PMID:15448747
| Citation |
Benov, L, Sequeira, F and Beema, AF (2004) Role of rpoS in the regulation of glyoxalase III in Escherichia coli. Acta Biochim. Pol. 51:857-60 |
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| Abstract |
Methylglyoxal is an endogenous electrophile produced in Escherichia coli by the enzyme methylglyoxal synthase to limit the accumulation of phosphorylated sugars. In enteric bacteria methylglyoxal is detoxified by the glutathione-dependent glyoxalase I/II system, by glyoxalase III, and by aldehyde reductase and alcohol dehydrogenase. Here we demonstrate that glyoxalase III is a stationary-phase enzyme. Its activity reached a maximum at the entry into the stationary phase and remained high for at least 20 h. An rpoS- mutant displayed normal glyoxalase I and II activities but was unable to induce glyoxalase III in stationary phase. It thus appears that glyoxalase III is regulated by rpoS and might be important for survival of non-growing E. coli cultures. |
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| Keywords |
Aldehyde Oxidoreductases/metabolism; Bacterial Proteins/genetics; Escherichia coli/cytology; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins/genetics; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Genes, Bacterial; Lactoylglutathione Lyase/metabolism; Mutation; Pyruvaldehyde/metabolism; Sigma Factor/genetics; Thiolester Hydrolases/metabolism |
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