The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

glnA  -  glutamine synthetase

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of glnA

  • The top 10 homologs were all bacterial glutamine synthetases, including Salmonella typhimurium glnA [1].
  • Cloned H. pylori glnA complemented a glnA mutation in E. coli, and GlnA enzyme activity could be measured spectrophotometrically [1].
  • Role of glnA-linked genes in regulation of glutamine synthetase and histidase formation in Klebsiella aerogenes [2].
  • 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)] [3].
  • 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] [4].

High impact information on glnA


Chemical compound and disease context of glnA


Biological context of glnA

  • This mutant strain, Peru2DeltaglnA, is unable to grow on medium that does not contain glutamine; this growth deficiency is complemented by pKEK71-NotI, a plasmid containing a complete copy of the Salmonella typhimurium glnA gene, or by pTIC5, a derivative of pKEK71-NotI containing a 1 [14].
  • The glnA, ntrB, and ntrC genes form an operon [15].
  • DNA sequencing of these four genes, manB, pduF, glnA, and spaM, showed no genetic diversity among the isolates tested, with a 100% identity in nucleotide sequence [16].
  • The N-regulatory mutations are closely linked on the chromosome to the structural gene for glutamine synthetase, glnA: we discuss the possibility that they lie in a regulatory gene, glnR, which is distinct from glnA [13].
  • Although this phenotype resembles that of mutants with lesions in the regulatory gene for glutamine synthetase, glnG, these mutations do not lie in the glnG gene [10].

Associations of glnA with chemical compounds

  • In an attempt to produce a GlnA-deficient mutant of H. pylori, a kanamycin resistance cassette was cloned into the Tth111I site of H. pylori glnA [1].
  • Studies of the S. typhimurium gdh strain in ammonia-limited continuous culture and of gdh glnA double-mutant strains indicated that decreases in the glutamine pool remained profound in strains with a single pathway for ammonia assimilation [17].
  • Purification and characterization of the glutamine synthetase from one of the mutants and a control strain demonstrated that the mutant enzyme is defective in the reverse gamma-glutamyltransferase activity but has biosynthetic activity that is resistant to inhibition by L-methionine SR-sulfoximine [10].
  • We provide evidence that ammonium, nitrate, and light regulate GS transcript accumulation in green algae [18].
  • Analysis of GS transcript levels in mutants with defects in the nitrate assimilation pathway show that nitrate assimilation and ammonium assimilation are regulated independently [18].

Regulatory relationships of glnA


Other interactions of glnA


Analytical, diagnostic and therapeutic context of glnA


  1. Helicobacter pylori glutamine synthetase lacks features associated with transcriptional and posttranslational regulation. Garner, R.M., Fulkerson, J., Mobley, H.L. Infect. Immun. (1998) [Pubmed]
  2. Role of glnA-linked genes in regulation of glutamine synthetase and histidase formation in Klebsiella aerogenes. Rothman, N., Rothstein, D., Foor, F., Magasanik, B. J. Bacteriol. (1982) [Pubmed]
  3. Evidence that nitrogen regulatory gene ntrC of Salmonella typhimurium is transcribed from the glnA promoter as well as from a separate ntr promoter. Krajewska-Grynkiewicz, K., Kustu, S. Mol. Gen. Genet. (1984) [Pubmed]
  4. Characterization of mutations that lie in the promoter-regulatory region for glnA, the structural gene encoding glutamine synthetase. McCarter, L., Krajewska-Grynkiewicz, K., Trinh, D., Wei, G., Kustu, S. Mol. Gen. Genet. (1984) [Pubmed]
  5. Novel subunit-subunit interactions in the structure of glutamine synthetase. Almassy, R.J., Janson, C.A., Hamlin, R., Xuong, N.H., Eisenberg, D. Nature (1986) [Pubmed]
  6. Function of a bacterial activator protein that binds to transcriptional enhancers. Popham, D.L., Szeto, D., Keener, J., Kustu, S. Science (1989) [Pubmed]
  7. Nitrogen regulation in Salmonella typhimurium. Identification of an ntrC protein-binding site and definition of a consensus binding sequence. Ferro-Luzzi Ames, G., Nikaido, K. EMBO J. (1985) [Pubmed]
  8. Glutamate is required to maintain the steady-state potassium pool in Salmonella typhimurium. Yan, D., Ikeda, T.P., Shauger, A.E., Kustu, S. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  9. Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine. Liaw, S.H., Pan, C., Eisenberg, D. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  10. L-Methionine SR-sulfoximine-resistant glutamine synthetase from mutants of Salmonella typhimurium. Miller, E.S., Brenchley, J.E. J. Biol. Chem. (1981) [Pubmed]
  11. The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Gill, H.S., Eisenberg, D. Biochemistry (2001) [Pubmed]
  12. Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation. Gill, H.S., Pfluegl, G.M., Eisenberg, D. Biochemistry (2002) [Pubmed]
  13. Nitrogen control of Salmonella typhimurium: co-regulation of synthesis of glutamine synthetase and amino acid transport systems. Kustu, S.G., McFarland, N.C., Hui, S.P., Esmon, B., Ames, G.F. J. Bacteriol. (1979) [Pubmed]
  14. Development of a DeltaglnA balanced lethal plasmid system for expression of heterologous antigens by attenuated vaccine vector strains of Vibrio cholerae. Ryan, E.T., Crean, T.I., Kochi, S.K., John, M., Luciano, A.A., Killeen, K.P., Klose, K.E., Calderwood, S.B. Infect. Immun. (2000) [Pubmed]
  15. Simultaneous prevention of glutamine synthesis and high-affinity transport attenuates Salmonella typhimurium virulence. Klose, K.E., Mekalanos, J.J. Infect. Immun. (1997) [Pubmed]
  16. Multilocus sequence typing lacks the discriminatory ability of pulsed-field gel electrophoresis for typing Salmonella enterica serovar Typhimurium. Fakhr, M.K., Nolan, L.K., Logue, C.M. J. Clin. Microbiol. (2005) [Pubmed]
  17. Sensing of nitrogen limitation by Bacillus subtilis: comparison to enteric bacteria. Hu, P., Leighton, T., Ishkhanova, G., Kustu, S. J. Bacteriol. (1999) [Pubmed]
  18. Isolation and characterization of glutamine synthetase genes in Chlamydomonas reinhardtii. Chen, Q., Silflow, C.D. Plant Physiol. (1996) [Pubmed]
  19. Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA. Fisher, S.H., Brandenburg, J.L., Wray, L.V. Mol. Microbiol. (2002) [Pubmed]
  20. Regulation of the ammonia assimilatory enzymes in Salmonella typhimurium. Brenchley, J.E., Baker, C.A., Patil, L.G. J. Bacteriol. (1975) [Pubmed]
  21. Nucleotidylation, not phosphorylation, is the major source of the phosphotyrosine detected in enteric bacteria. Foster, R., Thorner, J., Martin, G.S. J. Bacteriol. (1989) [Pubmed]
  22. Supramolecular self-assembly of glutamine synthetase: mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking. Dabrowski, M.J., Yanchunas, J., Villafranca, B.C., Dietze, E.C., Schurke, P., Atkins, W.M. Biochemistry (1994) [Pubmed]
  23. Isolation and crystallization of unadenylylated glutamine synthetase from Salmonella typhimurium. Janson, C.A., Almassy, R.J., Westbrook, E.M., Eisenberg, D. Arch. Biochem. Biophys. (1984) [Pubmed]
WikiGenes - Universities