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Protein tyrosine nitration in higher plants grown under natural and stress conditions

Protein tyrosine nitration is a post-translational modification (PTM) mediated by reactive nitrogen species (RNS) that is linked to nitro-oxidative damages in plant cells. During the last decade, the identification of proteins undergoing this PTM under adverse environmental conditions has increased....

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Autores principales: Corpas, Francisco J., Palma, José M., del Río, Luis A., Barroso, Juan B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3580390/
https://www.ncbi.nlm.nih.gov/pubmed/23444154
http://dx.doi.org/10.3389/fpls.2013.00029
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author Corpas, Francisco J.
Palma, José M.
del Río, Luis A.
Barroso, Juan B.
author_facet Corpas, Francisco J.
Palma, José M.
del Río, Luis A.
Barroso, Juan B.
author_sort Corpas, Francisco J.
collection PubMed
description Protein tyrosine nitration is a post-translational modification (PTM) mediated by reactive nitrogen species (RNS) that is linked to nitro-oxidative damages in plant cells. During the last decade, the identification of proteins undergoing this PTM under adverse environmental conditions has increased. However, there is also a basal endogenous nitration which seems to have a regulatory function. The technological advances in proteome analysis have allowed identifying these modified proteins and have shown that the number and identity of the nitrated proteins change among plant species, analysed organs and growing/culture conditions. In this work, the current knowledge of protein tyrosine nitration in higher plants under different situations is reviewed.
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spelling pubmed-35803902013-02-26 Protein tyrosine nitration in higher plants grown under natural and stress conditions Corpas, Francisco J. Palma, José M. del Río, Luis A. Barroso, Juan B. Front Plant Sci Plant Science Protein tyrosine nitration is a post-translational modification (PTM) mediated by reactive nitrogen species (RNS) that is linked to nitro-oxidative damages in plant cells. During the last decade, the identification of proteins undergoing this PTM under adverse environmental conditions has increased. However, there is also a basal endogenous nitration which seems to have a regulatory function. The technological advances in proteome analysis have allowed identifying these modified proteins and have shown that the number and identity of the nitrated proteins change among plant species, analysed organs and growing/culture conditions. In this work, the current knowledge of protein tyrosine nitration in higher plants under different situations is reviewed. Frontiers Media S.A. 2013-02-25 /pmc/articles/PMC3580390/ /pubmed/23444154 http://dx.doi.org/10.3389/fpls.2013.00029 Text en Copyright © 2013 Corpas, Palma, del Río and Barroso. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
spellingShingle Plant Science
Corpas, Francisco J.
Palma, José M.
del Río, Luis A.
Barroso, Juan B.
Protein tyrosine nitration in higher plants grown under natural and stress conditions
title Protein tyrosine nitration in higher plants grown under natural and stress conditions
title_full Protein tyrosine nitration in higher plants grown under natural and stress conditions
title_fullStr Protein tyrosine nitration in higher plants grown under natural and stress conditions
title_full_unstemmed Protein tyrosine nitration in higher plants grown under natural and stress conditions
title_short Protein tyrosine nitration in higher plants grown under natural and stress conditions
title_sort protein tyrosine nitration in higher plants grown under natural and stress conditions
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3580390/
https://www.ncbi.nlm.nih.gov/pubmed/23444154
http://dx.doi.org/10.3389/fpls.2013.00029
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