S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress

S-Thiolation is crucial for protection and regulation of thiol-containing proteins during oxidative stress and is frequently achieved by the formation of mixed disulfides with glutathione. However, many Gram-positive bacteria including Bacillus subtilis lack the low molecular weight (LMW) thiol glut...

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Veröffentlicht in:The Journal of biological chemistry 2007-09, Vol.282 (36), p.25981-25985
Hauptverfasser: Hochgräfe, Falko, Mostertz, Jörg, Pöther, Dierk-Christoph, Becher, Dörte, Helmann, John D., Hecker, Michael
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Sprache:eng
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Zusammenfassung:S-Thiolation is crucial for protection and regulation of thiol-containing proteins during oxidative stress and is frequently achieved by the formation of mixed disulfides with glutathione. However, many Gram-positive bacteria including Bacillus subtilis lack the low molecular weight (LMW) thiol glutathione. Here we provide evidence that S-thiolation by the LMW thiol cysteine represents a general mechanism in B. subtilis. In vivo labeling of proteins with [35S]cysteine and nonreducing two-dimensional PAGE analyses revealed that a large subset of proteins previously identified as having redox-sensitive thiols are modified by cysteine in response to treatment with the thiol-specific oxidant diamide. By means of multidimensional shotgun proteomics, the sites of S-cysteinylation for six proteins could be identified, three of which are known to be S-glutathionylated in other organisms.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.C700105200