The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
AUTOR(ES)
Fuangthong, Mayuree
FONTE
The National Academy of Sciences
RESUMO
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 thiol-disulfide 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=124464Documentos Relacionados
- OhrR Is a Repressor of ohrA, a Key Organic Hydroperoxide Resistance Determinant in Bacillus subtilis
- Complex Regulation of the Organic Hydroperoxide Resistance Gene (ohr) from Xanthomonas Involves OhrR, a Novel Organic Peroxide-Inducible Negative Regulator, and Posttranscriptional Modifications
- Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
- Hydrocarbon formation in the reductive cleavage of hydroperoxides by cytochrome P-450.
- Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif.
