Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of transcription and translation inhibitors on NADP-glutamate dehydrogenase and glutamine synthetase synthesis in nitrogen-starving Ankistrodesmus braunii cells have been studied. Considering the results obtained one can suggest that both enzymes are coded in the chloroplast genome and that during nitrogen starvation specific mRNA's are partly transferred from the chloroplast into the cytoplasm and can be translated there on 80S ribosomes.
Mol Cell Biochem 1982 Dec 10
PMID:The role of chloroplast and cytoplasm in the NADP-glutamate dehydrogenase and glutamine synthetase synthesis in Ankistrodesmus cells. 613 76

We present pharmacological and genetic evidence that regulation of different genes by glucocorticoid hormones in the rat hepatoma cell line, HTC, occurs in a coordinate manner. We have analyzed the responses of four different glucocorticoid-inducible proteins, tyrosine aminotransferase [L-tyrosine:2-oxoglutarate aminotransferase (EC 2.6.1.5)], glutamine synthetase [L-glutamate:ammonia ligase (EC 6.3.1.2)], a secreted glycoprotein Belt I, and the mouse mammary tumor virus (MMTV)-encoded protein (gp52) in these cells. The concentration of dexamethasone necessary for half-maximal induction of each of these proteins is 10-20 nM, the same concentration necessary to half-saturate glucocorticoid receptors. Furthermore, glucocorticoids of varying potency elicit parallel inductions of these markers. MSN5.3, a glucocorticoid receptor-defective cell line selected for its inability to induce gp52, is also unable to induce the other three cellular gene products. In contrast, another class of variants incapable of gp52 induction retains inducibility of the other three markers. We show here by "superinfection" with MMTV that these cells harbor a defect in the original integrated provirus itself and not in the cellular induction machinery. The results presented here suggest that the induction of glucocorticoid-responsive genes in these cells is mediated by a single glucocorticoid induction pathway.
Mol Pharmacol 1983 May
PMID:Analysis of glucocorticoid-inducible genes in wild-type and variant rat hepatoma cells. 613 49

Using the Casadaban Mu d1 phage (Casadaban and Cohen 1979) we fused cis-acting regulatory sites for the Salmonella typhimurium glnA gene, the structural gene encoding glutamine synthetase, to lacZ so that transcription of lacZ was controlled by the glnA promoter-operator. Activities of beta-galactosidase in two glnA::Mu d1 fusion strains were high, approximately 25% and 125% the induced level of beta-galactosidase when transcription of lacZ is under control of the lac promoter, indicating that glutamine synthetase is not required to activate transcription of its own structural gene. Introduction of nitrogen regulatory mutations ntrA::Tn10 or ntrC::Tn10 into fusion strains resulted in greatly decreased synthesis of beta-galactosidase indicating that the positive regulatory factors encoded by ntrA and ntrC activate glnA expression at the level of transcription. Comparison of beta-galactosidase activities in fusion strains with those in fusions carrying ntrC or ntrA mutations indicated that: 1) the magnitude of activation of glnA expression is at least 43-fold; 2) the magnitude of repression is approximately 13-fold and repression occurs at the level of transcription; 3) the degree of modulation of glnA expression by ntr products is at least 560-fold (13 X 43); and 4) glutamine synthetase is not required for repression of transcription of its own structural gene. In contrast to strains carrying non-polar mutations in glnA, strains carrying glnA insertion mutations, including glnA::Mu d1 fusions, are apparently defective in activating expression of some nitrogen controlled genes other than glnA. Defects cannot be accounted for by the absence of glutamine synthetase protein or catalytic activity; they appear to be due to decreased expression of nitrogen regulatory genes ntrB and/or ntrC, which are adjacent to glnA.
Mol Gen Genet 1983
PMID:Regulation of transcription of glnA, the structural gene encoding glutamine synthetase, in glnA::Mu d1 (ApR, lac) fusion strains of Salmonella typhimurium. 613 39

