation including verification, etc.  
-  Provide authorizing official's name (request will be rejected if      not included).   Include statement of copyright compliance if applicable.  
-  Indicate willingness to pay applicable charges.    Include NAL call number if available.Contact the Document Delivery
     Services Branch at (301) 504-6503 if additional information is     required.

                      NAL DOCUMENT DELIVERY SERVICES 
                                                                  June 1993
United States Department of AgricultureNational Agricultural LibraryPublic Services DivisionDocument Delivery Services BranchBeltsville, Maryland  20705-2351
The National Agricultural Library has established document delivery servicepolicies for three user categories.  They are 1) individuals; 2) libraries, other information centers, and commercial organizations; and 3) foreign libraries, information centers, and commercial organizations.  Availableservices for each user category are given below.  For informationon electronic access for interlibrary loan requests, read Bullet 15.-  DOCUMENT DELIVERY SERVICES TO INDIVIDUALS  The National Agricultural Library (NAL) supplies agriculturalmaterials not found elsewhere to other libraries.
Filling requests for materials readily available from other sourcesdiverts NAL's resources and diminishes its ability to serve as anational source for agricultural and agriculturally relatedmaterials.  Therefore, NAL is viewed as a library of last resort. Submit requests first to local or state library sources prior tosending to NAL.  In the United States, possible sources are publiclibraries, land-grant university or other large research librarieswithin a state.  In other countries submit requests through majoruniversity, national, or provincial institutions.
If the needed publications are not available from these sources,submit requests to NAL with a statement indicating theirnon-availability.  Submit one request per page following theinstructions for libraries below.
NAL'S DOCUMENT DELIVERY SERVICE INFORMATION FOR THE LIBRARY
The following information is provided to assist your librarian inobtaining the required materials.
LOAN SERVICE -- Materials in NAL's collection are loaned only toother U.S. libraries.  Requests for loans are made through localpublic, academic, or special libraries.
The following materials are not available for loan: serials (exceptUSDA serials); rare, reference, and reserve books; microforms; andproceedings of conferences or symposia.  Photocopy or microform ofnon-circulating publications may be purchased as described below.
DOCUMENT DELIVERY SERVICE -- Photocopies of articles are availablefor a fee.  Make requests through local public, academic, orspecial libraries.  The library will submit a separate interlibraryloan form for each article or item requested.  If the citation isfrom an NAL database (CAIN/AGRICOLA, "Bibliography of Agriculture,"or the NAL Catalog) and the call number is given, put that callnumber in the proper block on the request form.  Willingness to paycharges must be indicated on the form.  Include compliance withcopyright law or a statement that the article is for "researchpurposes only" on the interlibrary loan form or letter.  Requestscannot be processed without these statements.
CHARGES:-  Photocopy, hard copy of microfilm and microfiche - $5.00 for      the first 10 pages or fraction copied from a single article or     publication.  $3.00 for each additional 10 pages or fraction.   Duplication of NAL-owned microfilm - $10.00 per reel.  
-  Duplication of NAL-owned microfiche - $ 5.00 for the first      fiche and $ .50 for each additional fiche per title.
BILLING -- Charges include postage and handling, and are subject tochange.  Invoices are issued quarterly by the National TechnicalInformation Service (NTIS), 5285 Port Royal Road, Springfield, VA22161.   Establishing a deposit account with NTIS is encouraged.  DO NOT SEND PREPAYMENT.
SEND REQUESTS TO:           USDA, National Agricultural Library          Document Delivery Services Branch, PhotoLab          10301 Baltimore Blvd., NAL Bldg.          Beltsville, Maryland  20705-2351
Contact the Head, Document Delivery Services Branch in writing orby calling (301) 504-5755 with questions or comments about thispolicy.
2)   DOCUMENT DELIVERY SERVICES AVAILABLE TO LIBRARIES, OTHER
     INFORMATION CENTERS AND COMMERCIAL ORGANIZATIONS.
The National Agricultural Library (NAL) accepts requests fromlibraries and other organizations in accordance with the nationaland international interlibrary loan code and guidelines.  In itsnational role, NAL supplies copies of agricultural materials notfound elsewhere.  Filling requests for materials readily availablefrom other sources diverts NAL's resources and diminishes itsability to serve as a national source for agricultural andagriculturally related materials.  Therefore, NAL is viewed as alibrary of last resort.
Submit requests to state/region/network sources prior to sending toNAL.  Within the United States, possible sources are publiclibraries, land-grant university libraries or other large researchlibraries within a state.  In other countries submit requests tomajor university, national or provincial institutions.  If theneeded publications are not available from these sources, submitrequests to NAL with a statement indicating their non-availability.
REQUESTS -- Submit on the American Library Association (ALA) or theInternational Federation of Library Associations and Institutions(IFLA) interlibrary loan form or via electronic mail ortelefacsimile (see over for more details).  Include the completename of the person authorizing the request on each form; thestandard bibliographic source which lists the title as owned byNAL; and the call number if the citation is from an NAL database(CAIN/AGRICOLA, "Bibliography of Agriculture," or the NAL catalog).
