Redox proteomics reveal a role for peroxiredoxinylation in stress protection
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- dc.contributor.author Seisenbacher, Gerhard
- dc.contributor.author Nakic, Zrinka Raguz
- dc.contributor.author Borràs, Eva
- dc.contributor.author Sabidó Aguadé, Eduard, 1981-
- dc.contributor.author Sauer, Uwe
- dc.contributor.author Nadal Clanchet, Eulàlia de
- dc.contributor.author Posas Garriga, Francesc
- dc.date.accessioned 2025-02-20T13:00:37Z
- dc.date.available 2025-02-20T13:00:37Z
- dc.date.issued 2025
- dc.description.abstract The redox state of proteins is essential for their function and guarantees cell fitness. Peroxiredoxins protect cells against oxidative stress, maintain redox homeostasis, act as chaperones, and transmit hydrogen peroxide signals to redox regulators. Despite the profound structural and functional knowledge of peroxiredoxins action, information on how the different functions are concerted is still scarce. Using global proteomic analyses, we show here that the yeast peroxiredoxin Tsa1 interacts with many proteins of essential biological processes, including protein turnover and carbohydrate metabolism. Several of these interactions are of a covalent nature, and we show that failure of peroxiredoxinylation of Gnd1 affects its phosphogluconate dehydrogenase activity and impairs recovery upon stress. Thioredoxins directly remove TSA1-formed mixed disulfide intermediates, thus expanding the role of the thioredoxin-peroxiredoxin redox cycle pair to buffer the redox state of proteins.
- dc.description.sponsorship The laboratories of F.P. and E.d.N. are supported by a coordinated grant PID2021-124723NB-C21/C222 funded by MICIU/AEI/10.13039/501100011033 and ERDF/EU, and the Government of Catalonia (2017 SGR799). We gratefully acknowledge institutional funding from the Ministry of Science, Innovation, and Universities through the Centres of Excellence Severo Ochoa Award, and from the CERCA Programme of the Government of Catalonia and the Unidad de Excelencia María de Maeztu, funded by the AEI (CEX2018-000792-M). F.P. and E.d.N. are recipients of an ICREA Acadèmia award (Government of Catalonia). G.S. was supported by an Advanced Postdoc.Mobility fellowship (P300P3_147895) by the Swiss National Science Foundation.
- dc.format.mimetype application/pdf
- dc.identifier.citation Seisenbacher G, Nakic ZR, Borràs E, Sabidó E, Sauer U, de Nadal E, et al. Redox proteomics reveal a role for peroxiredoxinylation in stress protection. Cell Rep. 2025 Jan 21;44(2):115224. DOI: 10.1016/j.celrep.2024.115224
- dc.identifier.doi http://dx.doi.org/10.1016/j.celrep.2024.115224
- dc.identifier.issn 2211-1247
- dc.identifier.uri http://hdl.handle.net/10230/69654
- dc.language.iso eng
- dc.publisher Elsevier
- dc.relation.ispartof Cell Rep. 2025 Jan 21;44(2):115224
- dc.relation.projectID info:eu-repo/grantAgreement/ES/3PE/PID2021-124723NB-C21
- dc.relation.projectID info:eu-repo/grantAgreement/ES/2PE/CEX2018-000792-M
- dc.rights © 2024 The Authors. Published by Elsevier Inc. 1 This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- dc.rights.accessRights info:eu-repo/semantics/openAccess
- dc.rights.uri http://creativecommons.org/licenses/by/4.0/
- dc.subject.keyword CP: Molecular biology
- dc.subject.keyword Tsa1
- dc.subject.keyword Oxidative stress
- dc.subject.keyword Peroxiredoxins
- dc.subject.keyword Redox biology
- dc.subject.keyword Stress
- dc.title Redox proteomics reveal a role for peroxiredoxinylation in stress protection
- dc.type info:eu-repo/semantics/article
- dc.type.version info:eu-repo/semantics/publishedVersion