Previous work has indicated that nitrogen regulatory genes ntrB and ntrC of Salmonella typhimurium are closely linked to glnA, the structural gene encoding glutamine synthetase; proceeding clockwise the order of genes in the 86 U region of the map is polA...ntrC ntrB glnA glnA promoter...rha. To study ntrC transcription we have constructed operon fusions of ntrC to lacZ using the Casadaban Mu d1 (Apr lac) phage so that we can measure beta-galactosidase activity as a reflection of ntrC transcription and we have introduced into fusion strains promoter constitutive mutations at glnA [glnAp(Con)]. The glnAp(Con) mutations, which elevate glnA expression in fusion strains, also elevate beta-galactosidase activity, indicating that ntrC is cotranscribed with glnA. Consistent with this interpretation, polar insertion mutations in glnA decrease beta-galactosidase activity of fusion strains carrying glnAp(Con) mutations. However, glnA insertions do not eliminate beta-galactosidase activity of glnAp(Con) ntrC::Mu d1 strains and they have little effect on beta-galactosidase activity of the original ntrC::Mu d1 fusion strains. The latter results confirm that ntrC can also be transcribed from an ntr promoter downstream of glnA. Polar insertion mutations in ntrB eliminate beta-galactosidase activity of both the original fusion strains and fusion strains carrying glnA(Con) mutations, indicating that the ntr promoter lies between glnA and ntrB.
Mol Gen Genet 1984
PMID:Evidence that nitrogen regulatory gene ntrC of Salmonella typhimurium is transcribed from the glnA promoter as well as from a separate ntr promoter. 614 Jun 20

Mutants resistant to 80 microM L-methionine-DL-sulfoximine (MS) were isolated on glucose-minimal 15 mM NH4+ medium plates from Escherichia coli cells which were hypersensitive to this concentration of the analogue by virtue of their harboring glnG mutations. MS-resistant mutants derived from strain MX902 carried, in addition to its glnG74 ::Tn5 allele, mutations tightly linked to glnA, as shown by P1-mediated transduction experiments. One particular allele, gln-76, which suppressed the MS-sensitivity conferred by glnG74 ::Tn5 but not its Ntr- phenotype (inability to transport and utilize compounds such as arginine or proline as the only nitrogen sources), was shown to allow constitutive expression of glutamine synthetase in the absence not only of a functional glnG product but also of a functional glnF product. This behavior was found to be cis-dominant in complementation experiments with F'14 merogenotes . In an otherwise wild-type genetic background as in MX929 (gln-76 glnA+ glnL+ glnG+ glnF +), however, normal activation, mediated by the glnG and glnF products was preferred over that mediated by gln-76.
Mol Gen Genet 1984
PMID:cis-Dominant, glutamine synthetase constitutive mutations of Escherichia coli independent of activation by the glnG and glnF products. 614 84

In enteric bacteria products of nitrogen regulatory genes ntrA, ntrB and ntrC are known to regulate transcription both positively and negatively at glnA, the structural gene encoding glutamine synthetase [L-glutamate:ammonia-ligase (ADP-forming), EC 6.3.1.2]. We have characterized two types of cis-acting mutations in the glnA promoter-regulatory region. One type, which we have called promoter Up [glnAp (Up)], elevates transcription of glnA to high levels without need for ntr-mediated activation but leaves expression sensitive to ntr-mediated repression. The other type renders glnA transcription insensitive to repression but leaves it normally responsive to activation. Properties of the two types of promoter-regulatory mutations suggest that sites for ntr-mediated activation of glnA transcription are functionally distinct from sites for ntr-mediated repression.
Mol Gen Genet 1984
PMID:Characterization of mutations that lie in the promoter-regulatory region for glnA, the structural gene encoding glutamine synthetase. 615 Nov 13

Stadtman, Holzer and their colleagues (reviewed in Stadtman and Ginsburg 1974) demonstrated that the enzyme glutamine synthetase (GS) [(L-glutamate: ammonia ligase (ADP-forming), EC 6.3.1.2] is covalently modified by adenylylation in a variety of bacterial genera and that the modification is reversible. These studies further indicated that adenylylated GS is the less active form in vitro. To assess the physiological significance of adenylylation of GS we have determined the growth defects of mutant strains (glnE) of S. typhimurium that are unable to modify GS and we have determined the basis for these growth defects. The glnE strains, which lack GS adenylyl transferase activity (ATP: [L-glutamate: ammonia ligase (ADP-forming)] adenylyltransferase, EC 2.7.7.42), show a large growth defect specifically upon shift from a nitrogen-limited growth medium to medium containing excess ammonium (NH4+). The growth defect appears to be due to very high catalytic activity of GS after shift, which lowers the intracellular glutamate pool to approximately 10% that under preshift conditions. Consistent with this view, recovery of a rapid growth rate on NH4+ is accompanied by an increase in the glutamate pool. The glnE strains have normal ATP pools after shift. They synthesize very large amounts of glutamine and excrete glutamine into the medium, but excess glutamine does not seem to inhibit growth. We hypothesize that a major function for adenylylation of bacterial GS is to protect the cellular glutamate pool upon shift to NH4+ -excess conditions and thereby to allow rapid growth.
Mol Gen Genet 1984
PMID:Covalent modification of bacterial glutamine synthetase: physiological significance. 615 21

