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http://purl.uniprot.org/citations/19170879http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19170879http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19170879http://www.w3.org/2000/01/rdf-schema#comment"Quinones and alpha,beta-unsaturated carbonyls are naturally occurring electrophiles that target cysteine residues via thiol-(S)-alkylation. We analysed the global expression profile of Bacillus subtilis to the toxic carbonyls methylglyoxal (MG) and formaldehyde (FA). Both carbonyl compounds cause a stress response characteristic for thiol-reactive electrophiles as revealed by the induction of the Spx, CtsR, CymR, PerR, ArsR, CzrA, CsoR and SigmaD regulons. MG and FA triggered also a SOS response which indicates DNA damage. Protection against FA is mediated by both the hxlAB operon, encoding the ribulose monophosphate pathway for FA fixation, and a thiol-dependent formaldehyde dehydrogenase (AdhA) and DJ-1/PfpI-family cysteine proteinase (YraA). The adhA-yraA operon and the yraC gene, encoding a gamma-carboxymuconolactone decarboxylase, are positively regulated by the MerR-family regulator, YraB(AdhR). AdhR binds specifically to its target promoters which contain a 7-4-7 inverted repeat (CTTAAAG-N4-CTTTAAG) between the -35 and -10 elements. Activation of adhA-yraA transcription by AdhR requires the conserved Cys52 residue in vivo. We speculate that AdhR is redox-regulated via thiol-(S)-alkylation by aldehydes and that AdhA and YraA are specifically involved in reduction of aldehydes and degradation or repair of damaged thiol-containing proteins respectively."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2008.06568.x"xsd:string
http://purl.uniprot.org/citations/19170879http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2008.06568.x"xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Antelmann H."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Antelmann H."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Hecker M."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Hecker M."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Helmann J.D."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Helmann J.D."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Lalk M."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Lalk M."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Liebeke M."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Liebeke M."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Maeder U."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Maeder U."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Eiamphungporn W."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Eiamphungporn W."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Nguyen T.T.H."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/author"Nguyen T.T.H."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/19170879http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string