bluuebunny/crossref_metadata_2025_split huggingface dataset:
Does nutrition-related stress carry over to spruce budworm,Choristoneura fumiferana(Lepidoptera: Tortricidae) progeny?
Authors: Carisey N. , Bauce É. 
Published: July 2002

AbstractThree different patterns of feeding of sixth-instar spruce budworm,Choristoneura fumiferanaClemens were simulated in the laboratory. Larvae were fed artificial diets whose nitrogen and total soluble sugar contents varied according to levels similar to those found in three types of balsam fir,Abies balsamea(L.) Miller foliage (current-year foliage from middle and lower crown sections and one-year-old foliage). The biological performance of offspring was studied according to the nutrition of their parents. Although food quality had no impact on pupal weight of female parents and individual mean egg weight, progeny fitness was influenced by parental nutrition. Old foliage simulated diet, poor in nitrogen, clearly affected the early larval development of progeny, especially the percent of egg hatch and first-instar survival. Lower crown current-year foliage simulated diet, with low total soluble sugar content, reduced the first-instar survival of the progeny. However, the selective pressure exerted by low food qualities on the parental generation and on the early stages of their progenies resulted inC. fumiferanapopulations having higher tolerance to starvation and higher survival after the diapause period. These results highlighted the potentially direct and indirect effects ofC. fumiferanaparental nutrition on the next generation. The patterns of feeding of parental generations would appear to affect the quality and size of subsequent populations through several selections on the different life-history stages of both generations.
Ascorbate Deficiency Can Limit Violaxanthin De-Epoxidase Activity in Vivo
Authors: Müller-Moulé Patricia , Conklin Patricia L. , Niyogi Krishna K. 
Published: July 2002

Abstract
As a response to high light, plants have evolved non-photochemical quenching (NPQ), mechanisms that lead to the dissipation of excess absorbed light energy as heat, thereby minimizing the formation of dangerous oxygen radicals. One component of NPQ is pH dependent and involves the formation of zeaxanthin from violaxanthin. The enzyme responsible for the conversion of violaxanthin to zeaxanthin is violaxanthin de-epoxidase, which is located in the thylakoid lumen, is activated by low pH, and has been shown to use ascorbate (vitamin C) as its reductant in vitro. To investigate the effect of low ascorbate levels on NPQ in vivo, we measured the induction of NPQ in a vitamin C-deficient mutant of Arabidopsis, vtc2-2. During exposure to high light (1,500 μmol photons m−2s−1), vtc2-2 plants initially grown in low light (150 μmol photons m−2 s−1) showed lower NPQ than the wild type, but the same quantum efficiency of photosystem II. Crosses between vtc2-2 and Arabidopsis ecotype Columbia established that the ascorbate deficiency cosegregated with the NPQ phenotype. The conversion of violaxanthin to zeaxanthin induced by high light was slower in vtc2-2, and this conversion showed saturation below the wild-type level. Both the NPQ and the pigment phenotype of the mutant could be rescued by feeding ascorbate to leaves, establishing a direct link between ascorbate, zeaxanthin, and NPQ. These experiments suggest that ascorbate availability can limit violaxanthin de-epoxidase activity in vivo, leading to a lower NPQ. The results also demonstrate the interconnectedness of NPQ and antioxidants, both important protection mechanisms in plants.
Abscisic Acid Induces the Alcohol Dehydrogenase Gene in Arabidopsis
Authors: de Bruxelles G. L. , Peacock W. J. , Dennis E. S. , Dolferus R. 
Published: July 2002

Abstract
Exogenous abscisic acid (ABA) induced the alcohol dehydrogenase gene (Adh) in Arabidopsis roots. Both the G-box-1 element and the GT/GC motifs (anaerobic response element) were required for Adh inducibility. Measurement of endogenous ABA levels during stress treatment showed that ABA levels increased during dehydration treatment but not following exposure to either hypoxia or low temperature. Arabidopsis ABA mutants (aba1 and abi2) displayed reduced Adh mRNA induction levels following either dehydration treatment or exogenous application of ABA. Low-oxygen response was slightly increased in the aba1 mutant but was unchanged in abi2. Low-temperature response was unaffected in both aba1 and abi2 mutants. Our results indicate that, although induction of the Adh gene by ABA, dehydration, and low temperature required the same cis-acting promoter elements, their regulatory pathways were at least partially separated in a combined dehydration/ABA pathway and an ABA-independent low-temperature pathway. These pathways were in turn independent of a third signal transduction pathway leading to low-oxygen response, which did not involve either ABA or the G-box-1 promoter element.
Degradation Pattern of Photosystem II Reaction Center Protein D1 in Intact Leaves (The Major Photoinhibition-Induced Cleavage Site in D1 Polypeptide Is Located Amino Terminally of the DE Loop)
Authors: Kettunen R. , Tyystjarvi E. , Aro E. M. 
Published: July 2002

