New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation

Persulfidation, a posttranslational modification of cysteines to persulfides, is the best characterized molecular mechanism of H2S signaling. This study is focused on new functions for thioredoxins (TRXs) in plants beyond those of thiol disulfide (S–S) exchange, including the regulation of protein p...

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Autores: De Brasi-Velasco Sabrina, Aroca, Ángeles, Romero, Luis C., Gotor, Cecilia, Sevilla Valenzuela, Francisca G., Jiménez, Ana
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/386955
Acceso en línea:http://hdl.handle.net/10261/386955
Access Level:acceso abierto
Palabra clave:Ascorbate peroxidase
Dehydroascorbate reductase
Monodehydroascorbate reductase
Persulfidation
Redox regulation
Thioredoxin o1
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network_name_str España
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dc.title.none.fl_str_mv New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
title New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
spellingShingle New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
De Brasi-Velasco Sabrina
Ascorbate peroxidase
Dehydroascorbate reductase
Monodehydroascorbate reductase
Persulfidation
Redox regulation
Thioredoxin o1
title_short New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
title_full New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
title_fullStr New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
title_full_unstemmed New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
title_sort New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidation
dc.creator.none.fl_str_mv De Brasi-Velasco Sabrina
Aroca, Ángeles
Romero, Luis C.
Gotor, Cecilia
Sevilla Valenzuela, Francisca G.
Jiménez, Ana
author De Brasi-Velasco Sabrina
author_facet De Brasi-Velasco Sabrina
Aroca, Ángeles
Romero, Luis C.
Gotor, Cecilia
Sevilla Valenzuela, Francisca G.
Jiménez, Ana
author_role author
author2 Aroca, Ángeles
Romero, Luis C.
Gotor, Cecilia
Sevilla Valenzuela, Francisca G.
Jiménez, Ana
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Agencia Estatal de Investigación (España)
Ministerio de Ciencia e Innovación (España)
European Commission
Gobierno de la Región de Murcia
Junta de Andalucía
Aroca, Ángeles [0000-0003-4915-170X]
Romero, Luis C. [0000-0002-2414-4813]
Gotor, Cecilia [0000-0003-4272-7446]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Ascorbate peroxidase
Dehydroascorbate reductase
Monodehydroascorbate reductase
Persulfidation
Redox regulation
Thioredoxin o1
topic Ascorbate peroxidase
Dehydroascorbate reductase
Monodehydroascorbate reductase
Persulfidation
Redox regulation
Thioredoxin o1
description Persulfidation, a posttranslational modification of cysteines to persulfides, is the best characterized molecular mechanism of H2S signaling. This study is focused on new functions for thioredoxins (TRXs) in plants beyond those of thiol disulfide (S–S) exchange, including the regulation of protein persulfidation as it has been described in animal systems. To elucidate the impact of TRXo1 deficiency on the protein persulfidation pattern in plants of Arabidopsis thaliana L. wild type (WT) and two Attrxo1 T-DNA insertion mutants grown under non stress conditions, a quantitative proteomic approach was performed. The proteomic analysis revealed a higher number of proteins that were more persulfidated in the mutants compared to WT plants, suggesting a role for TRXo1 in protein depersulfidation. Interestingly, most of the differentially persulfidated proteins were located in the chloroplast, implying a coordination between chloroplast H2S-dependent persulfidation and mitochondrial TRXo1 depersulfidation. Among the differentially persulfidated proteins located in mitochondria, the antioxidant enzymes sAPX, DHAR1 and MDAR6 were selected for further studies. The effect of H2S-dependent persulfidation on their enzymatic activities and its reversibility by the NADPH/thioredoxin reductase (NTRB)/TRXo1 system was analyzed, as well as their persulfidation levels were quantified. Sulfide treatment brought about increases in the activity levels of the enzymes, that match with a raise on the persulfidation levels. Interestingly, both activations declining after treatment with the thioredoxin system, indicate the regulation of their persulfidation by TRXo1. These results point to a positive effect of persulfidation on the enzymatic activities and also to a new depersulfidase activity for TRXo1. All together these results give a new insight of the mechanism of elimination of –SSH groups in plants exerted by TRXo1, and the involvement of a redox regulation on the protein persulfidation.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
