Journal
MOLECULAR MICROBIOLOGY
Volume 71, Issue 4, Pages 876-894Publisher
WILEY
DOI: 10.1111/j.1365-2958.2008.06568.x
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Funding
- Deutsche Forschungsgemeinschaft
- Bundesministerium fur Bildung und Forschung [BACELL-SysMo 031397A]
- Fonds der Chemischen Industrie
- Bildungsministerium of the country Mecklenburg-Vorpommern
- European Union [LSHG-CT-2004-503468]
- BACELL-BaSysBio [LSHG-CT-2006-037469]
- National Science Foundation [MCB-0640616]
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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.
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