Mutants of the yeast Saccharomyces cerevisiae have been isolated which fail to derepress glutamine synthetase upon glutamine limitation. The mutations define a single nuclear gene, GLN3, which is located on chromosome 5 near HOM3 and HIS1 and is unlinked to the structural gene for glutamine synthetase, GLN1. The three gln3 mutations are recessive, and one is amber suppressible, indicating that the GLN3 product is a positive regulator of glutamine synthetase expression. Four polypeptides, in addition to the glutamine synthetase subunit are synthesized at elevated rates when GLN3+ cultures are shifted from glutamine to glutamate media as determined by pulse-labeling and one- and two-dimensional gel electrophoresis. The response of all four proteins is blocked by gln3 mutations. In addition, the elevated NAD-dependent glutamate dehydrogenase activity normally found in glutamate-grown cells is not found in gln3 mutants. Glutamine limitation of gln1 structural mutants has the opposite effect, causing elevated levels of NAD-dependent glutamate dehydrogenase even in the presence of ammonia. We suggest that there is a regulatory circuit that responds to glutamine availability through the GLN3 product.
Mol Cell Biol 1984 Dec
PMID:Regulation of glutamine-repressible gene products by the GLN3 function in Saccharomyces cerevisiae. 615 12

Production of glutamine synthetase in Saccharomyces cerevisiae is controlled by three regulatory systems. One system responds to glutamine levels and depends on the positively acting GLN3 product. This system mediates derepression of glutamine synthetase in response to pyrimidine limitation as well, but genetic evidence argues that this is an indirect effect of depletion of the glutamine pool. The second system is general amino acid control, which couples derepression of a variety of biosynthetic enzymes to starvation for many single amino acids. This system operates through the positive regulatory element GCN4. Expression of histidinol dehydrogenase, which is under general control, is not stimulated by glutamine limitation. A third system responds to purine limitation. No specific regulatory element has been identified, but depression of glutamine synthetase is observed during purine starvation in gln3 gcn4 double mutants. This demonstrates that a separate purine regulatory element must exist. Pulse-labeling and immunoprecipitation experiments indicate that all three systems control glutamine synthetase at the level of subunit synthesis.
Mol Cell Biol 1984 Dec
PMID:Three regulatory systems control production of glutamine synthetase in Saccharomyces cerevisiae. 615 13

A recombinant plasmid (pcPvNGS-01) containing sequences related to glutamine synthetase (GS) has been identified from a cDNA library constructed from poly (A)+ RNA isolated from root nodules of Phaseolus vulgaris L. The identification of this recombinant relied on the observations that: (a) the clone hybridized strongly to purified GS mRNA; (b) in hybrid-select translation experiments, the clone selected mRNA that produced a polypeptide identical in molecular weight to purified GS subunits which was immunoprecipitated with anti-GS-antiserum; and (c) the translated nucleotide sequence of the cloned cDNA was homologous to a partial amino acid sequence of higher plant GS. The cloned cDNA hybridized to poly (A)+ RNA of different mobilities from leaves, roots, and nodules of P. vulgaris. In RNA "dot" blots washed at different stringencies, differences were observed both in the relative amounts of GS mRNA in different tissues and in the strength of their hybridization to the cDNA probe. The cloned probe hybridized to several fragments of restricted P. vulgaris DNA but not to DNA from Rhizobium phaseoli. These results suggest that GS is coded for by a small multigene family showing organ-specific expression.
J Mol Appl Genet 1984
PMID:Glutamine synthetase of Phaseolus vulgaris L.: organ-specific expression of a multigene family. 615 82


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>