This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fuangthong, M.
Right arrow Articles by Helmann, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fuangthong, M.
Right arrow Articles by Helmann, J. D.

 Previous Article  |  Next Article 

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.

OhrR Is a Repressor of ohrA, a Key Organic Hydroperoxide Resistance Determinant in Bacillus subtilis

Mayuree Fuangthong,1 Sopapan Atichartpongkul,2 Skorn Mongkolsuk,2,3 and John D. Helmann1,*

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 sigma 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 (sigma B, PerR, and OhrR) that contribute to peroxide stress responses.


* Corresponding author. Mailing address: Department of Microbiology, Cornell University, Ithaca, NY 14853-8101. Phone: (607) 255-6570. Fax: (607) 255-3904. E-mail: jdh9{at}cornell.edu.


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.



This article has been cited by other articles:

  • Saikolappan, S., Sasindran, S. J., Yu, H. D., Baseman, J. B., Dhandayuthapani, S. (2009). The Mycoplasma genitalium MG_454 Gene Product Resists Killing by Organic Hydroperoxides. J. Bacteriol. 191: 6675-6682 [Abstract] [Full Text]  
  • Poor, C. B., Chen, P. R., Duguid, E., Rice, P. A., He, C. (2009). Crystal Structures of the Reduced, Sulfenic Acid, and Mixed Disulfide Forms of SarZ, a Redox Active Global Regulator in Staphylococcus aureus. J. Biol. Chem. 284: 23517-23524 [Abstract] [Full Text]  
  • Kumarevel, T., Tanaka, T., Umehara, T., Yokoyama, S. (2009). ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators. Nucleic Acids Res 37: 4723-4735 [Abstract] [Full Text]  
  • Eiamphungporn, W., Soonsanga, S., Lee, J.-W., Helmann, J. D. (2009). Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro. Nucleic Acids Res 37: 1174-1181 [Abstract] [Full Text]  
  • Chen, H., Hu, J., Chen, P. R., Lan, L., Li, Z., Hicks, L. M., Dinner, A. R., He, C. (2008). The Pseudomonas aeruginosa multidrug efflux regulator MexR uses an oxidation-sensing mechanism. Proc. Natl. Acad. Sci. USA 105: 13586-13591 [Abstract] [Full Text]  
  • Hochgrafe, F., Wolf, C., Fuchs, S., Liebeke, M., Lalk, M., Engelmann, S., Hecker, M. (2008). Nitric Oxide Stress Induces Different Responses but Mediates Comparable Protein Thiol Protection in Bacillus subtilis and Staphylococcus aureus. J. Bacteriol. 190: 4997-5008 [Abstract] [Full Text]  
  • Soonsanga, S., Fuangthong, M., Helmann, J. D. (2007). Mutational Analysis of Active Site Residues Essential for Sensing of Organic Hydroperoxides by Bacillus subtilis OhrR. J. Bacteriol. 189: 7069-7076 [Abstract] [Full Text]  
  • Oh, S.-Y., Shin, J.-H., Roe, J.-H. (2007). Dual Role of OhrR as a Repressor and an Activator in Response to Organic Hydroperoxides in Streptomyces coelicolor. J. Bacteriol. 189: 6284-6292 [Abstract] [Full Text]  
  • Lee, J.-W., Soonsanga, S., Helmann, J. D. (2007). A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR. Proc. Natl. Acad. Sci. USA 104: 8743-8748 [Abstract] [Full Text]  
  • Panmanee, W., Vattanaviboon, P., Poole, L. B., Mongkolsuk, S. (2006). Novel Organic Hydroperoxide-Sensing and Responding Mechanisms for OhrR, a Major Bacterial Sensor and Regulator of Organic Hydroperoxide Stress. J. Bacteriol. 188: 1389-1395 [Abstract] [Full Text]  
