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Genetics and Molecular Biology |
Laboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok 10210, Thailand1
Department of Biotechnology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand2
Department of Microbiology, Wing Hall, Cornell University, Ithaca, NY 14853-8101, USA3
Author for correspondence: Skorn Mongkolsuk. Tel: +66 2 574 0623 ext. 1402. Fax: +66 2 574 2027. e-mail: skorn{at}tubtim.cri.or.th
Xanthomonas campestris Ohr (a protein involved in organic peroxide protection) and Escherichia coli OsmC (an osmotically inducible protein of unknown function) are related proteins. Database searches and phylogenetic analyses reveal that Ohr and OsmC homologues cluster into two related subfamilies of proteins widely distributed in both Gram-negative and Gram-positive bacteria. To determine if these two subfamilies are functionally distinct, ohr and osmC in Pseudomonas aeruginosa (a bacterium with one representative from each subfamily) were analysed. Only ohr mutants are hypersensitive to organic peroxide, and this phenotype can be restored by complementation with ohr but not osmC. In addition, expression of ohr was highly induced only by organic peroxides, and not by other oxidants or stresses. In contrast, osmC was induced by ethanol and osmotic stress. A similar pattern of regulation was observed for Ohr and OsmC homologues in the Gram-positive bacterium Deinococcus radiodurans, though uninduced expression was much higher and induction lower in this species. These data clearly support the conclusion that Ohr and OsmC define two functionally distinct subfamilies with distinct patterns of regulation.
Keywords: Pseudomonas aeruginosa, Deinococcus radiodurans, organic peroxide resistance, osmotic stress
Abbreviations: Ahp, alkyl hydroperoxide reductase; tBOOH, tert-butyl hydroperoxide
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