Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1989 Jun;171(6):3572–3574. doi: 10.1128/jb.171.6.3572-3574.1989

Glutamine auxotrophs of Bacillus subtilis that overproduce glutamine synthetase antigen have altered conserved amino acids in or near the active site.

J Zhang 1, M Strauch 1, A I Aronson 1
PMCID: PMC210090  PMID: 2566596

Abstract

A number of mutations within the Bacillus subtilis glutamine synthetase (GS) gene result in altered catalytic properties and overproduction of the GS antigen. The restriction fragments containing mutations from three such mutants were sequenced, and they all had amino acid changes in conserved residues found either within or near sequences contributing to the active site of the Salmonella typhimurium GS.

Full text

PDF
3572

Images in this article

3573Image
on p.3573

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Almassy R. J., Janson C. A., Hamlin R., Xuong N. H., Eisenberg D. Novel subunit-subunit interactions in the structure of glutamine synthetase. 1986 Sep 25-Oct 1Nature. 323(6086):304–309. doi: 10.1038/323304a0. [DOI] [PubMed] [Google Scholar]
  2. Dean D. R., Hoch J. A., Aronson A. I. Alteration of the Bacillus subtilis glutamine synthetase results in overproduction of the enzyme. J Bacteriol. 1977 Sep;131(3):981–987. doi: 10.1128/jb.131.3.981-987.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Deuel T. F. Bacillus subtilis glutamine synthetase. Specific catalytic changes associated with limited sulfhydryl modification. J Biol Chem. 1971 Feb 10;246(3):599–605. [PubMed] [Google Scholar]
  4. Farber J. M., Levine R. L. Sequence of a peptide susceptible to mixed-function oxidation. Probable cation binding site in glutamine synthetase. J Biol Chem. 1986 Apr 5;261(10):4574–4578. [PubMed] [Google Scholar]
  5. Fisher S. H., Rosenkrantz M. S., Sonenshein A. L. Glutamine synthetase gene of Bacillus subtilis. Gene. 1984 Dec;32(3):427–438. doi: 10.1016/0378-1119(84)90018-0. [DOI] [PubMed] [Google Scholar]
  6. Fisher S. H., Sonenshein A. L. Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression. J Bacteriol. 1984 Feb;157(2):612–621. doi: 10.1128/jb.157.2.612-621.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Janson C. A., Kayne P. S., Almassy R. J., Grunstein M., Eisenberg D. Sequence of glutamine synthetase from Salmonella typhimurium and implications for the protein structure. Gene. 1986;46(2-3):297–300. doi: 10.1016/0378-1119(86)90415-4. [DOI] [PubMed] [Google Scholar]
  8. Schreier H. J., Fisher S. H., Sonenshein A. L. Regulation of expression from the glnA promoter of Bacillus subtilis requires the glnA gene product. Proc Natl Acad Sci U S A. 1985 May;82(10):3375–3379. doi: 10.1073/pnas.82.10.3375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Schreier H. J., Sonenshein A. L. Altered regulation of the glnA gene in glutamine synthetase mutants of Bacillus subtilis. J Bacteriol. 1986 Jul;167(1):35–43. doi: 10.1128/jb.167.1.35-43.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Strauch M. A., Aronson A. I., Brown S. W., Schreier H. J., Sonenhein A. L. Sequence of the Bacillus subtilis glutamine synthetase gene region. Gene. 1988 Nov 30;71(2):257–265. doi: 10.1016/0378-1119(88)90042-x. [DOI] [PubMed] [Google Scholar]
  11. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES