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dc.contributor.authorBarreto Parra, Lina Patricia
dc.contributor.authorGarcera, Ana
dc.contributor.authorJansson, Kristina
dc.contributor.authorSunnerhagen, Per
dc.contributor.authorHerrero Perpiñán, Enrique
dc.date.accessioned2014-05-16T16:58:31Z
dc.date.available2014-05-16T16:58:31Z
dc.date.issued2006
dc.identifier.issn1535-9778 (versió paper)
dc.identifier.issn1535-9786
dc.identifier.urihttp://hdl.handle.net/10459.1/47217
dc.description.abstractSaccharomyces cerevisiae cells contain three omega-class glutathione transferases with glutaredoxin activity (Gto1, Gto2, and Gto3), in addition to two glutathione transferases (Gtt1 and Gtt2) not classifiable into standard classes. Gto1 is located at the peroxisomes, where it is targeted through a PTS1-type sequence, whereas Gto2 and Gto3 are in the cytosol. Among the GTO genes, GTO2 shows the strongest induction of expression by agents such as diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide or cadmium, in a manner that is dependent on transcriptional factors Yap1 and/or Msn2/4. Diamide and 1-chloro-2,4-dinitrobenzene (causing depletion of reduced glutathione) also induce expression of GTO1 over basal levels. Phenotypic analyses with single and multiple mutants in the S. cerevisiae glutathione transferase genes show that, in the absence of Gto1 and the two Gtt proteins, cells display increased sensitivity to cadmium. A gto1-null mutant also shows growth defects on oleic acid-based medium, which is indicative of abnormal peroxisomal functions, and altered expression of genes related to sulfur amino acid metabolism. As a consequence, growth of the gto1 mutant is delayed in growth medium without lysine, serine, or threonine, and the mutant cells have low levels of reduced glutathione. The role of Gto1 at the S. cerevisiae peroxisomes could be related to the redox regulation of the Str3 cystathionine -lyase protein. This protein is also located at the peroxisomes in S. cerevisiae, where it is involved in transulfuration of cysteine into homocysteine, and requires a conserved cysteine residue for its biological activity.ca_ES
dc.language.isoengca_ES
dc.publisherAmerican Society for Microbiologyca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1128/EC.00216-06ca_ES
dc.relation.ispartofEukaryotic cell, 2006, vol. 5, núm. 10, p. 1748-1759ca_ES
dc.rights(c) American Society for Microbiology, 2006ca_ES
dc.subjectLlevat de cervesaca_ES
dc.subject.otherSaccharomyces cerevisiaeca_ES
dc.subject.otherAminoàcids--Metabolismeca_ES
dc.titleA peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolismca_ES
dc.typearticleca_ES
dc.identifier.idgrec010456
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1128/EC.00216-06


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