The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation

Thiol-based redox post-translational modifications have emerged as important mechanisms of signaling and regulation in all organisms, and thioredoxin plays a key role by controlling the thiol-disulfide status of target proteins. Recent redox proteomic studies revealed hundreds of proteins regulated...

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Autores: Pérez Pérez, María Esther, Mauriès, Adeline, Maes, Alexandre, Tourasse, Nicolas J., Hamon, Marion, Lemaire, Stéphane D., Marchand, Christophe H.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/102285
Acceso en línea:https://hdl.handle.net/11441/102285
https://doi.org/10.1016/j.molp.2017.07.009
Access Level:acceso abierto
Palabra clave:Chlamydomonas reinhardtii
Disulfide bond
Isotope-coded affinity tag
Redox proteomics
Redox regulation
Thioredoxin targets
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spelling The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox RegulationPérez Pérez, María EstherMauriès, AdelineMaes, AlexandreTourasse, Nicolas J.Hamon, MarionLemaire, Stéphane D.Marchand, Christophe H.Chlamydomonas reinhardtiiDisulfide bondIsotope-coded affinity tagRedox proteomicsRedox regulationThioredoxin targetsThiol-based redox post-translational modifications have emerged as important mechanisms of signaling and regulation in all organisms, and thioredoxin plays a key role by controlling the thiol-disulfide status of target proteins. Recent redox proteomic studies revealed hundreds of proteins regulated by glutathionylation and nitrosylation in the unicellular green alga Chlamydomonas reinhardtii, while much less is known about the thioredoxin interactome in this organism. By combining qualitative and quantitative proteomic analyses, we have comprehensively investigated the Chlamydomonas thioredoxome and 1188 targets have been identified. They participate in a wide range of metabolic pathways and cellular processes. This study broadens not only the redox regulation to new enzymes involved in well-known thioredoxin-regulated metabolic pathways but also sheds light on cellular processes for which data supporting redox regulation are scarce (aromatic amino acid biosynthesis, nuclear transport, etc). Moreover, we characterized 1052 thioredoxin-dependent regulatory sites and showed that these data constitute a valuable resource for future functional studies in Chlamydomonas. By comparing this thioredoxome with proteomic data for glutathionylation and nitrosylation at the protein and cysteine levels, this work confirms the existence of a complex redox regulation network in Chlamydomonas and provides evidence of a tremendous selectivity of redox post-translational modifications for specific cysteine residues.Fondation pour la Recherche Medicale DBI2014231801Agence Nationale de la Recherche 12-BSV5-0019 REDPRO2Elsevier2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/102285https://doi.org/10.1016/j.molp.2017.07.009reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésMolecular Plant, 10 (8), 1107-1125.DBI201423180112-BSV5-0019 REDPRO2https://doi.org/10.1016/j.molp.2017.07.009info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1022852026-06-17T12:51:07Z
dc.title.none.fl_str_mv The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
title The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
spellingShingle The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
Pérez Pérez, María Esther
Chlamydomonas reinhardtii
Disulfide bond
Isotope-coded affinity tag
Redox proteomics
Redox regulation
Thioredoxin targets
title_short The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
title_full The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
title_fullStr The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
title_full_unstemmed The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
title_sort The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation
dc.creator.none.fl_str_mv Pérez Pérez, María Esther
Mauriès, Adeline
Maes, Alexandre
Tourasse, Nicolas J.
Hamon, Marion
Lemaire, Stéphane D.
Marchand, Christophe H.
author Pérez Pérez, María Esther
author_facet Pérez Pérez, María Esther
Mauriès, Adeline
Maes, Alexandre
Tourasse, Nicolas J.
Hamon, Marion
Lemaire, Stéphane D.
Marchand, Christophe H.
author_role author
author2 Mauriès, Adeline
Maes, Alexandre
Tourasse, Nicolas J.
Hamon, Marion
Lemaire, Stéphane D.
Marchand, Christophe H.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Chlamydomonas reinhardtii
Disulfide bond
Isotope-coded affinity tag
Redox proteomics
Redox regulation
Thioredoxin targets
topic Chlamydomonas reinhardtii
Disulfide bond
Isotope-coded affinity tag
Redox proteomics
Redox regulation
Thioredoxin targets
description Thiol-based redox post-translational modifications have emerged as important mechanisms of signaling and regulation in all organisms, and thioredoxin plays a key role by controlling the thiol-disulfide status of target proteins. Recent redox proteomic studies revealed hundreds of proteins regulated by glutathionylation and nitrosylation in the unicellular green alga Chlamydomonas reinhardtii, while much less is known about the thioredoxin interactome in this organism. By combining qualitative and quantitative proteomic analyses, we have comprehensively investigated the Chlamydomonas thioredoxome and 1188 targets have been identified. They participate in a wide range of metabolic pathways and cellular processes. This study broadens not only the redox regulation to new enzymes involved in well-known thioredoxin-regulated metabolic pathways but also sheds light on cellular processes for which data supporting redox regulation are scarce (aromatic amino acid biosynthesis, nuclear transport, etc). Moreover, we characterized 1052 thioredoxin-dependent regulatory sites and showed that these data constitute a valuable resource for future functional studies in Chlamydomonas. By comparing this thioredoxome with proteomic data for glutathionylation and nitrosylation at the protein and cysteine levels, this work confirms the existence of a complex redox regulation network in Chlamydomonas and provides evidence of a tremendous selectivity of redox post-translational modifications for specific cysteine residues.
publishDate 2017
dc.date.none.fl_str_mv 2017
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/11441/102285
https://doi.org/10.1016/j.molp.2017.07.009
url https://hdl.handle.net/11441/102285
https://doi.org/10.1016/j.molp.2017.07.009
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Molecular Plant, 10 (8), 1107-1125.
DBI2014231801
12-BSV5-0019 REDPRO2
https://doi.org/10.1016/j.molp.2017.07.009
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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