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Regulation of katF and katE in Escherichia coli K-12 by weak acids


Regulation of katF and katE in Escherichia coli K-12 by weak acids



Journal of Bacteriology 174(14): 4769-4776



ISSN/ISBN: 0021-9193

PMID: 1385595

DOI: 10.1128/jb.174.14.4769-4776.1992

Chromosomal transcriptional and translational lacZ fusions to the katE (structural gene for the HPII hydroperoxidase) and katF (putative sigma factor required for katE expression) genes of Escherichia coli were isolated, and the regulation of these fusions was used to identify factors that control the expression of these two important antioxidant factors. While katE was found to be regulated primarily at the level of transcription (since induction patterns were similar for both transcriptional and translational fusions), katF expression was a function of both transcriptional and translational signals. The katE gene was induced 57-fold as cells entered the stationary phase, while katF was induced 23-fold. katF induction was coincident with katE induction and occurred at the onset of the stationary growth phase. Expression of both katE and katF could be induced by resuspending uninduced exponential-phase cells in spent culture supernatant recovered from stationary-phase cells. The component of stationary-phase culture supernatant responsible for induction of the katF regulon appeared to be acetate, since expression of both katE and katF fusions was induced when exponential-phase cells were exposed to this weak acid. Other weak acids, including propionate and benzoate, were also found to be effective inducers of expression of both katF and katE. Induction of katE and katF fusions was unaffected in merodiploid strains containing both mutant and wild-type alleles, indicating that expression of both genes is independent of the wild-type gene product. Examination of catalase zymograms prepared from cells exposed to various levels of acetate revealed that both HPI and HPII catalases are induced by this weak acid, suggesting that there is a common link in the regulation of these two enzymes.

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