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J. Biol. Chem., Vol. 282, Issue 36, 25981-25985, September 7, 2007

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

Falko Hochgräfe, Jörg Mostertz¹, Dierk-Christoph Pöther, Dörte Becher, John D. Helmann, and Michael Hecker²

From the Institute for Microbiology, Ernst-Moritz-Arndt-University Greifswald, D-17487 Greifswald, Germany and the Department of Microbiology, Cornell University, Ithaca, New York 14853-8101

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.

Received for publication, May 30, 2007 , and in revised form, July 2, 2007.

^* This work was supported by grants from the European Union (LSHC-CT-2004-503468), the Deutsche Forschungsgemeinschaft (HE 1887/7-4), and the Bildungsministerium of des Landes Mecklenburg-Vorpommern (to M. H.) and by NSF Grant MCB-0640616 (to J. D. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ Present address: Interfaculty Inst. for Genetics and Functional Genomics, Junior Research Group Transcriptomics, University of Greifswald, 17489 Greifswald, Germany.

² To whom correspondence should be addressed. Tel.: 49-3834-864200; Fax: 49-3834-864202; E-mail: hecker{at}uni-greifswald.de.

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