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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2015
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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. |
format | Online Article Text |
id | pubmed-4285867 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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