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Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin

2010-12Journal article Open access
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dc.contributor.authorZito, Ester
dc.contributor.authorMelo, Eduardo
dc.contributor.authorYang, Yun
dc.contributor.authorWahlander, Asa
dc.contributor.authorNeubert, Thomas A.
dc.contributor.authorRon, David
dc.date.accessioned2018-12-07T14:52:53Z
dc.date.available2018-12-07T14:52:53Z
dc.date.issued2010-12
dc.description.abstractEndoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative protein folding in simple eukaryotes such as yeast and worms. Surprisingly, ERO1-deficient mammalian cells exhibit only a modest delay in disulfide bond formation. To identify ERO1-independent pathways to disulfide bond formation, we purified PDI oxidants with a trapping mutant of PDI. Peroxiredoxin IV (PRDX4) stood out in this list, as the related cytosolic peroxiredoxins are known to form disulfides in the presence of hydroperoxides. Mouse embryo fibroblasts lacking ERO1 were intolerant of PRDX4 knockdown. Introduction of wild-type mammalian PRDX4 into the ER rescued the temperature-sensitive phenotype of an ero1 yeast mutation. In the presence of an H2O2-generating system, purified PRDX4 oxidized PDI and reconstituted oxidative folding of RNase A. These observations implicate ER-localized PRDX4 in a previously unanticipated, parallel, ERO1-independent pathway that couples hydroperoxide production to oxidative protein folding in mammalian cells.
dc.description.sponsorshipEMBO [ALTF649-2008]; Fundacao para a Ciencia e Tecnologia, Portugal [SFRH/BSAB/922/2009, PTDC/QUI/73027/2006, IBB/CBME LA]; NIH [DK47119, DK075311, ES08681]; 100 Women In Hedge Funds Foundation; [NS050276]; [CA016087]; Medical Research Council [G0600717B]
dc.description.sponsorshipIBB/CBME LA
dc.description.versioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doihttps://doi.org/10.1016/j.molcel.2010.11.010
dc.identifier.issn1097-2765
dc.identifier.urihttp://hdl.handle.net/10400.1/11253
dc.language.isoeng
dc.peerreviewedyes
dc.publisherCell Press
dc.relationSingle-Molecule Detection of the Prion Protein: Characterization of Conformational Change Involved on Prion Diseases
dc.rights.uriinfo:eu-repo/semantics/publishedVersion
dc.subjectDisulfide bond formation
dc.subjectThiol oxidase
dc.subjectRedox state
dc.subjectHuman cells
dc.subjectStress
dc.subjectGene
dc.subjectEro1
dc.subjectDeath
dc.subjectMitochondria
dc.subjectHomeostasis
dc.titleOxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleSingle-Molecule Detection of the Prion Protein: Characterization of Conformational Change Involved on Prion Diseases
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBSAB%2F922%2F2009/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI%2F73027%2F2006/PT
oaire.citation.endPage797
oaire.citation.issue5
oaire.citation.startPage787
oaire.citation.titleMolecular Cell
oaire.citation.volume40
oaire.fundingStreamSFRH
oaire.fundingStream3599-PPCDT
person.familyNamePinho Melo
person.givenNameEduardo
person.identifier1443188
person.identifier.ciencia-id3C1C-C10C-1510
person.identifier.orcid0000-0002-0974-8977
person.identifier.scopus-author-id35566177900
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
rcaap.typearticle
relation.isAuthorOfPublication5fa1895f-5577-4652-961a-886ec9bf41b1
relation.isAuthorOfPublication.latestForDiscovery5fa1895f-5577-4652-961a-886ec9bf41b1
relation.isProjectOfPublication6be915aa-3a11-4e44-945b-b98170cfce94
relation.isProjectOfPublicatione494aee3-f280-4be8-8899-13235f48e1dd
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