Abstract
Photoinhibition-induced degradation of the D1 protein of the photosystem II reaction center was studied in intact pumpkin (Cucurbita pepo L.) leaves. Photoinhibition was observed to cause the cleavage of the D1 protein at two distinct sites. The main cleavage generated an 18-kD N-terminal and a 20-kD C-terminal degradation fragment of the D1 protein. This cleavage site was mapped to be located clearly N terminally of the DE loop. The other, less-frequent cleavage occurred at the DE loop and produced the well-documented 23-kD, N-terminal D1 degradation product. Furthermore, the 23-kD, N-terminal D1 fragment appears to be phosphorylated and can be detected only under severe photoinhibition in vivo. Comparison of the D1 degradation pattern after in vivo photoinhibition to that after in vitro acceptor-side and donor-side photoinhibition, performed with isolated photosystem II core particles, gives indirect evidence in support of donor-side photoinhibition in intact leaves.
Two Divergent Members of a Tobacco 4-Coumarate:Coenzyme A Ligase (4CL) Gene Family (cDNA Structure, Gene Inheritance and Expression, and Properties of Recombinant Proteins)
Authors: Lee D. , Douglas C. J. 
Published: July 2002

Abstract
Several cDNA clones encoding 4-coumarate:coenzyme A ligase (4CL) were isolated from a tobacco (Nicotiana tabacum) cDNA library and grouped into two classes. Sequencing of one cDNA from each class showed that the clones were similar to other 4CL genes and about 80% identical with each other. Genomic Southern blots using DNA from Nicotiana sylvestris, Nicotiana tomentosiformis, and N. tabacum demonstrated the presence of both classes of 4CL sequences (4CL1 and 4CL2) in the progenitor species and in tobacco. Northern blots indicated that 4CL mRNA transcripts are highest in old stems and higher in the unpigmented corolla tubes than in the pigmented limbs of tobacco flowers. The 4CL genes are developmentally regulated and are wound and methyl jasmonate inducible. The relative abilities of recombinant 4CL1 and 4CL2 proteins to utilize 4-coumarate, ferulate, and caffeate as substrates were similar and comparable with that of 4CL in tobacco stem extracts. Surprisingly, both recombinant 4CL proteins utilized cinnamate as a substrate, an activity not observed in stem extracts. This activity was inhibited by a heat-labile, high-molecular-weight factor found in tobacco stem extracts, suggesting that the substrate specificity of 4CL is, in part, determined by the activity of proteinaceous cellular components.
Synthesis of Small Heat-Shock Proteins Is Part of the Developmental Program of Late Seed Maturation
Authors: Wehmeyer N. , Hernandez L. D. , Finkelstein R. R. , Vierling E. 
Published: July 2002

Abstract
Small heat-shock proteins (sHSPs) accumulate in plants in response to high-temperature stress. Specific sHSPs, the cytosolic class I and class II proteins, are also expressed in the absence of stress in maturing seeds of several species, and a role for these proteins in desiccation tolerance, dormancy, or germination has been hypothesized. We demonstrate that class I sHSPs are expressed during Arabidopsis seed development in a pattern similar to that previously observed in other species: they are first detected during mid-maturation, are most abundant in dry seeds, and decline rapidly during germination. Although the class I sHSP family in Arabidopsis appears to consist of four genes, expression of a single gene, Athsp17.4, accounts for the majority of sHSPs in maturing seeds. sHSP levels were also examined in seeds of several Arabidopsis mutants with reduced sensitivity to abscisic acid inhibition, including aba1, abi1 and abi2, abi3–1, abi3–6, abi4, and abi5–1. The abi3–1 mutant has 10-fold reduced levels of sHSPs; sHSPs are undetectable in the abi3–6 mutant. All other mutants were indistinguishable from wild type. These results suggest that sHSP expression in seeds is regulated by the ABI3 response pathway and wild-type levels of sHSPs are not sufficient for seed dormancy and not necessary for desiccation tolerance. However, roles in either process cannot be ruled out. In total the data indicate that the expression of sHSPs in seeds is part of the normal developmental program of late seed maturation and the presence of sHSPs has adaptive significance for plant reproduction.
De Novo Purine Synthesis in Arabidopsis thaliana (II. The PUR7 Gene Encoding 5[prime]-Phosphoribosyl-4-(N-Succinocarboxamide)-5-Aminoimidazole Synthetase Is Expressed in Rapidly Dividing Tissues)
Authors: Senecoff J. F. , McKinney E. C. , Meagher R. B. 
Published: July 2002