LOAN SERVICE -- Materials in the NAL collection are loaned only toU.S. libraries.  The loan period is one month.
The following materials are not available for loan:  serials(except for USDA serials); rare, reference, and reserve books;microforms; and proceedings of conferences or symposia.  Photocopyor microform of the non-circulating publications is suppliedautomatically (as described below) when the requesting organizationindicates that photocopy is acceptable on the loan form.
AUDIOVISUALS (AVs) -- Order at least 3-4 weeks before the intendedshow date.  Give show date and alternate show date when requestingspecific titles.  Request specific format needed if more than oneformat is given in the citation.
DOCUMENT DELIVERY SERVICE -- Submit a separate completedinterlibrary loan form for each article required.  Indicatewillingness to pay charges on the form and compliance withcopyright law or include a statement that the article is for"research purposes only."  Requests are not processed without thesestatements.
CHARGES:-  Photocopy, hard copy of microfilm and microfiche - $5.00 for      the first 10 pages or fraction copied from a single article or     publication.  $3.00 for each additional 10 pages or fraction.   Duplication of NAL-owned microfilm - $10.00 per reel.  
-  Duplication of NAL-owned microfiche - $5.00 for the first      fiche and $ .50 for each additional fiche per title.
BILLING - Charges include postage and handling, and are subject tochange.  Invoices are issued quarterly by the National TechnicalInformation Service (NTIS), 5285 Port Royal Road, Springfield, VA22161.  Establishing a deposit account with NTIS is encouraged.  DONOT SEND PREPAYMENT.
Send Requests to:     USDA, National Agricultural Library     Document Delivery Services Branch, ILL, PhotoLab     10301 Baltimore Blvd.,  NAL Bldg.     Beltsville, Maryland  20705-2351
Contact the Head, Document Delivery Services Branch in writing orby calling (301) 504-5755 with questions or comments about thispolicy.
3)   DOCUMENT DELIVERY SERVICES AVAILABLE TO FOREIGN LIBRARIES,
     INFORMATION CENTERS AND COMMERCIAL ORGANIZATIONS.
The National Agricultural Library (NAL) accepts requests fromlibraries and other organizations in accordance with the nationaland international interlibrary loan code and guidelines.
In its national role, NAL supplies copies of agricultural materialsnot found elsewhere.  Filling requests for materials readilyavailable from other sources diverts NAL's resources and diminishesits ability to serve as a national source for agricultural andagriculturally related materials.  Therefore, NAL is viewed as alibrary of last resort.
Submit requests to major university libraries, national orprovincial institutions or network sources prior to sendingrequests to NAL.  If the needed publications are not available fromthese sources, submit requests to NAL with a statement indicatingtheir non-availability.
AGLINET -- Requesters in countries with an AGLINET library areencouraged to make full use of that library and its networkingcapabilities.  As an AGLINET participant, NAL provides freedocument delivery service for materials published in the UnitedStates to other AGLINET participants.
REQUESTS -- Submit requests on the American Library Association(ALA) or the International Federation of Library Associations andInstitutions (IFLA) interlibrary loan form or via electronic mailor telefacsimile (see over for more details).  Include the completename of the person authorizing the request on each form; thestandard bibliographic source which lists the title as owned byNAL; and the call number if the  citation is from an NAL database(CAIN/AGRICOLA, "Bibliography of Agriculture", or the NAL catalog).
DOCUMENT DELIVERY SERVICE -- Submit a separate completedinterlibrary loan form for each article requested.  Indicatewillingness to pay charges on the form, and compliance withcopyright law or include a statement that the article is for"research purposes only".  Requests cannot be processed withoutthese statements.
CHARGES:-  Photocopy, hard copy of microfilm and microfiche - $5.00 for      the first 10 pages or fraction copied from a single article or     publication.  $3.00 for each additional 10 pages or fraction.   Duplication of NAL-owned microfilm - $10.00 per reel.  
-  Duplication of NAL-owned microfiche - $5.00 for the first      fiche and $ .50 for each additional fiche per title.
BILLING - Charges include postage and handling, and are subject tochange.  Invoices are issued quarterly by the National TechnicalInformation Service (NTIS), 5285 Port Royal Road, Springfield, VA22161.  Establishing deposit account with NTIS is encouraged. Annual billing is available to foreign institutions on request bycontacting NAL at the address below.  DO NOT SEND PREPAYMENT.
Send Requests to:      USDA, National Agricultural Library     Document Delivery Services Branch, ILL, PhotoLab     10301 Baltimore Blvd., NAL Bldg.     Beltsville, Maryland  20705-2351
Contact the Head, Document Delivery Services Branch at (301)504-5755 with questions or comments about this policy.