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PMID: 2999068 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Characterization of a gamma-glutamyl kinase from Escherichia coli that confers proline overproduction and osmotic tolerance.

Journal of bacteriology ·Vol. 164 ·No. 3 ·1985-12-00 ·Pages 1088-93

Smith LT

Abstract

Mutation(s) in the proBA operon of Escherichia coli confers proline overproduction and enhanced osmotic tolerance in enteric bacteria (L. N. Csonka, Mol. Gen. Genet. 182:82-86, 1981; M. J. Mahan and L. N. Csonka, J. Bacteriol. 156:1249-1262, 1983). A glutamate-dependent ATPase assay was developed and used to determine proB-encoded gamma-glutamyl kinase activity in the absence of glutamate-gamma-semialdehyde dehydrogenase. This assay indicated that the feedback insensitivity of mutant gamma-glutamyl kinase was independent of glutamate-gamma-semialdehyde dehydrogenase. However, the capacity of glutamate-gamma-semialdehyde dehydrogenase from the osmotolerant mutant to interact with the kinase was altered in thermal stability, suggesting that mutations in both proB and proA may be required for osmotolerance.

MeSH Terms
Adenosine Triphosphatases/metabolism Aldehyde Oxidoreductases/metabolism Escherichia coli/enzymology Glutamate-5-Semialdehyde Dehydrogenase Hot Temperature Hydroxamic Acids/metabolism Mutation Operon Osmotic Fragility Phosphotransferases/metabolism Phosphotransferases (Carboxyl Group Acceptor) Proline/biosynthesis Protein Denaturation Temperature
Chemicals
Hydroxamic Acids Proline Aldehyde Oxidoreductases Glutamate-5-Semialdehyde Dehydrogenase Phosphotransferases Phosphotransferases (Carboxyl Group Acceptor) glutamate 5-kinase Adenosine Triphosphatases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Smith L T
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18 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.164.3.1088-1093.1985
Published
1985-12-00
Pages
1088-93
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC219301
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.164.3.1088-1093.1985 PMC Full Text View journal details
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