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Gene Review:

glnA - glutamine synthetase

Staphylococcus aureus RF122

Gustafson, J. et al., Lei, M. et al., Schreier, H.J. et al., Greenlee, W.J. et al.

Schreier, Caruso, Maier,

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Disease relevance of glnA

Chymotrypsin and Staphylococcus aureus protease produce similar cleavages in glutamine synthetase [1].
Limited proteolysis of glutamine synthetase from Escherichia coli has been studied under nondenaturing conditions (pH 7.6, 20 degrees C) [1].
GlnR plays a major role in regulation in Bacillus subtilis by directly controlling expression of glutamine synthetase (GS) as well as several genes involved in nitrogen metabolism [2].

High impact information on glnA

Tryptic digestion is also retarded by some of the feedback inhibitors of glutamine synthetase including CTP, L-alanine, L-serine, L-histidine, and glucosamine 6-phosphate [1].
Limited proteolysis of glutamine synthetase is inhibited by glutamate and by feedback inhibitors [1].
With tabtoxinine, a potent inhibitor of glutamine synthetase, as a model, beta-lactams 9R and 9S were synthesized as potential precursors of a D-alanyl phosphate mimic [3].
Northern (RNA) blots probed with putative glnR or glnA fragments revealed that 1.7- and 1.9-kb transcripts characteristic of wild-type cells were replaced by less abundant 7.0- and 7.2-kb transcripts in the femC::omega 2005 mutant [4].
The femC locus of Staphylococcus aureus required for methicillin resistance includes the glutamine synthetase operon [4].

Biological context of glnA

The Tn551 insertion femC::omega 2005 was found to interrupt an open reading frame coding for a putative protein of 121 amino acids which is highly similar to the glutamine synthetase repressors (GlnR) of Bacillus spp [4].
Total glutamine synthetase activity was also decreased in the mutant strain; the addition of glutamine to defined media restored the wild-type methicillin resistance phenotype of the femC mutant [4].

Associations of glnA with chemical compounds

These results suggest that the loss of wild-type levels of glutamine synthetase and the consequent decrease in glutamine availability cause a decreased level of methicillin resistance [4].

References

Limited proteolysis of glutamine synthetase is inhibited by glutamate and by feedback inhibitors. Lei, M., Aebi, U., Heidner, E.G., Eisenberg, D. J. Biol. Chem. (1979) [Pubmed]
Control of Bacillus subtilis glutamine synthetase expression by glnR from Staphylococcus aureus. Schreier, H.J., Caruso, S.M., Maier, K.C. Curr. Microbiol. (2000) [Pubmed]
Synthesis of an analogue of tabtoxinine as a potential inhibitor of D-alanine:D-alanine ligase (ADP forming). Greenlee, W.J., Springer, J.P., Patchett, A.A. J. Med. Chem. (1989) [Pubmed]
The femC locus of Staphylococcus aureus required for methicillin resistance includes the glutamine synthetase operon. Gustafson, J., Strässle, A., Hächler, H., Kayser, F.H., Berger-Bächi, B. J. Bacteriol. (1994) [Pubmed]

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