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dc.contributor.authorBarros, M. H.-
dc.contributor.authorJohnson, A.-
dc.contributor.authorTzagoloff, A.-
dc.date.accessioned2014-05-20T13:50:09Z-
dc.date.accessioned2016-10-25T17:02:23Z-
dc.date.available2014-05-20T13:50:09Z-
dc.date.available2016-10-25T17:02:23Z-
dc.date.issued2004-07-23-
dc.identifierhttp://dx.doi.org/10.1074/jbc.M405014200-
dc.identifier.citationJournal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc., v. 279, n. 30, p. 31943-31947, 2004.-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/11449/17905-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/17905-
dc.description.abstractDeletion of reading frame YHR116W of the Saccharomyces cerevisiae nuclear genome elicits a respiratory deficiency. The encoded product, here named Cox23p, is shown to be required for the expression of cytochrome oxidase. Cox23p is homologous to Cox17p, a water-soluble copper protein previously implicated in the maturation of the Cu-A center of cytochrome oxidase. The respiratory defect of a cox23 null mutant is rescued by high concentrations of copper in the medium but only when the mutant harbors COX17 on a high copy plasmid. Overexpression of Cox17p by itself is not a sufficient condition to rescue the mutant phenotype. Cox23p, like Cox17p, is detected in the intermembrane space of mitochondria and in the postmitochondrial supernatant fraction, the latter consisting predominantly of cytosolic proteins. Because Cox23p and Cox17p are not part of a complex, the requirement of both for cytochrome oxidase assembly suggests that they function in a common pathway with Cox17p acting downstream of Cox23p.en
dc.format.extent31943-31947-
dc.language.isoeng-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.sourceWeb of Science-
dc.titleCOX23, a homologue of COX17, is required for cytochrome oxidase assemblyen
dc.typeoutro-
dc.contributor.institutionColumbia University-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationColumbia Univ, Dept Biol Sci, New York, NY 10027 USA-
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias Botucatu, Dept Genet, BR-18607741 São Paulo, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias Botucatu, Dept Genet, BR-18607741 São Paulo, Brazil-
dc.identifier.doi10.1074/jbc.M405014200-
dc.identifier.wosWOS:000222726800122-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Biological Chemistry-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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