Dataset Information

S-nitrosylation in Chlamydomonas reinhardtii

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Chlamydomonas Reinhardtii

SUBMITTER: Christophe H. MARCHAND

PROVIDER: PXD000569 | Pride | 2013-12-19

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	BST1_Control_Band1_1215002-11.raw	Raw
	BST1_Control_Band1to5_1215002-15-06_CTRL.msf	Msf
	BST1_Control_Band1to5_1215002-15-06_CTRL.pep.xml	Pepxml
	BST1_Control_Band1to5_1215002-15-06_CTRL.prot.xml	Xml
	BST1_Control_Band2_1215002-12.raw	Raw

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Publications

Insight into protein S-nitrosylation in Chlamydomonas reinhardtii.

Morisse Samuel S Zaffagnini Mirko M Gao Xing-Huang XH Lemaire Stéphane D SD Marchand Christophe H CH

Antioxidants & redox signaling 20140306 9

<h4>Aims</h4>Protein S-nitrosylation, a post-translational modification (PTM) consisting of 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 o ...[more]

PMID: 24328795

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