1887

Abstract

Inspection of the genomic DNA sequence of the oral anaerobe reveals that the micro-organism possesses the peroxide-sensing transcription activator OxyR, but not the superoxide-sensing transcription factor SoxR. Investigatation of oxidative-stress-responsive proteins in by two-dimensional gel electrophoresis showed that two proteins were predominantly upregulated in oxidative conditions. In a mutant these two proteins were not induced by treatment with hydrogen peroxide under aerobic conditions. By N-terminal amino acid sequencing, the two proteins were found to be superoxide dismutase and alkyl hydroperoxide reductase, encoded by and , respectively. Northern blot and fusion analyses revealed that and were positively regulated by OxyR. Primer extension analysis located the promoter regions of and , and putative −35 boxes of these promoters were found immediately adjacent to their putative OxyR-binding sequences. Moreover, the promoter regions of and had the ability to bind OxyR protein. These results demonstrate that is one of the OxyR regulons, suggesting that OxyR functions as an intracellular redox sensor rather than a peroxide sensor in this organism. A gene of , which is taxonomically related to , is inducible by redox stresses but not controlled by its OxyR. A DNA fragment including the promoter region could bind the OxyR protein; however, a putative OxyR binding sequence within the DNA fragment was 14 bases distant from a putative −35 box of its promoter.

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2006-04-01
2020-10-20
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