Project : PXD000569



S-nitrosylation in Chlamydomonas reinhardtii


Protein S-nitrosylation, a post-translational modification consisting in the covalent binding of nitric oxide (NO) to a cysteine thiol moiety, plays a major role in cell signaling and is recognized to be involved in numerous physiological processes and diseases in mammals. The importance of nitrosylation in photosynthetic eukaryotes has been less studied. The aim of this study was to expand our knowledge on protein nitrosylation by performing a large scale proteomic analysis of proteins undergoing nitrosylation in vivo in Chlamydomonas reinhardtii cells under nitrosative stress. Using two complementary proteomic approaches, 492 nitrosylated proteins were identified. They participate in a wide range of biological processes and pathways including photosynthesis, carbohydrate metabolism, amino acid metabolism, translation, protein folding or degradation, cell motility and stress. Several proteins were confirmed in vitro by western blot, site-directed mutagenesis and activity measurements. Moreover, 392 sites of nitrosylation were also identified. These results strongly suggest that S-nitrosylation could constitute a major mechanism of regulation in C. reinhardtii under nitrosative stress conditions. This study constitutes the largest proteomic analysis of protein nitrosylation reported to date. The identification of 381 previously unrecognized targets of nitrosylation further extends our knowledge on the importance of this post-translational modification in photosynthetic eukaryotes.

Sample Processing Protocol

See details in reference PMID : 24328795

Data Processing Protocol

See details in reference PMID : 24328795


Christophe MARCHAND, Redox Post-Translational Modifications

Submission Date



Not available


LTQ Orbitrap Velos


Not available

Experiment Type

Bottom-up proteomics


    Morisse S, Zaffagnini M, Gao XH, Lemaire SD, Marchand CH; Insight into protein S-nitrosylation in Chlamydomonas reinhardtii., Antioxid Redox Signal, 2013 Dec 13, PubMed(s) : 24328795

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