Is oxidized thioredoxin a major trigger for cysteine oxidation? Clues from a redox proteomics approach
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- dc.contributor.author García Santamarina, Sarela, 1978-ca
- dc.contributor.author Boronat i Llop, Susanna, 1965-ca
- dc.contributor.author Calvo, Isabel A.ca
- dc.contributor.author Rodríguez Gabriel, Miguelca
- dc.contributor.author Ayté del Olmo, Joséca
- dc.contributor.author Molina, Henrikca
- dc.contributor.author Hidalgo Hernando, Elenaca
- dc.date.accessioned 2016-01-14T15:21:54Z
- dc.date.available 2016-01-14T15:21:54Z
- dc.date.issued 2013
- dc.description.abstract Cysteine oxidation mediates oxidative stress toxicity and signaling. It has been long proposed that the thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (Trr), is not only involved in recycling classical Trx substrates, such as ribonucleotide reductase, but it also regulates general cytoplasmic thiol homeostasis. To investigate such a role, we have performed a proteome-wide analysis of cells expressing or not the two components of the Trx system. We have compared the reversibly oxidized thiol proteomes of wild-type Schizosaccharomyces pombe cells with mutants lacking Trx or Trr. Specific Trx substrates are reversibly-oxidized in both strain backgrounds; however, in the absence of Trr, Trx can weakly recycle its substrates at the expense of an alternative electron donor. A massive thiol oxidation occurs only in cells lacking Trr, with 30% of all cysteine-containing peptides being reversibly oxidized; this oxidized cysteine proteome depends on the presence of Trxs. Our observations lead to the hypothesis that, in the absence of its reductase, the natural electron donor Trx becomes a powerful oxidant and triggers general thiol oxidation.ca
- dc.description.sponsorship This work was supported by the Spanish Ministry of Science and Innovation (BFU2009-06933 and BFU2012-32045), PLAN E and FEDER, by the Spanish program Consolider-Ingenio 2010 Grant CSD 2007-0020, and by SGR2009-196 from Generalitat de Catalunya (Spain) to E.H. E. H. and J.A. are recipients of ICREA Academia Awards (Generalitat de Catalunya).
- dc.format.mimetype application/pdfca
- dc.identifier.citation García-Santamarina S, Boronat S, Calvo IA, Rodríguez-Gabriel M, Ayté J, Molina H et al. Is oxidized thioredoxin a major trigger for cysteine oxidation? Clues from a redox proteomics approach. Antioxid Redox Signal. 2013;18(13):1549-56. DOI: 10.1089/ars.2012.5037ca
- dc.identifier.doi http://dx.doi.org/10.1089/ars.2012.5037
- dc.identifier.issn 1523-0864
- dc.identifier.uri http://hdl.handle.net/10230/25577
- dc.language.iso engca
- dc.publisher Mary Ann Liebert, Incca
- dc.relation.ispartof Antioxidants & redox signaling. 2013;18(13):1549-56
- dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BFU2009-06933
- dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BFU2012-32045
- dc.relation.projectID info:eu-repo/grantAgreement/ES/2PN/CSD2007-0020
- dc.rights This is a copy of an article published in the Antioxidants & redox signaling © 2013 copyright Mary Ann Liebert, Inc.; Antioxidants & redox signaling is available online at: http://www.liebertonline.com.ca
- dc.rights.accessRights info:eu-repo/semantics/openAccessca
- dc.subject.other Reacció d'oxidació-reduccióca
- dc.subject.other Glicoproteïnesca
- dc.title Is oxidized thioredoxin a major trigger for cysteine oxidation? Clues from a redox proteomics approachca
- dc.type info:eu-repo/semantics/articleca
- dc.type.version info:eu-repo/semantics/acceptedVersionca