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J Biol Chem. 2007 Sep 7;282(36):25981-5. Epub 2007 Jul 4.

S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.

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  • 1Institute for Microbiology, Ernst-Moritz-Arndt-University Greifswald, D-17487 Greifswald, Germany.


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 [(35)S]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.

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