20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteins

Página do item simplificado
dc.contributor.authorDemasi, Marilene
dc.contributor.authorHand, Adrian
dc.contributor.authorOhara, Erina
dc.contributor.authorOliveira, Cristiano L. P.
dc.contributor.authorBicev, Renata N.
dc.contributor.authorBertoncini, Clelia A. [UNIFESP]
dc.contributor.authorNetto, Luis E. S.
dc.contributor.institutionInst Butantan
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:37:47Z
dc.date.available2016-01-24T14:37:47Z
dc.date.issued2014-09-01
dc.description.abstractProtein S-glutathionylation is a post-translational modification that controls many cellular pathways. Recently, we demonstrated that the alpha 5-subunit of the 20S proteasome is S-glutathionylated in yeast cells grown to the stationary phase in rich medium containing glucose, stimulating 20S core gate opening and increasing the degradation of oxidized proteins. in the present study, we evaluated the correlation between proteasomal S-glutathionylation and the intracellular redox status. the redox status was controlled by growing yeast cells in distinct carbon sources which induced respiratory (glycerol/ethanol) or fermentative (glucose) metabolism. Cells grown under glycerol/ethanol displayed higher reductive power when compared to cells grown under glucose. When purified from cells grown in glucose, 20S proteasome alpha 5-subunit exhibited an intense anti-glutathione labeling. A higher frequency of the open catalytic chamber gate was observed in the S-glutathionylated preparations as demonstrated by transmission electron microscopy. Therefore, cells that had been grown in glucose displayed an increased ability to degrade oxidized proteins. the results of the present study suggest that 20S proteasomal S-glutathionylation is a relevant adaptive response to oxidative stress that is capable to sense the intracellular redox environment, leading to the removal of oxidized proteins via a process that is not dependent upon ubiquitylation and ATP consumption. (C) 2014 Elsevier Inc. All rights reserved.en
dc.description.affiliationInst Butantan, Lab Bioquim & Biofis, BR-05503001 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Fis, BR-05508 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Biociencias, Dept Genet & Biol Evolut, BR-05508 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, EPM, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent65-71
dc.identifierhttp://dx.doi.org/10.1016/j.abb.2014.05.002
dc.identifier.citationArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 557, p. 65-71, 2014.
dc.identifier.doi10.1016/j.abb.2014.05.002
dc.identifier.issn0003-9861
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/38148
dc.identifier.wosWOS:000339646600009
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subject20S proteasomeen
dc.subjectS-glutathionylationen
dc.subjectS. cerevisiaeen
dc.subjectRedox modulationen
dc.subjectOxidized proteinsen
dc.subjectProteolysisen
dc.title20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteinsen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
EPM - Artigos