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dc.contributor.authorCabiscol Català, Elisa
dc.contributor.authorPiulats Combalia, Eva
dc.contributor.authorEchave Lozano, Pedro
dc.contributor.authorHerrero Perpiñán, Enrique
dc.contributor.authorRos Salvador, Joaquim
dc.date.accessioned2015-07-07T09:43:08Z
dc.date.issued2000
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/10459.1/48412
dc.description.abstractWe have analyzed the proteins that are oxidatively damaged when Saccharomyces cerevisiae cells are ex- posed to stressing conditions. Carbonyl groups generated by hydrogen peroxide or menadione on proteins of aero- bically respiring cells were detected by Western blotting, purified, and identified. Mitochondrial proteins such as E2 subunits of both pyruvate dehydrogenase and ␣-keto- glutarate dehydrogenase, aconitase, heat-shock protein 60, and the cytosolic fatty acid synthase (␣ subunit) and glyceraldehyde-3-phosphate dehydrogenase were the ma- jor targets. In addition we also report the in vivo modifi- cation of lipoamide present in the above-mentioned E2 subunits under the stressing conditions tested and that this also occurs with the homologous enzymes present in Escherichia coli cells that were used for comparative analysis. Under fermentative conditions, the main pro- tein targets in S. cerevisiae cells treated with hydrogen peroxide or menadione were pyruvate decarboxylase, enolase, fatty acid synthase, and glyceraldehyde-3-phos- phate dehydrogenase. Under the stress conditions tested, fermenting cells exhibit a lower viability than aerobically respiring cells and, consistently, increased peroxide gen- eration as well as higher content of protein carbonyls and lipid peroxides. Our results strongly suggest that the oxidative stress in prokaryotic and eukaryotic cells shares common features.ca_ES
dc.language.isoengca_ES
dc.publisherThe American Society for Biochemistry and Molecular Biologyca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1074/jbc.M003140200ca_ES
dc.relation.ispartofThe Journal of Biological Chemistry, 2000, vol. 275, núm 35, p. 27393-27398ca_ES
dc.rights(c) The American Society for Biochemistry and Molecular Biology, 2000ca_ES
dc.titleOxidative stress promotes specific protein damage in Saccharomyces cerevisiaeca_ES
dc.typearticleca_ES
dc.identifier.idgrec001516
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1074/jbc.M003140200


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