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dc.contributor.authorHerrero Perpiñán, Enrique
dc.contributor.authorRos Salvador, Joaquim
dc.contributor.authorBellí i Martínez, Gemma
dc.contributor.authorCabiscol Català, Elisa
dc.date.accessioned2015-07-07T08:37:01Z
dc.date.issued2008
dc.identifier.issn0006-3002
dc.identifier.urihttp://hdl.handle.net/10459.1/48408
dc.description.abstractProtein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules.ca_ES
dc.language.isoengca_ES
dc.publisherElsevierca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1016/j.bbagen.2007.12.004ca_ES
dc.relation.ispartofBiochimica et Biophysica Acta, 2008, vol. 1780, núm. 11, p.1217-1235ca_ES
dc.rights(c) Elsevier, 2007ca_ES
dc.subjectCatalaseca_ES
dc.subjectSuperoxide dismutaseca_ES
dc.subjectPeroxidaseca_ES
dc.titleRedox control and oxidative stress in yeast cellsca_ES
dc.typearticleca_ES
dc.identifier.idgrec013101
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccessca_ES
dc.identifier.doihttps://doi.org/10.1016/j.bbagen.2007.12.004
dc.date.embargoEndDate2025-01-01


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