  • Chuchue, T., Tanboon, W., Prapagdee, B., Dubbs, J. M., Vattanaviboon, P., Mongkolsuk, S. (2006). ohrR and ohr Are the Primary Sensor/Regulator and Protective Genes against Organic Hydroperoxide Stress in Agrobacterium tumefaciens. J. Bacteriol. 188: 842-851 [Abstract] [Full Text]  
  • Chatterjee, S. S., Hossain, H., Otten, S., Kuenne, C., Kuchmina, K., Machata, S., Domann, E., Chakraborty, T., Hain, T. (2006). Intracellular Gene Expression Profile of Listeria monocytogenes. Infect. Immun. 74: 1323-1338 [Abstract] [Full Text]  
  • Smits, W. K., Dubois, J.-Y. F., Bron, S., van Dijl, J. M., Kuipers, O. P. (2005). Tricksy Business: Transcriptome Analysis Reveals the Involvement of Thioredoxin A in Redox Homeostasis, Oxidative Stress, Sulfur Metabolism, and Cellular Differentiation in Bacillus subtilis. J. Bacteriol. 187: 3921-3930 [Abstract] [Full Text]  
  • Klomsiri, C., Panmanee, W., Dharmsthiti, S., Vattanaviboon, P., Mongkolsuk, S. (2005). Novel Roles of ohrR-ohr in Xanthomonas Sensing, Metabolism, and Physiological Adaptive Response to Lipid Hydroperoxide. J. Bacteriol. 187: 3277-3281 [Abstract] [Full Text]  
  • Wilkinson, S. P., Grove, A. (2004). HucR, a Novel Uric Acid-responsive Member of the MarR Family of Transcriptional Regulators from Deinococcus radiodurans. J. Biol. Chem. 279: 51442-51450 [Abstract] [Full Text]  
  • Lorquet, F., Goffin, P., Muscariello, L., Baudry, J.-B., Ladero, V., Sacco, M., Kleerebezem, M., Hols, P. (2004). Characterization and Functional Analysis of the poxB Gene, Which Encodes Pyruvate Oxidase in Lactobacillus plantarum. J. Bacteriol. 186: 3749-3759 [Abstract] [Full Text]  
  • Zuber, P. (2004). Spx-RNA Polymerase Interaction and Global Transcriptional Control during Oxidative Stress. J. Bacteriol. 186: 1911-1918 [Full Text]  
  • Mostertz, J., Scharf, C., Hecker, M., Homuth, G. (2004). Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress. Microbiology 150: 497-512 [Abstract] [Full Text]  
  • Nakano, S., Kuster-Schock, E., Grossman, A. D., Zuber, P. (2003). Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 100: 13603-13608 [Abstract] [Full Text]  
  • Cussiol, J. R. R., Alves, S. V., Antonio de Oliveira, M., Netto, L. E. S. (2003). Organic Hydroperoxide Resistance Gene Encodes a Thiol-dependent Peroxidase. J. Biol. Chem. 278: 11570-11578 [Abstract] [Full Text]  
  • Helmann, J. D., Wu, M. F. W., Gaballa, A., Kobel, P. A., Morshedi, M. M., Fawcett, P., Paddon, C. (2003). The Global Transcriptional Response of Bacillus subtilis to Peroxide Stress Is Coordinated by Three Transcription Factors. J. Bacteriol. 185: 243-253 [Abstract] [Full Text]  
  • Hahn, J.-S., Oh, S.-Y., Roe, J.-H. (2002). Role of OxyR as a Peroxide-Sensing Positive Regulator in Streptomyces coelicolor A3(2). J. Bacteriol. 184: 5214-5222 [Abstract] [Full Text]  
  • Fuangthong, M., Helmann, J. D. (2002). The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc. Natl. Acad. Sci. USA 99: 6690-6695 [Abstract] [Full Text]  
  • Shea, R. J., Mulks, M. H. (2002). ohr, Encoding an Organic Hydroperoxide Reductase, Is an In Vivo-Induced Gene in Actinobacillus pleuropneumoniae. Infect. Immun. 70: 794-802 [Abstract] [Full Text]