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J. Biol. Chem., Vol. 283, Issue 31, 21571-21578, August 1, 2008

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In Vivo Targets of S-Thiolation in Chlamydomonas reinhardtii^*

Laure Michelet, Mirko Zaffagnini, Hélène Vanacker, Pierre Le Maréchal, Christophe Marchand, Michael Schroda^¶, Stéphane D. Lemaire¹, and Paulette Decottignies

From the Institut de Biotechnologie des Plantes, UMR 8618, Bâtiment 630, and the Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR 8619, CNRS/University of Paris-Sud 11, Orsay F-91405 cedex, France and the ^¶Institute of Biology II, Plant Biochemistry, University of Freiburg, Freiburg D-79104, Germany

Glutathionylation is the major form of S-thiolation in cells. This reversible redox post-translational modification consists of the formation of a mixed disulfide between a free thiol on a protein and a molecule of glutathione. This recently described modification, which is considered to occur under oxidative stress, can protect cysteine residues from irreversible oxidation, and alter positively or negatively the activity of diverse proteins. This modification and its targets have been mainly studied in non-photosynthetic organisms so far. We report here the first proteomic approach performed in vivo on photosynthetically competent cells, using the eukaryotic unicellular green alga Chlamydomonas reinhardtii with radiolabeled [³⁵S]cysteine to label the glutathione pool and diamide as oxidant. This method allowed the identification of 25 targets, mainly chloroplastic, involved in various metabolic processes. Several targets are related to photosynthesis, such as the Calvin cycle enzymes phosphoglycerate kinase and ribose-5-phosphate isomerase. A number of targets, such as chaperones and peroxiredoxins, are related to stress responses. The glutathionylation of HSP70B, chloroplastic 2-Cys peroxiredoxin and isocitrate lyase was confirmed in vitro on purified proteins and the targeted residues were identified.

Received for publication, March 25, 2008 , and in revised form, May 14, 2008.

^* This work was supported by the Agence Nationale de la Recherche (Grant JC-45751) and CNRS (Programme Protéomique et Génie des Protéines). 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 Fig. S1.

¹ To whom correspondence should be addressed: Tel.: 33-1-69-15-33-38; Fax: 33-1-69-15-34-23; E-mail: stephane.lemaire{at}u-psud.fr.

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