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Protein S-nitrosylation: specificity and identification strategies in plants

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...

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Autores principales: Lamotte, Olivier, Bertoldo, Jean B., Besson-Bard, Angélique, Rosnoblet, Claire, Aimé, Sébastien, Hichami, Siham, Terenzi, Hernán, Wendehenne, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285867/
https://www.ncbi.nlm.nih.gov/pubmed/25750911
http://dx.doi.org/10.3389/fchem.2014.00114
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author Lamotte, Olivier
Bertoldo, Jean B.
Besson-Bard, Angélique
Rosnoblet, Claire
Aimé, Sébastien
Hichami, Siham
Terenzi, Hernán
Wendehenne, David
author_facet Lamotte, Olivier
Bertoldo, Jean B.
Besson-Bard, Angélique
Rosnoblet, Claire
Aimé, Sébastien
Hichami, Siham
Terenzi, Hernán
Wendehenne, David
author_sort Lamotte, Olivier
collection PubMed
description 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.
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spelling pubmed-42858672015-03-06 Protein S-nitrosylation: specificity and identification strategies in plants Lamotte, Olivier Bertoldo, Jean B. Besson-Bard, Angélique Rosnoblet, Claire Aimé, Sébastien Hichami, Siham Terenzi, Hernán Wendehenne, David Front Chem Chemistry 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. Frontiers Media S.A. 2015-01-07 /pmc/articles/PMC4285867/ /pubmed/25750911 http://dx.doi.org/10.3389/fchem.2014.00114 Text en Copyright © 2015 Lamotte, Bertoldo, Besson-Bard, Rosnoblet, Aimé, Hichami, Terenzi and Wendehenne. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Chemistry
Lamotte, Olivier
Bertoldo, Jean B.
Besson-Bard, Angélique
Rosnoblet, Claire
Aimé, Sébastien
Hichami, Siham
Terenzi, Hernán
Wendehenne, David
Protein S-nitrosylation: specificity and identification strategies in plants
title Protein S-nitrosylation: specificity and identification strategies in plants
title_full Protein S-nitrosylation: specificity and identification strategies in plants
title_fullStr Protein S-nitrosylation: specificity and identification strategies in plants
title_full_unstemmed Protein S-nitrosylation: specificity and identification strategies in plants
title_short Protein S-nitrosylation: specificity and identification strategies in plants
title_sort protein s-nitrosylation: specificity and identification strategies in plants
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285867/
https://www.ncbi.nlm.nih.gov/pubmed/25750911
http://dx.doi.org/10.3389/fchem.2014.00114
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