Nitrogen Regulation in Salmonella typhimurium

Kustu, Sydney; Burton, Doris; García, Emilio García; McCarter, Linda L.; McFarland, Nancy

doi:10.1016/b978-0-12-506040-0.50011-x

Cited by 9 publications

(10 citation statements)

References 29 publications

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“…In E. coli and S. typhimurium the ntrB and ntrC genes, which are closely linked to the glnA gene, regulate highaffinity arginine and glutamine transport systems and the activation of the K. pneumoniae hut operon carried by E. coli ET8051 (16,23,27,38). The ability of the E. coli YMC10, ET8051, and ET8051(pHZ200) strains to grow on minimal media containing arginine or low levels of glutamine was determined (Table 3).…”

Section: Resultsmentioning

confidence: 99%

“…The regulation of transcription of the structural gene for GS, glnA, has been extensively studied in the gram-negative bacteria Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium. In these bacteria transcription of gInA is regulated by the products of the ntrB (glnL) and ntrC (glnG) genes, which are linked to the gInA gene, as well as by the product of the unlinked ntrA (glnF) gene (11,16,20,23,27). However, there is no evidence for regulatory ntr genes in the gram-positive aerobic sporulating bacterium Bacillus subtilis (9,12,20), and GS seems to play a role in regulating its own synthesis (6,30).…”

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confidence: 99%

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Cloning, Expression, and Purification of Glutamine Synthetase from Clostridium acetobutylicum

Usdin

Zappe

Jones

et al. 1986

Appl Environ Microbiol

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A glutamine synthetase (GS) gene, glnA, from the gram-positive obligate anaerobe Clostridium acetobutylicum was cloned on recombinant plasmid pHZ200 and enabled Escherichia coli glnA deletion mutants to utilize (NH4)2SO4 as a sole source of nitrogen. The cloned C. acetobutylicum gene was expressed from a regulatory region contained within the cloned DNA fragment. ginA expression was subject to nitrogen regulation in E. coli. This cloned glnA DNA did not enable an E. coli ginA ntrB ntrC deletion mutant to utilize arginine or low levels of glutamine as sole nitrogen sources, and failed to activate histidase activity in this strain which contained the Klebsiella aerogenes hut operon. The GS produced by pHZ200 was purified and had an apparent subunit molecular weight of approximately 59,000. There was no DNA or protein homology between the cloned C. acetobutylicum ginA gene and GS and the corresponding gene and GS from E. coli. The C. acetobutylicum GS was inhibited by Mg2' in they -glutamyl transferase assay, but there was no evidence that the GS was adenylylated. * Corresponding author. vated or regulated by plasmid pC1857 which contains a temperature-sensitive lambda repressor gene (28). The EcoRI gene has a single BglII cloning site. C. acetobutylicum P262 was grown from heat-shocked spores to mid

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Cloning, Expression, and Purification of Glutamine Synthetase from Clostridium acetobutylicum

Usdin

Zappe

Jones

et al. 1986

Appl Environ Microbiol

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“…It has been shown that the product of the glnF gene is required for the synthesis of glutamine synthetase (14,17,18). One model suggests that this product converts the product of another gene, ginG, from a repressor to an activator of glutamine synthetase formation (14,18,19). The fact that glnF mutants lacking PII due to a mutation in glnB fail to produce glutamine synthetase indicates that the product of the ginG gene, even in the absence of PIIA, is fully capable of repressing glutamine synthetase (14).…”

Section: Resultsmentioning

confidence: 99%

Regulation of the synthesis of glutamine synthetase by the PII protein in Klebsiella aerogenes.

Foor¹,

Reuveny²,

Magasanik³

1980

Proc. Natl. Acad. Sci. U.S.A.

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Certain mutations at the glnB locus result in the failure to fully derepress glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2] and to convert it to the active nonadenylylated form in response to nitrogen limitation. In these mutants the P11 regulatory protein is altered such that it cannot be converted by uridylyltransferase to the form stimulating deadenylylation of glutamine synthetase by adenylyltransferase. Additional mutations as well as insertions of transposon Tn5 at the gInB site result in the loss of P11. The loss of PI, does not prevent adenylylation and deadenylylation of glutamine synthetase but reduces the rates of these reactions. Cells lacking PII have a high level of glutamine synthetase even when they are grown with an excess of ammonia and the enzyme is highly adenylylated. The results suggest that the PII protein plays a role, independent of its effect on adenylylation, in the regulation of the level of glutamine synthetase. The biosynthetic activity of glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2] in enteric bacteria is progressively decreased by the specific covalent attachment of adenylyl groups to each of its 12 subunits (1). This reversible modification is catalyzed by the enzyme adenylyltransferase (ATase). Adenylylation is stimulated by the small (44,000 dalton) regulatory protein PITA (2). Deadenylylation is stimulated by PIID, a uridylylated form of PIIA. The interconversion of PIIA and PIID is catalyzed by uridylyltransferase (UTase) and uridylyl-removing enzyme(s).Glutamine stimulates the adenylylation reaction as well as the conversion of PID to PITA; 2-ketoglutarate inhibits adenylylation but stimulates the deadenylylation reaction and the conversion of PITA to PIID. Glutamine inhibits the latter two reactions. Thus, the relative amounts of PITA and PIID and the adenylylation state of glutamine synthetase are determined in a reciprocal manner by the concentrations of these two metabolites; these in turn are determined by the availability of nitrogen in the cell. When growth is limited by the nitrogen source, the level of 2-ketoglutarate is high, the level of glutamine is low, and the adenylylation state of glutamine synthetase is low. When growth is limited by some other component, such as carbon, glutamine is high, 2-ketoglutarate is low, and the adenylylation state of glutamine synthetase is high (3). In addition, the synthesis of glutamine synthetase is regulated by the availability of nitrogen. During nitrogen-limited growth the level of glutamine synthetase is high, whereas during carbonlimited growth the level of glutamine synthetase is low (3,4).We have studied the regulation of the level and the adenyl- MATERIALS AND METHODS Bacterial Strains. All strains are phage Pl-sensitive derivatives (5) of K. aerogenes MK-1 (6). Media have been described (7).Genetic Techniques. Generalized transduction was carried out as described by Goldberg et al. (5) with phage P1clrLO0CM (obtained from B. Tyler). Lysates of donor st...

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“…Adenylylation is the covalent attachment of AMP residues to the individual subunits of the enzyme (8). In cells grown in limiting concentrations of ammonia, transcription from ginA probably increases due both to the lifting ofrepression and to the activation of transcription by a positive regulator(s) (9,10). After the shift from ammonia-excess to ammonia-limiting conditions, the combined effect of these controls is to increase Gin synthetase activity within the cell by a factor of 5 or more.…”

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A cloned cyanobacterial gene for glutamine synthetase functions in Escherichia coli, but the enzyme is not adenylylated.

Fisher¹,

Tuli²,

Haselkorn³

1981

Proc. Natl. Acad. Sci. U.S.A.

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Nitrogen Regulation in Salmonella typhimurium

Cited by 9 publications

References 29 publications

Cloning, Expression, and Purification of Glutamine Synthetase from Clostridium acetobutylicum

Cloning, Expression, and Purification of Glutamine Synthetase from Clostridium acetobutylicum

Regulation of the synthesis of glutamine synthetase by the PII protein in Klebsiella aerogenes.

A cloned cyanobacterial gene for glutamine synthetase functions in Escherichia coli, but the enzyme is not adenylylated.

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