dc.contributorColumbia University
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:50:09Z
dc.date.accessioned2022-10-05T14:22:47Z
dc.date.available2014-05-20T13:50:09Z
dc.date.available2022-10-05T14:22:47Z
dc.date.created2014-05-20T13:50:09Z
dc.date.issued2004-07-23
dc.identifierJournal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc., v. 279, n. 30, p. 31943-31947, 2004.
dc.identifier0021-9258
dc.identifierhttp://hdl.handle.net/11449/17905
dc.identifier10.1074/jbc.M405014200
dc.identifierWOS:000222726800122
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3892491
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.
dc.languageeng
dc.publisherAmer Soc Biochemistry Molecular Biology Inc
dc.relationJournal of Biological Chemistry
dc.relation4.010
dc.relation2,672
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.titleCOX23, a homologue of COX17, is required for cytochrome oxidase assembly
dc.typeArtigo


Este ítem pertenece a la siguiente institución