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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Synechocystis sp. PCC 6803 glutamine synthetase type I (GS) activity is controlled by direct interaction with two inactivating factors (IF7 and IF17). IF7 and IF17 are homologous polypeptides encoded by the gifA and gifB genes respectively. We investigated the transcriptional regulation of these genes. Expression of both genes is maximum in the presence of ammonium, when GS is inactivated. Nitrogen starvation attenuates the ammonium-mediated induction of gifA and gifB as well as the ammonium-mediated inactivation of GS. Putative binding sites for the transcription factor NtcA were identified at -7.5 and -30.5 bp upstream of gifB and gifA transcription start points respectively. Synechocystis NtcA protein binding to both promoters was demonstrated by gel electrophoresis mobility shift assays. Constitutive high expression levels of both genes were found in a Synechocystis NtcA non-segregated mutant (SNC1), which showed a fourfold reduction in the ntcA expression. These experiments indicate a repressive role for NtcA on the transcription of gifA and gifB genes. Our results demonstrate that NtcA plays a central role in GS regulation in cyanobacteria, stimulating transcription of the glnA gene (GS structural gene) and suppressing transcription of the GS inactivating factor genes gifA and gifB.
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PMID:NtcA represses transcription of gifA and gifB, genes that encode inhibitors of glutamine synthetase type I from Synechocystis sp. PCC 6803. 1071 99

The liver shows net glutamine uptake after a protein-containing meal, during uncontrolled diabetes, sepsis and short-term starvation, but changes to net release during long-term starvation and metabolic acidosis. Some studies report a small net release of glutamate by the liver. The differential expression of glutamine synthetase (perivenous) and glutaminase (periportal) within the liver indicates that glutamine is used for urea synthesis in periportal cells, whereas glutamine synthesis serves to detoxify any residual ammonia in perivenous cells. Experiments in vivo suggest that changes in net hepatic glutamine balance are due predominantly to regulation of glutaminase activity, with the flux through glutamine synthetase being relatively constant.
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PMID:Glutamine and glutamate metabolism across the liver sinusoid. 1073 66

High light stress (40 W/m(2))-induced alterations in the nitrogen assimilatory enzymes in Spirulina platensis were studied under the Ca(2+) and phosphate (Pi)-supplemented as well as starved conditions. Results revealed that activities of nitrate reductase (NR), amino acid transferases (AST/GOT and ALT/GPT), and protease enzymes in the high-light-incubated cells were relatively higher under the Ca(2+)- and Pi-starved conditions. On the contrary, relative rates of glutamine synthetase (GS) and ATPase activities were lower in the Ca(2+)- and Pi-starved cells. But the Spirulina cells under the Ca(2+)- and Pi-added conditions showed enhanced activity of both GS and ATPase enzymes. During the high-light stress, a decline in the GS activity, particularly under the Ca(2+)- and Pi-starved conditions, was indicative of a nitrogen starvation-like condition. This could be one of the reasons for induction of the NR and protease enzymes. A higher rate of GS activity was recorded under both the Ca(2+)- and Pi-supplemented conditions, perhaps owing to the enhanced rate of ATPase activity in such conditions. But a declining pattern of both NR and protease activities in the presence of Ca(2+) and Pi, despite the higher rate of ATPase activity, might involve some other mechanism like the protein-kinase system.
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PMID:Calcium and phosphate regulation of nitrogen metabolism in the cyanobacterium Spirulina platensis under the high light stress. 1101 76

The metabolism of glutamine, the main respiratory fuel of enterocytes, is governed by the activity of glutaminase and glutamine synthetase. Because starvation induces intestinal atrophy, it might alter the rate of intestinal glutamine utilization. This study examined the effect of starvation on the activity, level of mRNA, and distribution of mRNA of glutaminase and glutamine synthetase in the rat intestine. Rats were randomized into groups and were either: (1) fed for 2 days with rat food ad libitum or (2) starved for 2 days. Standardized segments of jejunum and ileum were removed for the estimation of enzyme activity, level of mRNA, and in situ hybridization analysis. The jejunum of the fed rats had a greater activity of both enzymes per centimeter of intestine (P < 0.01), a greater glutaminase specific activity (1.97 +/- 0.45 vs. 1.09 +/- 0.34 micromol/hr/mg protein, P < 0.01), and a lower level of glutaminase and glutamine synthetase mRNA. The ileum of the fed rats had a greater activity of glutamine synthetase per centimeter of intestine (162.9 +/- 50.6 vs. 91.0 +/- 23.1 nmol/hr/cm bowel, P < 0.01), a lower level of glutaminase mRNA, and a greater level of glutamine synthetase mRNA. In situ hybridization analysis showed that starvation does not alter the distribution of glutaminase and glutamine synthetase mRNA in the intestinal mucosa. This study confirms that starvation decreases the total intestinal activity per centimeter of both glutaminase and glutamine synthetase. More importantly, the results indicate that the intestine adapts to starvation by accumulating glutaminase mRNA. This process prepares the intestine for a restoration of intake.
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PMID:Starvation alters the activity and mRNA level of glutaminase and glutamine synthetase in the rat intestine. 1104 34