Abstract
The small genome size and excellent genetics of Arabidopsis, as well as the ease with which it is transformed, make it a superb candidate for molecular genetic studies of the purine biosynthetic pathway. Herein we report the isolation, physical characterization, and dissection of the expression patterns of the single gene encoding 5[prime]-phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole synthetase. This enzyme, encoded by the PUR7 gene, catalyzes aspartate addition at the α--amino group to the growing purine backbone. The expression of the PUR7 as directed by the 5[prime] region, containing the promoter, mRNA leader, and leader intron, was examined in Arabidopsis using a transgenic reporter system. Our analysis demonstrates that the highest level of purine biosynthesis occurs in mitotically active tissues of the plant. Furthermore, purine biosynthesis appears to be under developmental and hormonal regulation. Inhibition of purine biosynthesis using substrate analogs results in arrested plant development and induction of purine gene expression. Purine nucleotides and their derivatives provide multiple cofactors for a variety of metabolic processes. Our findings begin to identify some of the regulatory mechanisms that affect the production of purine nucleotides in Arabidopsis and may give important insights into nitrogen metabolism in general.
Pyrophosphorylases in Potato (V. Allelic Polymorphism of UDP-Glucose Pyrophosphorylase in Potato Cultivars and Its Association with Tuber Resistance to Sweetening in the Cold)
Authors: Sowokinos J. R. , Thomas C. , Burrell M. M. 
Published: July 2002

Abstract
UDP-glucose pyrophosphorylase (UGPase) was cloned from six American and nine European potato (Solanum tuberosum L.) cultivars. Restriction mapping of the different UGPase-cDNAs with BamHI, HindIII, and EcoRI revealed that at least two mRNA populations were present in most cultivars. Staining for UGPase activity in nondenaturing gels of proteins extracted from developing potato tubers yielded two major isozymes that were highly active and appeared to be dimeric in nature. Following sodium dodecyl sulfate-polyacrylamide gel electrophoresis, all isozymes were disassociated into a single subunit with a molecular mass of 53 kD. Since UGPase has been demonstrated to be a single-copy gene in the haploid genome of potato (A.Y. Borovkov, P.E. McClean, J.R. Sowokinos, S.H. Ruud, G.A. Secor [1995] J Plant Physiol 147: 644–652), there must be allelic differences at the UGPase locus (chromosome 11). The two alleles, designated ugpA and ugpB, were identified by the absence and presence of a BamHI site, respectively. The relative band intensities of the two cDNA populations following polymerase chain reaction amplification and agarose gel electrophoresis were related to a potato cultivar's ability to resist sweetening when exposed to cold temperatures.
Characterization of AtSEC12 and AtSAR1 (Proteins Likely Involved in Endoplasmic Reticulum and Golgi Transport)
Authors: Bar-Peled M. , Raikhel N. V. 
Published: July 2002

Abstract
Transport of cargo proteins from the endoplasmic reticulum (ER) to the cis-Golgi network is mediated by protein-coated vesicles. The coat, called COPII coat, consists of proteins that are recruited from the cytosol and interact with integral membrane proteins of the ER. In yeast, both cytosolic proteins (Sec13/31, Sec23/24, and Sar1) and ER-associated proteins (Sec12 and others) have been purified and characterized and it has been possible to demonstrate transport vesicle formation in vitro. Arabidopsis thaliana homologs of Sar1 and Sec12 have recently been identified, but little is known about the properties of the proteins or their subcellular distribution. Here we demonstrate that AtSAR1, a 22-kD protein that binds GTP, and AtSEC12, a 43-kD GTP-exchange protein, are both associated with the ER. However, about one-half of the cellular AtSAR1 is present in the cytosol. When AtSAR1 is overexpressed in transgenic plants, the additional protein is also cytosolic. When tissue-culture cells are cold-shocked (12 h at 8[deg]C), AtSAR1 levels appeared to decline and a larger proportion of the total protein was found in the cytosol. Given the known function of AtSAR1 in yeast, we propose that the amount of ER-associated AtSAR1 is an indication of the intensity of the secretory process. Thus, we expect that such a cold shock will adversely affect ER-to-Golgi transport of proteins.
Broad-Range and Binary-Range Acyl-Acyl-Carrier-Protein Thioesterases Suggest an Alternative Mechanism for Medium-Chain Production in Seeds
Authors: Voelker T. A. , Jones A. , Cranmer A. M. , Davies H. M. , Knutzon D. S. 
Published: July 2002