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status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/386955
url http://hdl.handle.net/10261/386955
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
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info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-141885NB-I00
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The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI https://doi.org/10.1016/j.redox.2025.103627
https://doi.org/10.1016/j.redox.2025.103627
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dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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instname:Consejo Superior de Investigaciones Científicas (CSIC)
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spelling New role for thioredoxins in plants: implication of TRXo1 in protein depersulfidationDe Brasi-Velasco SabrinaAroca, ÁngelesRomero, Luis C.Gotor, CeciliaSevilla Valenzuela, Francisca G.Jiménez, AnaAscorbate peroxidaseDehydroascorbate reductaseMonodehydroascorbate reductasePersulfidationRedox regulationThioredoxin o1Persulfidation, a posttranslational modification of cysteines to persulfides, is the best characterized molecular mechanism of H2S signaling. This study is focused on new functions for thioredoxins (TRXs) in plants beyond those of thiol disulfide (S–S) exchange, including the regulation of protein persulfidation as it has been described in animal systems. To elucidate the impact of TRXo1 deficiency on the protein persulfidation pattern in plants of Arabidopsis thaliana L. wild type (WT) and two Attrxo1 T-DNA insertion mutants grown under non stress conditions, a quantitative proteomic approach was performed. The proteomic analysis revealed a higher number of proteins that were more persulfidated in the mutants compared to WT plants, suggesting a role for TRXo1 in protein depersulfidation. Interestingly, most of the differentially persulfidated proteins were located in the chloroplast, implying a coordination between chloroplast H2S-dependent persulfidation and mitochondrial TRXo1 depersulfidation. Among the differentially persulfidated proteins located in mitochondria, the antioxidant enzymes sAPX, DHAR1 and MDAR6 were selected for further studies. The effect of H2S-dependent persulfidation on their enzymatic activities and its reversibility by the NADPH/thioredoxin reductase (NTRB)/TRXo1 system was analyzed, as well as their persulfidation levels were quantified. Sulfide treatment brought about increases in the activity levels of the enzymes, that match with a raise on the persulfidation levels. Interestingly, both activations declining after treatment with the thioredoxin system, indicate the regulation of their persulfidation by TRXo1. These results point to a positive effect of persulfidation on the enzymatic activities and also to a new depersulfidase activity for TRXo1. All together these results give a new insight of the mechanism of elimination of –SSH groups in plants exerted by TRXo1, and the involvement of a redox regulation on the protein persulfidation.This study was supported by the ERDF A way of making Europe and MCIN/AEI/10.13039/501100011033 (grant No. PID2021-127335NB-I00, PID2022-141885NB-I00 and Network RED2022-134072-T), NextGenerationEU/PRTR (grant No. TED2021-131443B–I00), Séneca Foundation, Región de Murcia (22051/PI/22) and Junta de Andalucía (grant No. PROYEXCEL_00177).Peer reviewedElsevierAgencia Estatal de Investigación (España)Ministerio de Ciencia e Innovación (España)European CommissionGobierno de la Región de MurciaJunta de AndalucíaAroca, Ángeles [0000-0003-4915-170X]Romero, Luis C. [0000-0002-2414-4813]Gotor, Cecilia [0000-0003-4272-7446]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/386955reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-127335NB-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-141885NB-I00info:eu-repo/grantAgreement/AEI//RED2022-134072-Tinfo:eu-repo/grantAgreement/AEI//TED2021-131443B–I00The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI https://doi.org/10.1016/j.redox.2025.103627https://doi.org/10.1016/j.redox.2025.103627Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3869552026-05-22T06:33:51Z
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