The expression of sll1689, an open reading frame from the cyanobacterium Synechocystis sp. strain PCC 6803 putatively encoding a member of the sigma(70) family of sigma factors, appears to be regulated by the nitrogen control transcription factor NtcA. Disruption of sll1689 had no noticeable effect on exponential growth, identifying its product as a member of the group 2, nonessential class of sigma(70)-like sigma factors; however, this disruption decreased the viability of the cells after long periods of nitrogen starvation. We have named this gene rpoD2-V. The expression of glnN, encoding a type III glutamine synthetase, was impaired in strains bearing an inactivated copy of the rpoD2-V gene.
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PMID:Nitrogen-regulated group 2 sigma factor from Synechocystis sp. strain PCC 6803 involved in survival under nitrogen stress. 1120 9

The physiological regulation of glutamine synthetase (GS; EC 6.3.1.2) in the axenic Prochlorococcus sp. strain PCC 9511 was studied. GS activity and antigen concentration were measured using the transferase and biosynthetic assays and the electroimmunoassay, respectively. GS activity decreased when cells were subjected to nitrogen starvation or cultured with oxidized nitrogen sources, which proved to be nonusable for Prochlorococcus growth. The GS activity in cultures subjected to long-term phosphorus starvation was lower than that in equivalent nitrogen-starved cultures. Azaserine, an inhibitor of glutamate synthase, provoked an increase in enzymatic activity, suggesting that glutamine is not involved in GS regulation. Darkness did not affect GS activity significantly, while the addition of diuron provoked GS inactivation. GS protein determination showed that azaserine induces an increase in the concentration of the enzyme. The unusual responses to darkness and nitrogen starvation could reflect adaptation mechanisms of Prochlorococcus for coping with a light- and nutrient-limited environment.
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PMID:In vivo regulation of glutamine synthetase activity in the marine chlorophyll b-containing cyanobacterium Prochlorococcus sp. strain PCC 9511 (oxyphotobacteria). 1131 1

Nitrogen, which is a major limiting nutrient for plant growth, is assimilated as ammonium by the concerted action of glutamine synthetase (GS) and glutamate synthase (GOGAT). GS catalyses the critical incorporation of inorganic ammonium into the amino acid glutamine. Two types of GS isozymes, located in the cytosol (GS1) and in the chloroplast (GS2) have been identified in plants. Tobacco (Nicotiana tabacum) transformants, over-expressing GS1 driven by the constitutive CaMV 35S promoter were analysed. GS in leaves of GS-5 and GS-8 plants was up-regulated, at the level of RNA and proteins. These transgenic plants had six times higher leaf GS activity than controls. Under optimum nitrogen fertilization conditions there was no effect of GS over-expression on photosynthesis or growth. However, under nitrogen starvation the GS transgenics had c. 70% higher shoot and c. 100% greater root dry weight as well as 50% more leaf area than low nitrogen controls. This was achieved by the maintenance of photosynthesis at rates indistinguishable from plants under high nitrogen, while photosynthesis in control plants was inhibited by 40-50% by nitrogen deprivation. It was demonstrated that manipulation of GS activity has the potential to maintain crop photosynthetic productivity while reducing nitrogen fertilization and the concomitant pollution.
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PMID:Over-expression of cytosolic glutamine synthetase increases photosynthesis and growth at low nitrogen concentrations. 1143 23

