Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation

Post-translational modifications (PTMs) mediated by nitric oxide (NO)-derived molecules have become a new area of research, as they can modulate the function of target proteins. Proteomic data have shown that ascorbate peroxidase (APX) is one of the potential targets of PTMs mediated by NO-derived m...

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Autores: Begara-Morales, Juan Carlos, Sanchez-Calvo, Beatriz, Chaki, Mounira, Valderrama, Raquel, Mata-Pérez, Capilla, López-Jaramillo, Jaime, Padilla-Serrano, María Nieves, Carreras, Alfonso, Corpas, Francisco Javier, Barroso-Albarracín, Juan Bautista
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:España
Institución:Universidad de Jaén
Repositorio:RUJA. Repositorio Institucional de la Producción Científica de la Universidad de Jaén
OAI Identifier:oai:ruja.ujaen.es:10953/4125
Acceso en línea:https://hdl.handle.net/10953/4125
Access Level:acceso abierto
Palabra clave:Ascorbate peroxidase
Nitration
Nitric oxide
S-nitrosoglutathione
S-nitrosylation
Peroxynitrite
Reactive nitrogen species
Salinity stress
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repository_id_str
spelling Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylationBegara-Morales, Juan CarlosSanchez-Calvo, BeatrizChaki, MouniraValderrama, RaquelMata-Pérez, CapillaLópez-Jaramillo, JaimePadilla-Serrano, María NievesCarreras, AlfonsoCorpas, Francisco JavierBarroso-Albarracín, Juan BautistaAscorbate peroxidaseNitrationNitric oxideS-nitrosoglutathioneS-nitrosylationPeroxynitriteReactive nitrogen speciesSalinity stressPost-translational modifications (PTMs) mediated by nitric oxide (NO)-derived molecules have become a new area of research, as they can modulate the function of target proteins. Proteomic data have shown that ascorbate peroxidase (APX) is one of the potential targets of PTMs mediated by NO-derived molecules. Using recombinant pea cytosolic APX, the impact of peroxynitrite (ONOO–) and S-nitrosoglutathione (GSNO), which are known to mediate protein nitration and S-nitrosylation processes, respectively, was analysed. While peroxynitrite inhibits APX activity, GSNO enhances its enzymatic activity. Mass spectrometric analysis of the nitrated APX enabled the determination that Tyr5 and Tyr235 were exclusively nitrated to 3-nitrotyrosine by peroxynitrite. Residue Cys32 was identified by the biotin switch method as S-nitrosylated. The location of these residues on the structure of pea APX reveals that Tyr235 is found at the bottom of the pocket where the haem group is enclosed, whereas Cys32 is at the ascorbate binding site. Pea plants grown under saline (150 mM NaCl) stress showed an enhancement of both APX activity and S-nitrosylated APX, as well as an increase of H₂O₂, NO, and S-nitrosothiol (SNO) content that can justify the induction of the APX activity. The results provide new insight into the molecular mechanism of the regulation of APX which can be both inactivated by irreversible nitration and activated by reversible S-nitrosylation.JBM acknowledges a PhD fellowship (F.P.U.) from the Ministry of Science and Innovation. This work was supported by an ERDF-co-financed grant from the Ministry of Science and Innovation (BIO2009-12003-C02-01, BIO2009-12003-C02-02, and BIO2012-33904) and Junta de Andalucía (groups BIO286 and BIO192), Spain.OXFORD UNIV PRESS202520252014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/10953/4125reponame:RUJA. Repositorio Institucional de la Producción Científica de la Universidad de Jaéninstname:Universidad de JaénInglésJournal of Experimental Botany [2014]; [65 (2)]: [527-538]info:eu-repo/semantics/openAccessoai:ruja.ujaen.es:10953/41252026-06-24T12:41:07Z
dc.title.none.fl_str_mv Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
title Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
spellingShingle Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
