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Methods for Analysis of Protein Glutathionylation and their Application to Photosynthetic Organisms

Molecular Plant 2009年第2期2卷 218-235页

作者： Xing-Huang Gao Mariette Bedhomme Daniel Veyel Mirko Zaffagnini Stephane D. Lemaire Institut de Biotechnologie des Plantes UMR 8618 CNRS/Universite Paris-Sud 11 Batiment 630 Orsay 91405 Cedex France

Protein S-glutathionylation, the reversible formation of a mixed-disulfide between glutathione and protein thiols, is involved in protection of protein cysteines from irreversible oxidation, but also in protein redox regulation. Recent studies have implicated S-glutathionylation as a cellular response to oxidative/nitrosative stress, likely playing an important role in signaling. Considering the potential importance of glutathionylation, a number of methods have been developed for identifying proteins undergoing glutathionylation. These methods, ranging from analysis of purified proteins in vitro to large-scale proteomic analyses in vivo, allowed identification of nearly 200 targets in mammals. By contrast, the number of known glutathionylated proteins is more limited in photosynthetic organisms, although they are severely exposed to oxidative stress. The aim of this review is to detail the methods available for identification and analysis of glutathionylated proteins in vivo and in vitro. The advantages and drawbacks of each technique will be discussed as well as their application to photosynthetic organisms. Furthermore, an overview of known glutathionylated proteins in photosynthetic organisms is provided and the physiological importance of this post-translational modification is discussed.

关键词： environmental signals oxidative and photo-oxidative stress proteomics signal transduction Glutathionylation Methods Glutaredoxin Glutathione.

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