Journal of Bacteriology, July 2001, p. 4134-4141, Vol. 183, No. 14
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.14.4134-4141.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Department of Microbiology, Cornell University, Ithaca, New York 14853-8101,1 and Laboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok 10210,2 and Department of Biotechnology, Faculty of Science, Mahidol University, Bangkok 10400,3 Thailand
Received 1 February 2001/Accepted 26 April 2001
Bacillus subtilis displays a complex adaptive response
to the presence of reactive oxygen species. To date, most proteins that
protect against reactive oxygen species are members of the peroxide-inducible PerR and
B regulons. We investigated
the function of two B. subtilis homologs of the
Xanthomonas campestris organic hydroperoxide resistance (ohr) gene. Mutational analyses indicate that both
ohrA and ohrB contribute to organic peroxide
resistance in B. subtilis, with the OhrA protein playing
the more important role in growing cells. Expression of
ohrA, but not ohrB, is strongly and
specifically induced by organic peroxides. Regulation of
ohrA requires the convergently transcribed gene,
ohrR, which encodes a member of the MarR family of
transcriptional repressors. In an ohrR mutant, ohrA expression is constitutive, whereas expression of the
neighboring ohrB gene is unaffected. Selection for mutant
strains that are derepressed for ohrA transcription
identifies a perfect inverted repeat sequence that is required for
OhrR-mediated regulation and likely defines an OhrR binding site. Thus,
B. subtilis contains at least three regulons
(
B, PerR, and OhrR) that contribute to peroxide stress responses.
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