Begara-Morales, Juan Carlos
Ascorbate peroxidase
Nitration
Nitric oxide
S-nitrosoglutathione
S-nitrosylation
Peroxynitrite
Reactive nitrogen species
Salinity stress
title_short Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
title_full Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
title_fullStr Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
title_full_unstemmed Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
title_sort Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
dc.creator.none.fl_str_mv Begara-Morales, Juan Carlos
Sanchez-Calvo, Beatriz
Chaki, Mounira
Valderrama, Raquel
Mata-Pérez, Capilla
López-Jaramillo, Jaime
Padilla-Serrano, María Nieves
Carreras, Alfonso
Corpas, Francisco Javier
Barroso-Albarracín, Juan Bautista
author Begara-Morales, Juan Carlos
author_facet Begara-Morales, Juan Carlos
Sanchez-Calvo, Beatriz
Chaki, Mounira
Valderrama, Raquel
Mata-Pérez, Capilla
López-Jaramillo, Jaime
Padilla-Serrano, María Nieves
Carreras, Alfonso
Corpas, Francisco Javier
Barroso-Albarracín, Juan Bautista
author_role author
author2 Sanchez-Calvo, Beatriz
Chaki, Mounira
Valderrama, Raquel
Mata-Pérez, Capilla
López-Jaramillo, Jaime
Padilla-Serrano, María Nieves
Carreras, Alfonso
Corpas, Francisco Javier
Barroso-Albarracín, Juan Bautista
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ascorbate peroxidase
Nitration
Nitric oxide
S-nitrosoglutathione
S-nitrosylation
Peroxynitrite
Reactive nitrogen species
Salinity stress
topic Ascorbate peroxidase
Nitration
Nitric oxide
S-nitrosoglutathione
S-nitrosylation
Peroxynitrite
Reactive nitrogen species
Salinity stress
description Post-translational modifications (PTMs) mediated by nitric oxide (NO)-derived molecules have become a new area of research, as they can modulate the function of target proteins. Proteomic data have shown that ascorbate peroxidase (APX) is one of the potential targets of PTMs mediated by NO-derived molecules. Using recombinant pea cytosolic APX, the impact of peroxynitrite (ONOO–) and S-nitrosoglutathione (GSNO), which are known to mediate protein nitration and S-nitrosylation processes, respectively, was analysed. While peroxynitrite inhibits APX activity, GSNO enhances its enzymatic activity. Mass spectrometric analysis of the nitrated APX enabled the determination that Tyr5 and Tyr235 were exclusively nitrated to 3-nitrotyrosine by peroxynitrite. Residue Cys32 was identified by the biotin switch method as S-nitrosylated. The location of these residues on the structure of pea APX reveals that Tyr235 is found at the bottom of the pocket where the haem group is enclosed, whereas Cys32 is at the ascorbate binding site. Pea plants grown under saline (150 mM NaCl) stress showed an enhancement of both APX activity and S-nitrosylated APX, as well as an increase of H₂O₂, NO, and S-nitrosothiol (SNO) content that can justify the induction of the APX activity. The results provide new insight into the molecular mechanism of the regulation of APX which can be both inactivated by irreversible nitration and activated by reversible S-nitrosylation.
publishDate 2014
dc.date.none.fl_str_mv 2014
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/10953/4125
url https://hdl.handle.net/10953/4125
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Journal of Experimental Botany [2014]; [65 (2)]: [527-538]
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv OXFORD UNIV PRESS
publisher.none.fl_str_mv OXFORD UNIV PRESS
dc.source.none.fl_str_mv reponame:RUJA. Repositorio Institucional de la Producción Científica de la Universidad de Jaén
instname:Universidad de Jaén
instname_str Universidad de Jaén
reponame_str RUJA. Repositorio Institucional de la Producción Científica de la Universidad de Jaén
collection RUJA. Repositorio Institucional de la Producción Científica de la Universidad de Jaén
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,198674

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