The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis

Oxidizing signals mediated by the thiol-dependent peroxidase activity of 2-Cys peroxiredoxins (PRXs) plays an essential role in fine-tuning chloroplast redox balance in response to changes in light intensity, a function that depends on NADPH-dependent thioredoxin reductase C (NTRC). In addition, pla...

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Autores: Casatejada Pérez, María Azahara, Puerto Galán, Leonor, Pérez Ruiz, Juan Manuel, Cejudo Fernández, Francisco Javier
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/155671
Acceso en línea:https://hdl.handle.net/11441/155671
https://doi.org/10.1016/j.redox.2023.102731
Access Level:acceso abierto
Palabra clave:Arabidopsis
Chloroplast
Glutathione peroxidase
NTRC
Peroxiredoxin
Thioredoxin
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spelling The contribution of glutathione peroxidases to chloroplast redox homeostasis in ArabidopsisCasatejada Pérez, María AzaharaPuerto Galán, LeonorPérez Ruiz, Juan ManuelCejudo Fernández, Francisco JavierArabidopsisChloroplastGlutathione peroxidaseNTRCPeroxiredoxinThioredoxinOxidizing signals mediated by the thiol-dependent peroxidase activity of 2-Cys peroxiredoxins (PRXs) plays an essential role in fine-tuning chloroplast redox balance in response to changes in light intensity, a function that depends on NADPH-dependent thioredoxin reductase C (NTRC). In addition, plant chloroplasts are equipped with glutathione peroxidases (GPXs), thiol-dependent peroxidases that rely on thioredoxins (TRXs). Despite having a similar reaction mechanism than 2-Cys PRXs, the contribution of oxidizing signals mediated by GPXs to the chloroplast redox homeostasis remains poorly known. To address this issue, we have generated the Arabidopsis (Arabidopsis thaliana) double mutant gpx1gpx7, which is devoid of the two GPXs, 1 and 7, localized in the chloroplast. Furthermore, to analyze the functional relationship of chloroplast GPXs with the NTRC-2-Cys PRXs redox system, the 2cpab-gpx1gpx7 and ntrc-gpx1gpx7 mutants were generated. The gpx1gpx7 mutant displayed wild type-like phenotype indicating that chloroplast GPXs are dispensable for plant growth at least under standard conditions. However, the 2cpab-gpx1gpx7 showed more retarded growth than the 2cpab mutant. The simultaneous lack of 2-Cys PRXs and GPXs affected PSII performance and caused higher delay of enzyme oxidation in the dark. In contrast, the ntrc-gpx1gpx7 mutant combining the lack of NTRC and chloroplast GPXs behaved like the ntrc mutant indicating that the contribution of GPXs to chloroplast redox homeostasis is independent of NTRC. Further supporting this notion, in vitro assays showed that GPXs are not reduced by NTRC but by TRX y2. Based on these results, we propose a role for GPXs in the chloroplast redox hierarchy.Ministerio de Ciencia e Innovación PID2020-115156 GB-I00Ministerio de Universidades FPU18-03035ElsevierBioquímica Vegetal y Biología MolecularMinisterio de Ciencia e Innovación (MICIN). EspañaMinisterio de Universidades2023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/155671https://doi.org/10.1016/j.redox.2023.102731reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésRedox Biology, 63, 102731.PID2020-115156 GB-I00FPU18-03035https://doi.org/10.1016/j.redox.2023.102731info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1556712026-06-17T12:51:07Z
dc.title.none.fl_str_mv The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
title The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
spellingShingle The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
Casatejada Pérez, María Azahara
Arabidopsis
Chloroplast
Glutathione peroxidase
NTRC
Peroxiredoxin
Thioredoxin
title_short The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
title_full The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
title_fullStr The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
title_full_unstemmed The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
title_sort The contribution of glutathione peroxidases to chloroplast redox homeostasis in Arabidopsis
dc.creator.none.fl_str_mv Casatejada Pérez, María Azahara
Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Cejudo Fernández, Francisco Javier
author Casatejada Pérez, María Azahara
author_facet Casatejada Pérez, María Azahara
Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Cejudo Fernández, Francisco Javier
author_role author
author2 Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Cejudo Fernández, Francisco Javier
author2_role author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Ministerio de Ciencia e Innovación (MICIN). España
Ministerio de Universidades
dc.subject.none.fl_str_mv Arabidopsis
Chloroplast
Glutathione peroxidase
NTRC
Peroxiredoxin
Thioredoxin
topic Arabidopsis
Chloroplast
Glutathione peroxidase
NTRC
Peroxiredoxin
Thioredoxin
description Oxidizing signals mediated by the thiol-dependent peroxidase activity of 2-Cys peroxiredoxins (PRXs) plays an essential role in fine-tuning chloroplast redox balance in response to changes in light intensity, a function that depends on NADPH-dependent thioredoxin reductase C (NTRC). In addition, plant chloroplasts are equipped with glutathione peroxidases (GPXs), thiol-dependent peroxidases that rely on thioredoxins (TRXs). Despite having a similar reaction mechanism than 2-Cys PRXs, the contribution of oxidizing signals mediated by GPXs to the chloroplast redox homeostasis remains poorly known. To address this issue, we have generated the Arabidopsis (Arabidopsis thaliana) double mutant gpx1gpx7, which is devoid of the two GPXs, 1 and 7, localized in the chloroplast. Furthermore, to analyze the functional relationship of chloroplast GPXs with the NTRC-2-Cys PRXs redox system, the 2cpab-gpx1gpx7 and ntrc-gpx1gpx7 mutants were generated. The gpx1gpx7 mutant displayed wild type-like phenotype indicating that chloroplast GPXs are dispensable for plant growth at least under standard conditions. However, the 2cpab-gpx1gpx7 showed more retarded growth than the 2cpab mutant. The simultaneous lack of 2-Cys PRXs and GPXs affected PSII performance and caused higher delay of enzyme oxidation in the dark. In contrast, the ntrc-gpx1gpx7 mutant combining the lack of NTRC and chloroplast GPXs behaved like the ntrc mutant indicating that the contribution of GPXs to chloroplast redox homeostasis is independent of NTRC. Further supporting this notion, in vitro assays showed that GPXs are not reduced by NTRC but by TRX y2. Based on these results, we propose a role for GPXs in the chloroplast redox hierarchy.
publishDate 2023
dc.date.none.fl_str_mv 2023
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/11441/155671
https://doi.org/10.1016/j.redox.2023.102731
url https://hdl.handle.net/11441/155671
https://doi.org/10.1016/j.redox.2023.102731
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Redox Biology, 63, 102731.
PID2020-115156 GB-I00
FPU18-03035
https://doi.org/10.1016/j.redox.2023.102731
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 Elsevier
publisher.none.fl_str_mv Elsevier
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 15,812429

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