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dc.contributor.authorCabiscol Català, Elisa
dc.contributor.authorBellí i Martínez, Gemma
dc.contributor.authorTamarit Sumalla, Jordi
dc.contributor.authorEchave Lozano, Pedro
dc.contributor.authorHerrero Perpiñán, Enrique
dc.contributor.authorRos Salvador, Joaquim
dc.date.accessioned2015-07-02T09:34:39Z
dc.date.issued2002
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/10459.1/48399
dc.description.abstractIn the present study, we have analyzed the role of the molecular chaperone Hsp60 in protection of Saccharo- myces cerevisiae against oxidative damage. We con- structed mutant strains in which the levels of Hsp60 protein, compared with wild-type cells, were four times greater, and the addition of doxycycline gradually re- duces them to 20% of wild-type. Under oxidative-stress conditions, the progressive decrease in Hsp60 levels in these mutants resulted in reduced cell viability and an increase in both cell peroxide species and protein car- bonyl content. Protection of Fe/S-containing enzymes from oxidative inactivation was found to be dose-de- pendent with respect to Hsp60 levels. As these enzymes release their iron ions under oxidative-stress condi- tions, the intracellular labile iron pool, monitored with calcein, was higher in cells with reduced Hsp60 levels. Consistently, the iron chelator deferoxamine protected low Hsp60-expressing cells from both oxidant-induced death and protein oxidation. These results indicate that the role of Hsp60 in oxidative-stress defense is explained by protection of several Fe/S proteins, which prevent the release of iron ions and thereby avert further damage.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.M206525200ca_ES
dc.relation.ispartofThe Journal of Biological Chemistry, 2002, vol. 277, núm 46, p. 44531-44538ca_ES
dc.rights(c) The American Society for Biochemistry and Molecular Biology, 2002ca_ES
dc.titleMitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiaeca_ES
dc.typearticleca_ES
dc.identifier.idgrec000006
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1074/jbc.M206525200


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