Abstract
In the current model of medium-chain (C8–14) fatty acid biosynthesis in seeds, specialized FatB acyl-acyl-carrier-protein (ACP) thioesterases are responsible for the production of medium chains. We have isolated and characterized FatB cDNAs from the maturing seeds of elm (Ulmus americana) and nutmeg (Myristica fragrans), which accumulate predominantly caprate (10:0)- and myristate (14:0)-containing oils, respectively. In neither species were we able to find cDNAs encoding enzymes specialized for these chain lengths. Nutmeg FatB hydrolyses C14–18 substrates in vitro and expression in Brassica napus seeds leads to an oil enriched in C14–18 saturates. Elm FatB1 displays a binary specificity: one activity is centered on 10:0-ACP, and a second is centered on palmitate (16:0)-ACP. After expression in B. napus seeds the oil is enriched in C10–18 saturates, predominantly 16:0, 14:0, and 10:0. The composition of free fatty acids produced by elm FatB1 in Escherichia coli shifts from C14–16 to mostly C8–10 by increasing the rate of chain termination by this enzyme. These results suggest the existence of an alternative mechanism used in the evolution of medium-chain production, a model of which is presented.
Defense Responses to Tetrapyrrole-Induced Oxidative Stress in Transgenic Plants with Reduced Uroporphyrinogen Decarboxylase or Coproporphyrinogen Oxidase Activity1
Authors: Mock Hans-Peter , Keetman Ulrich , Kruse Elisabeth , Rank Barbara , Grimm Bernhard 
Published: July 2002

Abstract
We analyzed the antioxidative defense responses of transgenic tobacco (Nicotiana tabacum) plants expressing antisense RNA for uroporphyrinogen decarboxylase or coproporphyrinogen oxidase. These plants are characterized by necrotic leaf lesions resulting from the accumulation of potentially photosensitizing tetrapyrroles. Compared with control plants, the transformants had increased levels of antioxidant mRNAs, particularly those encoding superoxide dismutase (SOD), catalase, and glutathione peroxidase. These elevated transcript levels correlated with increased activities of cytosolic Cu/Zn-SOD and mitochondrial Mn-SOD. Total catalase activity decreased in the older leaves of the transformants to levels lower than in the wild-type plants, reflecting an enhanced turnover of this photosensitive enzyme. Most of the enzymes of the Halliwell-Asada pathway displayed increased activities in transgenic plants. Despite the elevated enzyme activities, the limited capacity of the antioxidative system was apparent from decreased levels of ascorbate and glutathione, as well as from necrotic leaf lesions and growth retardation. Our data demonstrate the induction of the enzymatic detoxifying defense system in several compartments, suggesting a photosensitization of the entire cell. It is proposed that the tetrapyrroles that initially accumulate in the plastids leak out into other cellular compartments, thereby necessitating the local detoxification of reactive oxygen species.
Aluminum Induces a Decrease in Cytosolic Calcium Concentration in BY-2 Tobacco Cell Cultures1
Authors: Jones David L. , Kochian Leon V. , Gilroy Simon 
Published: July 2002

Abstract
Al toxicity is a major problem that limits crop productivity on acid soils. It has been suggested that Al toxicity is linked to changes in cellular Ca homeostasis and the blockage of plasma membrane Ca2+-permeable channels. BY-2 suspension-cultured cells of tobacco (Nicotiana tabacumL.) exhibit rapid cell expansion that is sensitive to Al. Therefore, the effect of Al on changes in cytoplasmic free Ca concentration ([Ca2+]cyt) was followed in BY-2 cells to assess whether Al perturbed cellular Ca homeostasis. Al exposure resulted in a prolonged reduction in [Ca2+]cyt and inhibition of growth that was similar to the effect of the Ca2+ channel blocker La3+ and the Ca2+ chelator ethyleneglycol-bis(β-aminoethyl ether)-N,N′-tetraacetic acid. The Ca2+channel blockers verapamil and nifedipine did not induce a decrease in [Ca2+]cyt in these cells and also failed to inhibit growth. Al and La3+, but not verapamil or nifedipine, reduced the rate of Mn2+ quenching of Indo-1 fluorescence, which is consistent with the blockage of Ca2+- and Mn2+-permeable channels. These results suggest that Al may act to block Ca2+ channels at the plasma membrane of plant cells and this action may play a crucial role in the phytotoxic activity of the Al ion.
Actin Depolymerization Affects Stress-Induced Translational Activity of Potato Tuber Tissue1
Authors: Morelli James K. , Zhou Wei , Yu Jia , Lu Chen , Vayda Michael E. 
Published: July 2002

