Protein S-nitrosylation: specificity and identification strategies in plants

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TitreProtein S-nitrosylation: specificity and identification strategies in plants
Type de publicationJournal Article
Year of Publication2015
AuteursLamotte O, Bertoldo JB, Besson-Bard A, Rosnoblet C, Aime SEB, Hichami S, Terenzi H, Wendehenne D
JournalFRONTIERS IN CHEMISTRY
Volume2
Pagination114
Date PublishedJAN 7
Type of ArticleReview
ISSN2296-2646
Mots-clésbiotin switch technique, Nitric oxide, Plants, post-translational modifications, S-nitrosylation, Signaling
Résumé

The role of nitric oxide (NO) as a major regulator of plant physiological functions has become increasingly evident. To further improve our understanding of its role, within the last few years plant biologists have begun to embrace the exciting opportunity of investigating protein S-nitrosylation, a major reversible NO-dependent post-translational modification (PTM) targeting specific Cys residues and widely studied in animals. Thanks to the development of dedicated proteomic approaches, in particular the use of the biotin switch technique (BST) combined with mass spectrometry, hundreds of plant protein candidates for S-nitrosylation have been identified. Functional studies focused on specific proteins provided preliminary comprehensive views of how this PTM impacts the structure and function of proteins and, more generally, of how NO might regulate biological plant processes. The aim of this review is to detail the basic principle of protein S-nitrosylation, to provide information on the biochemical and structural features of the S-nitrosylation sites and to describe the proteomic strategies adopted to investigate this PTM in plants. Limits of the current approaches and tomorrow's challenges are also discussed.

DOI10.3389/fchem.2014.00114