Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts

Thioredoxins (Trxs) are small, ubiquitous enzymes that catalyze disulphide–dithiol interchange in target enzymes. The large set of chloroplast Trxs, including f, m, x and y subtypes, use reducing equivalents fueled by photoreduced ferredoxin (Fdx) for fine-tuning photosynthetic performance and metab...

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Autores: Jurado Flores, Ana, Delgado Requerey, Victor, Gálvez Ramírez, Alicia, Puerto Galán, Leonor, Pérez Ruiz, Juan Manuel, Cejudo Fernández, Francisco Javier
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/102731
Acceso en línea:https://hdl.handle.net/11441/102731
https://doi.org/10.3390/antiox9111072
Access Level:acceso abierto
Palabra clave:2-Cys peroxiredoxin
Thioredoxin y
NTRC
Thioredoxin x
Redox regulation
Stress response
Photosynthesis
Chloroplast
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spelling Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis ChloroplastsJurado Flores, AnaDelgado Requerey, VictorGálvez Ramírez, AliciaPuerto Galán, LeonorPérez Ruiz, Juan ManuelCejudo Fernández, Francisco Javier2-Cys peroxiredoxinThioredoxin yNTRCThioredoxin xRedox regulationStress responsePhotosynthesisChloroplastThioredoxins (Trxs) are small, ubiquitous enzymes that catalyze disulphide–dithiol interchange in target enzymes. The large set of chloroplast Trxs, including f, m, x and y subtypes, use reducing equivalents fueled by photoreduced ferredoxin (Fdx) for fine-tuning photosynthetic performance and metabolism through the control of the activity of redox-sensitive proteins. Although biochemical analyses suggested functional diversity of chloroplast Trxs, genetic studies have established that deficiency in a particular Trx subtype has subtle phenotypic e ects, leading to the proposal that the Trx isoforms are functionally redundant. In addition, chloroplasts contain an NADPH-dependent Trx reductase with a joint Trx domain, termed NTRC. Interestingly, Arabidopsis mutants combining the deficiencies of x- or f-type Trxs and NTRC display very severe growth inhibition phenotypes, which are partially rescued by decreased levels of 2-Cys peroxiredoxins (Prxs). These findings indicate that the reducing capacity of Trxs f and x is modulated by the redox balance of 2-Cys Prxs, which is controlled by NTRC. In this study, we explored whether NTRC acts as a master regulator of the pool of chloroplast Trxs by analyzing its functional relationship with Trxs y. While Trx y interacts with 2-Cys Prxs in vitro and in planta, the analysis of Arabidopsis mutants devoid of NTRC and Trxs y suggests that Trxs y have only a minor e ect, if any, on the redox state of 2-Cys Prxs.MDPIBioquímica Vegetal y Biología Molecular2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/102731https://doi.org/10.3390/antiox9111072reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésAntioxidants, 9 (11), 1-18.https://doi.org/10.3390/antiox9111072info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1027312026-06-17T12:51:07Z
dc.title.none.fl_str_mv Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
title Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
spellingShingle Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
Jurado Flores, Ana
2-Cys peroxiredoxin
Thioredoxin y
NTRC
Thioredoxin x
Redox regulation
Stress response
Photosynthesis
Chloroplast
title_short Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
title_full Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
title_fullStr Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
title_full_unstemmed Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
title_sort Exploring the Functional Relationship between y-Type Thioredoxins and 2-Cys Peroxiredoxins in Arabidopsis Chloroplasts
dc.creator.none.fl_str_mv Jurado Flores, Ana
Delgado Requerey, Victor
Gálvez Ramírez, Alicia
Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Cejudo Fernández, Francisco Javier
author Jurado Flores, Ana
author_facet Jurado Flores, Ana
Delgado Requerey, Victor
Gálvez Ramírez, Alicia
Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Cejudo Fernández, Francisco Javier
author_role author
author2 Delgado Requerey, Victor
Gálvez Ramírez, Alicia
Puerto Galán, Leonor
Pérez Ruiz, Juan Manuel
Cejudo Fernández, Francisco Javier
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
dc.subject.none.fl_str_mv 2-Cys peroxiredoxin
Thioredoxin y
NTRC
Thioredoxin x
Redox regulation
Stress response
Photosynthesis
Chloroplast
topic 2-Cys peroxiredoxin
Thioredoxin y
NTRC
Thioredoxin x
Redox regulation
Stress response
Photosynthesis
Chloroplast
description Thioredoxins (Trxs) are small, ubiquitous enzymes that catalyze disulphide–dithiol interchange in target enzymes. The large set of chloroplast Trxs, including f, m, x and y subtypes, use reducing equivalents fueled by photoreduced ferredoxin (Fdx) for fine-tuning photosynthetic performance and metabolism through the control of the activity of redox-sensitive proteins. Although biochemical analyses suggested functional diversity of chloroplast Trxs, genetic studies have established that deficiency in a particular Trx subtype has subtle phenotypic e ects, leading to the proposal that the Trx isoforms are functionally redundant. In addition, chloroplasts contain an NADPH-dependent Trx reductase with a joint Trx domain, termed NTRC. Interestingly, Arabidopsis mutants combining the deficiencies of x- or f-type Trxs and NTRC display very severe growth inhibition phenotypes, which are partially rescued by decreased levels of 2-Cys peroxiredoxins (Prxs). These findings indicate that the reducing capacity of Trxs f and x is modulated by the redox balance of 2-Cys Prxs, which is controlled by NTRC. In this study, we explored whether NTRC acts as a master regulator of the pool of chloroplast Trxs by analyzing its functional relationship with Trxs y. While Trx y interacts with 2-Cys Prxs in vitro and in planta, the analysis of Arabidopsis mutants devoid of NTRC and Trxs y suggests that Trxs y have only a minor e ect, if any, on the redox state of 2-Cys Prxs.
publishDate 2020
dc.date.none.fl_str_mv 2020
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/11441/102731
https://doi.org/10.3390/antiox9111072
url https://hdl.handle.net/11441/102731
https://doi.org/10.3390/antiox9111072
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Antioxidants, 9 (11), 1-18.
https://doi.org/10.3390/antiox9111072
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 MDPI
publisher.none.fl_str_mv MDPI
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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