Whether on the scale of a single cell, organ or organism, glutamine homeostasis is to a large extent determined by the activities of glutaminase (GA, EC 3.5.1.2) and glutamine synthetase (GS, EC 6.3.1.2), the two enzymes that are the focus of this report. GA and GS each provide examples of regulation of gene expression at many different levels. In the case of GA, two different genes (hepatic- and kidney-type GA) encode isoforms of this enzyme. The expression of hepatic GA mRNA is increased during starvation, diabetes and high protein diet through a mechanism involving increased gene transcription. In contrast, the expression of kidney GA mRNA is increased post-transcriptionally by a mechanism that increases mRNA stability during acidosis. We found recently that several isoforms of rat and human kidney-type GA are formed by tissue-specific alternative RNA splicing. Although the implications of this post-transcriptional processing mechanism for GA activity are not yet clear, it allows for the expression of different GA isoforms in different tissues and may limit the expression of GA activity in muscle tissues by diverting primary RNA transcripts to a spliceform that produces a nonfunctional translation product. The expression of GS enzyme is also regulated by both transcriptional and post-transcriptional mechanisms. For example, the GS gene is transcriptionally activated by glucocorticoid hormones in a tissue-specific fashion. This hormonal response allows GS mRNA levels to increase in selected organs during catabolic states. However, the ultimate level of GS enzyme expression is further governed by a post-transcriptional mechanism regulating GS protein stability. In a unique form of product feedback, GS protein turnover is increased by glutamine. This mechanism appears to provide a means to index the production of glutamine to its intracellular concentration and, therefore, to its systemic demand. Herein, we also provide experimental evidence that GS protein turnover is dependent upon the activity of the 26S proteosome.
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PMID:Mechanisms governing the expression of the enzymes of glutamine metabolism--glutaminase and glutamine synthetase. 1153 95

In this study, we addressed the effects of N limitation in Bradyrhizobium japonicum for its association with soybean roots. The wild-type strain LP 3001 grew for six generations with a growth rate of 1.2 day(-1) in a minimal medium with 28 mM mannitol as the carbon source and with the N source [(NH(4))(2)SO(4)] limited to only 20 microM. Under these conditions, the glutamine synthetase (GS) activity was five to six times higher than in similar cultures grown with 1 or 0.1 mM (NH(4))(2)SO(4). The NtrBC-inducible GSII form of this enzyme accounted for 60% of the specific activity in N-starved rhizobia, being negligible in the other two cultures. The exopolysaccharide (EPS) and capsular polysaccharide (CPS) contents relative to cell protein were significantly higher in the N-starved cultures, but on the other hand, the poly-3-hydroxybutyrate level did not rise in comparison with N-sufficient cultures. In agreement with the accumulation of CPS in N-starved cultures, soybean lectin (SBL) binding as well as stimulation of rhizobial adsorption to soybean roots by SBL pretreatment were higher. The last effect was evident only in cultures that had not entered stationary phase. We also studied nodC gene induction in relation to N starvation. In the chromosomal nodC::lacZ fusion Bj110-573, nodC gene expression was induced by genistein 2.7-fold more in N-starved young cultures than in nonstarved ones. In stationary-phase cultures, nodC gene expression was similarly induced in N-limited cultures, but induction was negligible in cultures limited by another nutrient. Nodulation profiles obtained with strain LP 3001 grown under N starvation indicated that these cultures nodulated faster. In addition, as culture age increased, the nodulation efficiency decreased for two reasons: fewer nodules were formed, and nodulation was delayed. However, their relative importance was different according to the nutrient condition: in older cultures the overall decrease in the number of nodules was the main effect in N-starved cultures, whereas a delay in nodulation was more responsible for a loss in efficiency of N-sufficient cultures. Competition for nodulation was studied with young cultures of two wild-type strains differing only in their antibiotic resistance, the N-starved cultures being the most competitive.
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PMID:Improved soybean root association of N-starved Bradyrhizobium japonicum. 1171 84

The effect of nitrogen and carbon status on the regulation of glutamine synthetase (GS) and glutamate synthase (GOGAT) were investigated in Corynebacterium glutamicum 13032. Under carbon-sufficient, nitrogen-limiting conditions, GS and GOGAT activities were five- and seven-fold higher, respectively, and transcription of the corresponding genes (glnA and gltBD) was similarly induced. GS activity was also induced in complete medium with added glucose, while GOGAT activity was unaffected. Under carbon-limiting, nitrogen-limiting conditions, the level of GS induction was reduced approximately three-fold, whereas GOGAT activity did not respond. Disruption of the hkm gene, encoding a putative histidine kinase upstream of gltBD, reduced the levels of GOGAT activity two-fold under both nitrogen-rich and nitrogen-limiting conditions. Promoter studies using a hkm-chloramphenicol acetylase fusion plasmid revealed that transcription of hkm is moderately induced (ca. 1.5-fold) by nitrogen starvation, indicating that the Hkm protein may play a role in signal transduction of the nutritional status of the growth medium.
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PMID:Nitrogen and carbon regulation of glutamine synthetase and glutamate synthase in Corynebacterium glutamicum ATCC 13032. 1175 Aug 28


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