Abstract
Changes in polymerized actin during stress conditions were correlated with potato (Solanum tuberosum L.) tuber protein synthesis. Fluorescence microscopy and immunoblot analyses indicated that filamentous actin was nearly undetectable in mature, quiescent aerobic tubers. Mechanical wounding of postharvest tubers resulted in a localized increase of polymerized actin, and microfilament bundles were visible in cells of the wounded periderm within 12 h after wounding. During this same period translational activity increased 8-fold. By contrast, low-oxygen stress caused rapid reduction of polymerized actin coincident with acute inhibition of protein synthesis. Treatment of aerobic tubers with cytochalasin D, an agent that disrupts actin filaments, reduced wound-induced protein synthesis in vivo. This effect was not observed when colchicine, an agent that depolymerizes microtubules, was used. Neither of these drugs had a significant effect in vitro on run-off translation of isolated polysomes. However, cytochalasin D did reduce translational competence in vitro of a crude cellular fraction containing both polysomes and cytoskeletal elements. These results demonstrate the dependence of wound-induced protein synthesis on the integrity of microfilaments and suggest that the dynamics of the actin cytoskeleton may affect translational activity during stress conditions.
Phytochrome B Affects the Levels of a Graft-Transmissible Signal Involved in Tuberization1
Authors: Jackson Stephen D. , James Pat , Prat Salomé , Thomas Brian 
Published: July 2002

Abstract
Grafting experiments between phytochrome B antisense and wild-type potato (Solanum tuberosum L. subsp. andigena [line 7540]) plants provide evidence that phytochrome B is involved in the production of a graft-transmissible inhibitor of tuberization, the level of which is reduced in the antisense plants, allowing them to tuberize in noninducing photoperiods.
Correlation between Binding Affinity and Necrosis-Inducing Activity of Mutant AVR9 Peptide Elicitors1
Authors: Kooman-Gersmann Miriam , Vogelsang Ralph , Vossen Paul , van den Hooven Henno W. , Mahé Eve , Honée Guy , de Wit Pierre J.G.M. 
Published: July 2002

AbstractThe race-specific peptide elicitor AVR9 of the fungus Cladosporium fulvum induces a hypersensitive response only in tomato (Lycopersicon esculentum) plants carrying the complementary resistance gene Cf-9 (MoneyMaker-Cf9). A binding site for AVR9 is present on the plasma membranes of both resistant and susceptible tomato genotypes. We used mutant AVR9 peptides to determine the relationship between elicitor activity of these peptides and their affinity to the binding site in the membranes of tomato. Mutant AVR9 peptides were purified from tobacco (Nicotiana clevelandii) inoculated with recombinant potato virus X expressing the corresponding avirulence geneAvr9. In addition, several AVR9 peptides were synthesized chemically. Physicochemical techniques revealed that the peptides were correctly folded. Most mutant AVR9 peptides purified from potato virus X::Avr9-infected tobacco contain a single N-acetylglucosamine. These glycosylated AVR9 peptides showed a lower affinity to the binding site than the nonglycosylated AVR9 peptides, whereas their necrosis-inducing activity was hardly changed. For both the nonglycosylated and the glycosylated mutant AVR9 peptides, a positive correlation between their affinity to the membrane-localized binding site and their necrosis-inducing activity in MoneyMaker-Cf9 tomato was found. The perception of AVR9 in resistant and susceptible plants is discussed.
Expression of Small Heat-Shock Proteins at Low Temperatures1
Authors: Sabehat Adnan , Lurie Susan , Weiss David 
Published: July 2002

Abstract
We previously reported that short exposure of tomato (Lycopersicon esculentum L.) fruits to high temperature protects them from chilling injury. To study the involvement of heat-shock proteins (HSPs) in the acquisition of low-temperature tolerance, we cloned two heat-shock-induced genes that are also expressed at low temperatures. The cloned cDNAs belong to the small HSP group. Sequence analyses of the clones showed perfect homology to the tomato-ripening gene tom66 and to the tomato chloroplastic HSP21 gene tom111. The expression of both genes was induced by high temperature in fruits, flowers, leaves, and stems, but not by low or ambient temperatures or by other stresses such as drought and anaerobic conditions. When the heated fruits were transferred to low temperature, tom66and tom111 mRNA levels first decreased but were then reinduced. Induction was not observed in nonheated fruits at low temperature. Immunodetection of tom111-encoded protein indicated that this protein is present at low temperatures in the heated fruits. The results of this study show that the expression oftom66 and tom111 is correlated with protection against some, but not all, symptoms of chilling injury.