The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts

Hydrogen peroxide is a harmful by-product of photosynthesis, which also has important signalling activity. Therefore, the level of hydrogen peroxide needs to be tightly controlled. Chloroplasts harbour different antioxidant systems including enzymes such as the 2-Cys peroxiredoxins (2-Cys Prxs). Und...

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Autores: Puerto Galán, Leonor, Pérez Ruiz, Juan Manuel, Guinea, Manuel, Cejudo Fernández, Francisco Javier
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/58955
Acceso en línea:http://hdl.handle.net/11441/58955
https://doi.org/10.1093/jxb/eru512
Access Level:acceso abierto
Palabra clave:Arabidopsis thaliana
chloroplast, 2-Cys peroxiredoxin
overoxidation
redox regulation
sulfiredoxin
thioredoxin reductase
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spelling The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplastsPuerto Galán, LeonorPérez Ruiz, Juan ManuelGuinea, ManuelCejudo Fernández, Francisco JavierArabidopsis thalianachloroplast, 2-Cys peroxiredoxinoveroxidationredox regulationsulfiredoxinthioredoxin reductaseHydrogen peroxide is a harmful by-product of photosynthesis, which also has important signalling activity. Therefore, the level of hydrogen peroxide needs to be tightly controlled. Chloroplasts harbour different antioxidant systems including enzymes such as the 2-Cys peroxiredoxins (2-Cys Prxs). Under oxidizing conditions, 2-Cys Prxs are susceptible to inactivation by overoxidation of their peroxidatic cysteine, which is enzymatically reverted by sulfiredoxin (Srx). In chloroplasts, the redox status of 2-Cys Prxs is highly dependent on NADPH-thioredoxin reductase C (NTRC) and Srx; however, the relationship of these activities in determining the level of 2-Cys Prx overoxidation is unknown. Here we have addressed this question by a combination of genetic and biochemical approaches. An Arabidopsis thaliana double knockout mutant lacking NTRC and Srx shows a phenotype similar to the ntrc mutant, while the srx mutant resembles wild-type plants. The deficiency of NTRC causes reduced overoxidation of 2-Cys Prxs, whereas the deficiency of Srx has the opposite effect. Moreover, in vitro analyses show that the disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation, thus explaining the dominant role of NTRC on the level of 2-Cys Prx overoxidation in vivo. The overoxidation of chloroplast 2-Cys Prxs shows no circadian oscillation, in agreement with the fact that neither the NTRC nor the SRX genes show circadian regulation of expression. Additionally, the low level of 2-Cys Prx overoxidation in the ntrc mutant is light dependent, suggesting that the redox status of 2-Cys Prxs in chloroplasts depends on light rather than the circadian clock.España, Ministerio de Economía y Competitividad BIO2013-43556-PEspaña, Junta de Andalucía BIO-182España, Junta de Andalucía CVI-5919Oxford University PressBioquímica Vegetal y Biología Molecular2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/11441/58955https://doi.org/10.1093/jxb/eru512reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésJournal of Experimental Botany, 66 (10), 2957-2966.info:eu-repo/grantAgreement/MINECO/BIO2013-43556-P/BIO-182CVI-5919http://dx.doi.org/10.1093/jxb/eru512info:eu-repo/semantics/openAccessoai:idus.us.es:11441/589552026-06-17T12:51:07Z
dc.title.none.fl_str_mv The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
title The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
spellingShingle The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
Puerto Galán, Leonor
Arabidopsis thaliana
chloroplast, 2-Cys peroxiredoxin
overoxidation
redox regulation
sulfiredoxin
thioredoxin reductase
title_short The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
title_full The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
title_fullStr The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
title_full_unstemmed The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
title_sort The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
dc.creator.none.fl_str_mv Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Guinea, Manuel
Cejudo Fernández, Francisco Javier
author Puerto Galán, Leonor
author_facet Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Guinea, Manuel
Cejudo Fernández, Francisco Javier
author_role author
author2 Pérez Ruiz, Juan Manuel
Guinea, Manuel
Cejudo Fernández, Francisco Javier
author2_role author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
dc.subject.none.fl_str_mv Arabidopsis thaliana
chloroplast, 2-Cys peroxiredoxin
overoxidation
redox regulation
sulfiredoxin
thioredoxin reductase
topic Arabidopsis thaliana
chloroplast, 2-Cys peroxiredoxin
overoxidation
redox regulation
sulfiredoxin
thioredoxin reductase
description Hydrogen peroxide is a harmful by-product of photosynthesis, which also has important signalling activity. Therefore, the level of hydrogen peroxide needs to be tightly controlled. Chloroplasts harbour different antioxidant systems including enzymes such as the 2-Cys peroxiredoxins (2-Cys Prxs). Under oxidizing conditions, 2-Cys Prxs are susceptible to inactivation by overoxidation of their peroxidatic cysteine, which is enzymatically reverted by sulfiredoxin (Srx). In chloroplasts, the redox status of 2-Cys Prxs is highly dependent on NADPH-thioredoxin reductase C (NTRC) and Srx; however, the relationship of these activities in determining the level of 2-Cys Prx overoxidation is unknown. Here we have addressed this question by a combination of genetic and biochemical approaches. An Arabidopsis thaliana double knockout mutant lacking NTRC and Srx shows a phenotype similar to the ntrc mutant, while the srx mutant resembles wild-type plants. The deficiency of NTRC causes reduced overoxidation of 2-Cys Prxs, whereas the deficiency of Srx has the opposite effect. Moreover, in vitro analyses show that the disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation, thus explaining the dominant role of NTRC on the level of 2-Cys Prx overoxidation in vivo. The overoxidation of chloroplast 2-Cys Prxs shows no circadian oscillation, in agreement with the fact that neither the NTRC nor the SRX genes show circadian regulation of expression. Additionally, the low level of 2-Cys Prx overoxidation in the ntrc mutant is light dependent, suggesting that the redox status of 2-Cys Prxs in chloroplasts depends on light rather than the circadian clock.
publishDate 2015
dc.date.none.fl_str_mv 2015
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 http://hdl.handle.net/11441/58955
https://doi.org/10.1093/jxb/eru512
url http://hdl.handle.net/11441/58955
https://doi.org/10.1093/jxb/eru512
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Journal of Experimental Botany, 66 (10), 2957-2966.
info:eu-repo/grantAgreement/MINECO/BIO2013-43556-P/
BIO-182
CVI-5919
http://dx.doi.org/10.1093/jxb/eru512
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,301603

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