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The chloroplastic glutamine synthetase (GS-2) of tobacco is phosphorylated and associated with 14-3-3 proteins inside the chloroplast.
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The chloroplastic isoform of glutamine synthetase (GS-2, EC 6.3.1.2) from Nicotiana tabacum L. is phosphorylated at the serine residues. At least three of the six GS-2 subunits separated by two-dimensional polyacrylamide gel electrophoresis cross-reacted with an antibody raised against
Cis elements and trans-acting factors affecting regulation of a nonphotosynthetic light-regulated gene for chloroplast glutamine synthetase.
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The glutamine synthetase (GS) gene family in pea (Pisum sativum) consists of four nuclear genes encoding distinct isoenzymes. Molecular studies have show that the GS2 gene encoding chloroplast-localized GS is expected in specific cell types and is regulated by diverse factors such as light and
The 3' untranslated region of a soybean cytosolic glutamine synthetase (GS1) affects transcript stability and protein accumulation in transgenic alfalfa.
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Higher plants assimilate nitrogen in the form of ammonia through the concerted activity of glutamine synthetase (GS) and glutamate synthase (GOGAT). The GS enzyme is either located in the cytoplasm (GS1) or in the chloroplast (GS2). Glutamine synthetase 1 is regulated in different plants at the
Nucleotide sequence of a tobacco cDNA encoding plastidic glutamine synthetase and light inducibility, organ specificity and diurnal rhythmicity in the expression of the corresponding genes of tobacco and tomato.
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A full-length cDNA encoding glutamine synthetase (GS) was cloned from a lambda gt10 library of tobacco leaf RNA, and the nucleotide sequence was determined. An open reading frame accounting for a primary translation product consisting of 432 amino acids has been localized on the cDNA. The calculated
Glutamine and alpha-ketoglutarate are metabolite signals involved in nitrate reductase gene transcription in untransformed and transformed tobacco plants deficient in ferredoxin-glutamine-alpha-ketoglutarate aminotransferase.
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Transformed tobacco (Nicotiana tabacum L.) plants with varying activities of the key enzyme of ammonia assimilation, ferredoxin-glutamine-alpha-ketoglutarate aminotransferase (Fd-GOGAT; EC 1.4.7.1), were used to examine the roles of ammonium, glutamine (Gln) and alpha-ketoglutarate (alpha-KG) in the
Overproduction of alfalfa glutamine synthetase in transgenic tobacco plants.
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We have obtained transgenic tobacco plants overexpressing the enzyme glutamine synthetase (GS) by fusing an alfalfa GS gene to the cauliflower mosaic virus 35S promotor and integrating it into Nicotiana tabacum var. W38 plants by Agrobacterium tumefaciens mediated gene transfer. The amount of RNA
Targeting of glutamine synthetase to the mitochondria of transgenic tobacco.
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Two transgenic tobacco lines were genetically engineered to contain chimaeric genes encoding the glutamine synthetase (GS) gamma polypeptide of Phaseolus vulgaris (French bean), expressed from the cauliflower mosaic virus 35S promoter. One (MIT-1) contained two copies of a construct including the
Immunochemical comparison of glutamine synthetases from some solanaceae plants.
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The presence of different glutamine synthetase isoenzymes in different Solanaceae plants and their relative antigenicities against antiglutamine synthetase from tomato leaf serum were studied. All the plants tested showed one glutamine synthetase isoenzyme except for Mandragora autumnalis, which
Detection of a Cytosolic Glutamine Synthetase in Leaves of Nicotiana tabacum L. by Immunocytochemical Methods.
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Two glutamine synthetase (GS) polypeptides (44 and 39 kD) were immunodetected on western blots of leaf extracts from tobacco (Nicotiana tabacum L.), a plant that has been reported to contain only chloroplast GS in the leaves. By immunocytochemical methods, we confirmed the localization of GS in the
Glutamine Synthetase of Nicotiana plumbaginifolia: Cloning and in Vivo Expression.
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We have characterized the distinct forms of glutamine synthetase (GS) which are present in leaves and roots of Nicotiana plumbaginifolia. Mature leaves contain a single GS polypeptide (44 kilodaltons in size) which is localized to the stroma of intact chloroplasts. In contrast, the GS polypeptide in
Glutamine synthetase activity in Solanaceous cell suspensions accumulating alkaloids or not. 13C NMR and enzymatic assay.
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The metabolism of labelled pyruvate followed by 13C NMR and the measure of glutamine synthetase (GS) showed, according to previous results, a high activity of this enzyme in suspension cells of Nicotiana plumbaginifolia. This activity could derive glutamate from the alkaloid synthesizing pathways.
Negative regulation of nitrate reductase gene expression by glutamine or asparagine accumulating in leaves of sulfur-deprived tobacco.
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Tobacco (Nicotiana tabacum L.) plants were subjected to a prolonged period of sulfur-deprivation to characterize molecular and metabolic mechanisms that permit control of primary N-metabolism under these conditions. Prior to the appearance of chlorotic lesions, sulfur-deprived tobacco leaves showed
Photorespiration-dependent increases in phospho enolpyruvate carboxylase, isocitrate dehydrogenase and glutamate dehydrogenase in transformed tobacco plants deficient in ferredoxin-dependent glutamine-alpha-ketoglutarate aminotransferase.
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The metabolic cross-talk associated with re-assimilation of photorespiratory NH4+ was analysed in transformed tobacco (Nicotiana tabacum L.) plants with low activities of ferredoxin-dependent glutamine-alpha-ketoglutarate aminotransferase (Fd-GOGAT; EC 1.4.7.1). Amounts of ribulose-1,5-bisphosphate
Glutamine synthetase in the phloem plays a major role in controlling proline production
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To inhibit expression specifically in the phloem, a 274-bp fragment of a cDNA (Gln1-5) encoding cytosolic glutamine synthetase (GS1) from tobacco was placed in the antisense orientation downstream of the cytosolic Cu/Zn superoxide dismutase promoter of Nicotiana plumbaginifolia. After
Overexpression of cytosolic glutamine synthetase. Relation to nitrogen, light, and photorespiration.
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In plants, ammonium released during photorespiration exceeds primary nitrogen assimilation by as much as 10-fold. Analysis of photorespiratory mutants indicates that photorespiratory ammonium released in mitochondria is reassimilated in the chloroplast by a chloroplastic isoenzyme of glutamine
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