Identification and Characterization of
 gsp65
 , an Organic Hydroperoxide Resistance (
 ohr
 ) Gene Encoding a General Stress Protein in
 Enterococcus faecalis

Rincé, Alain; Giard, Jean‐Christophe; Pichereau, Vianney; Flahaut, Sigrid; Auffray, Yanick

doi:10.1128/jb.183.4.1482-1488.2001

Cited by 53 publications

(46 citation statements)

References 34 publications

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“…In addition to X. campestris and B. subtilis, ohr homologues been identified in Pseudomonas aeruginosa (Ochsner et al, 2001), Enterococcus faecalis (Rince et al, 2001) and Actinobacillus pleuropneumoniae (Shea and Mulks, 2002). Although the details of regulation in these systems have not yet been reported, the frequent linkage to an ohrR homologue suggests that this peroxide-sensing repressor is widespread (Sukchawalit et al, 2001).…”

Section: Regulation Of Peroxide Stress Responses 13mentioning

confidence: 99%

Regulation of inducible peroxide stress responses

Mongkolsuk¹,

Helmann²

2002

Molecular Microbiology

267

217

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Summary Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co‐ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide‐sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide‐ sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative.

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Section: Regulation Of Peroxide Stress Responses 13mentioning

confidence: 99%

Regulation of inducible peroxide stress responses

Mongkolsuk¹,

Helmann²

2002

Molecular Microbiology

267

217

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“…Interestingly, a second organic peroxide resistance gene, ohrB, is under control of B (11). The role of Ohr proteins in organic peroxide resistance has now been demonstrated in Xanthomonas campestris, Pseudomonas aeruginosa, Enterococcus faecalis, Actinobacillus pleuropneumoniae, and B. subtilis (10,(12)(13)(14)(15)(16). In many organisms, ohr genes are flanked by genes encoding OhrR homologs (9).…”

Section: R Eactive Oxygen Species (Ros) Including H 2 O 2 Superoximentioning

confidence: 99%

The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative

Fuangthong

Helmann

2002

Proc. Natl. Acad. Sci. U.S.A.

213

238

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Reactive oxygen species induce the expression of detoxification and repair genes critical for life in an aerobic environment. Bacterial factors that sense reactive oxygen species use either thioldisulfide exchange reactions (OxyR, RsrA) or redox labile 2Fe-2S clusters (SoxR). We demonstrate that the reduced form of Bacillus subtilis OhrR binds cooperatively to two adjacent inverted repeat sequences in the ohrA control region and thereby represses transcription. In the presence of organic hydroperoxides, OhrR is inactivated by the reversible oxidation of a single conserved cysteine residue to the corresponding cysteine-sulfenic acid, and perhaps to higher oxidation states.peroxide stress ͉ oxidative stress ͉ peroxiredoxin ͉ alkyl hydroperoxide reductase ͉ Bacillus subtilis

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“…ohr confers resistance to organic hydroperoxides, and inactivation of the gene leads to increased sensitivity to organic peroxides (19). ohr homologues are widely distributed in both gram-positive and gram-negative bacteria (1,6,12,22,25,28). The structure and biochemical mechanism of Ohr have been elucidated (12).…”

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confidence: 99%

Novel Roles of ohrR - ohr in Xanthomonas Sensing, Metabolism, and Physiological Adaptive Response to Lipid Hydroperoxide

et al. 2005

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Lipid hydroperoxides are highly toxic to biological systems. Here, the Xanthomonas campestris pv. phaseoli sensing and protective systems against linoleic hydroperoxide (LOOH) were investigated by examining the phenotypes, biochemical and regulatory characteristics of various Xanthomonas mutants in known peroxide resistance pathways. Analysis of LOOH resistance levels indicates that both alkyl hydroperoxide reductase (AhpC) and organic hydroperoxide resistance enzyme (Ohr) have important and nonredundant roles in the process. Nonetheless, inactivation of ohr leads to a marked reduction in LOOH resistance levels. The regulatory characteristics of an ohr mutant add further support to its primary role in LOOH protection. Northern analysis shows that LOOH had differential effects on induction of ahpC and ohr expression with the latter being more sensitive to the inducer. Analysis of the ahpC and ohr promoters confirmed that the LOOH-dependent induction of these promoters is mediated by the transcription regulators OxyR and OhrR, respectively. Using the in vivo promoter assays and the in vitro gel mobility shift assay, we show that LOOH directly oxidized OhrR at the sensing residue Cys-22 leading to its inactivation. In addition, physiological analysis shows that pretreatment of X. campestris pv. phaseoli with a sublethal dose of LOOH induced high levels of resistance to subsequent exposure to lethal concentrations of LOOH. This novel LOOH-induced adaptive response requires a functional ohrR-ohr operon. These data illustrate an important novel physiological role for the ohrR-ohr system in sensing and inactivating lipid hydroperoxides.

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Identification and Characterization of gsp65 , an Organic Hydroperoxide Resistance ( ohr ) Gene Encoding a General Stress Protein in Enterococcus faecalis

Cited by 53 publications

References 34 publications

Regulation of inducible peroxide stress responses

Regulation of inducible peroxide stress responses

The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative

Novel Roles of ohrR - ohr in Xanthomonas Sensing, Metabolism, and Physiological Adaptive Response to Lipid Hydroperoxide

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