The Bacteroides fragilis P20 scavengase homolog is important in the oxidative stress response but is not controlled by OxyR.

The oxidative stress response of obligate anaerobe, Bacteroides fragilis, is partially controlled by the redox regulator OxyR but an oxyR null mutant maintains a high level of aerotolerance. Studies using two-dimensional polyacrylamide gel electrophoresis showed that a thiol peroxidase-scavengase, Tps, was induced during oxygen exposure of an oxyR mutant. Tps is similar to 'atypical 2-cysteine peroxidases' such as scavengase p20 and it demonstrated catalytic activity against t-butyl hydroperoxide and H(2)O(2). A second gene, oim, encoding a putative membrane protein, was divergently transcribed from tps. Transcriptional analysis indicated that tps and oim were coordinately regulated by oxygen induction via an OxyR-independent mechanism. H(2)O(2) was a less potent inducer than oxygen exposure and in an oxyR mutant the mRNA levels were slightly reduced compared with the wild type. A null mutant of tps had increased sensitivity to killing by t-butyl hydroperoxide and oxygen but an oim mutant was similar to wild type. These data indicate that Tps is important for protection against some forms of oxidative stress.