Journal article
Control of Copper Resistance and Inorganic Sulfur Metabolism by Paralogous Regulators in Staphylococcus aureus
The Journal of biological chemistry, Vol.286(15), pp.13522-13531
04/15/2011
DOI: 10.1074/jbc.M111.220012
PMCID: PMC3075698
PMID: 21339296
Abstract
All strains of Staphylococcus aureus encode a putative copper-sensitive operon repressor (CsoR) and one other CsoR-like protein of unknown function. We show here that NWMN_1991 encodes a bona fide Cu(I)-inducible CsoR of a genetically unlinked copA-copZ copper resistance operon in S. aureus strain Newman. In contrast, an unannotated open reading frame found between NWMN_0027 and NWMN_0026 (denoted NWMN_0026.5) encodes a CsoR-like regulator that represses expression of adjacent genes by binding specifically to a pair of canonical operator sites positioned in the NWMN_0027-0026.5 intergenic region. Inspection of these regulated genes suggests a role in assimilation of inorganic sulfur from thiosulfate and vectorial sulfur transfer, and we designate NWMN_0026.5 as CstR (CsoR-like sulfur transferase repressor). Expression analysis demonstrates that CsoR and CstR control their respective regulons in response to distinct stimuli with no overlap in vivo. Unlike CsoR, CstR does not form a stable complex with Cu(I); operator binding is instead inhibited by oxidation of the intersubunit cysteine pair to a mixture of disulfide and trisulfide linkages by a likely metabolite of thiosulfate assimilation, sulfite. CsoR is unreactive toward sulfite under the same conditions. We conclude that CsoR and CstR are paralogs in S. aureus that function in the same cytoplasm to control distinct physiological processes.
Details
- Title: Subtitle
- Control of Copper Resistance and Inorganic Sulfur Metabolism by Paralogous Regulators in Staphylococcus aureus
- Creators
- Nicholas Grossoehme - Indiana University BloomingtonThomas E. Kehl-Fie - Vanderbilt UniversityZhen Ma - Indiana University BloomingtonKeith W. Adams - Vanderbilt UniversityDarin M. Cowart - University of GeorgiaRobert A. Scott - University of GeorgiaEric P. Skaar - Vanderbilt UniversityDavid P. Giedroc - Indiana University Bloomington
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.286(15), pp.13522-13531
- Publisher
- Amer Soc Biochemistry Molecular Biology Inc
- DOI
- 10.1074/jbc.M111.220012
- PMID
- 21339296
- PMCID
- PMC3075698
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Number of pages
- 10
- Grant note
- U54AI057157 / NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of Allergy & Infectious Diseases (NIAID) R01 GM042569 / National Institutes of Health; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA National Institutes of Health, National Center for Research Resources; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Center for Research Resources (NCRR) American Heart Association Department of Energy, Office of Biological and Environmental Research; United States Department of Energy (DOE) T32HL094296 / NATIONAL HEART, LUNG, AND BLOOD INSTITUTE; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Heart Lung & Blood Institute (NHLBI) T32 HL094296 U54 AI057157 / Southeastern Regional Center of Excellence for Emerging Infections and Biodefense; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of Allergy & Infectious Diseases (NIAID) R01GM097225 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS)
- Language
- English
- Date published
- 04/15/2011
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984618504902771
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