期刊
FEMS MICROBIOLOGY LETTERS
卷 261, 期 2, 页码 211-217出版社
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2006.00353.x
关键词
thiol peroxidase; oxidative stress; Bacteroides fragilis; scavengase
类别
资金
- NIAID NIH HHS [AI40588, R01 AI040588] Funding Source: Medline
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 H2O2. 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. H2O2 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.
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