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http://purl.uniprot.org/citations/19338496http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19338496http://www.w3.org/2000/01/rdf-schema#comment"CcO (cytochrome c oxidase) is a multisubunit bigenomic protein complex which catalyses the last step of the mitochondrial electron transport chain. The nuclear-encoded subunits are thought to have roles either in regulation or in the structural stability of the enzyme. Subunit Vb is a peripheral nuclear-encoded subunit of mammalian CcO that is dramatically reduced under hypoxia. Although it has been shown to contain different ligand-binding sites and undergo modifications, its precise function is not known. In the present study we generated a cell line from RAW 264.7 murine macrophages that has a more than 80% reduced level of Vb. Functional analysis of these cells showed a loss of CcO activity, membrane potential and less ability to generate ATP. Resolution of complexes on blue native gel and two-dimensional electrophoretic analysis showed an accumulation of subcomplexes of CcO and also reduced association with supercomplexes of the electron transfer chain. Furthermore, the mitochondria from CcO Vb knock-down cells generated increased ROS (reactive oxygen species), and the cells were unable to grow on galactose-containing medium. Pulse-chase experiments suggest the role of the CcO Vb subunit in the assembly of the complex. We show for the first time the role of a peripheral, non-transmembrane subunit in the formation as well as function of the terminal CcO complex."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.org/dc/terms/identifier"doi:10.1042/bj20090214"xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Lopez M."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Srinivasan S."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Chandran K."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Avadhani N.G."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Raza H."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Kalyanaraman B."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Hardy M."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Prabu S.K."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/author"Galati D."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/name"Biochem J"xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/pages"439-449"xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/title"Role of nuclear-encoded subunit Vb in the assembly and stability of cytochrome c oxidase complex: implications in mitochondrial dysfunction and ROS production."xsd:string
http://purl.uniprot.org/citations/19338496http://purl.uniprot.org/core/volume"420"xsd:string
http://purl.uniprot.org/citations/19338496http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19338496
http://purl.uniprot.org/citations/19338496http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19338496
http://purl.uniprot.org/uniprot/#_P19536-mappedCitation-19338496http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19338496
http://purl.uniprot.org/uniprot/#_Q9D881-mappedCitation-19338496http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19338496
http://purl.uniprot.org/uniprot/Q9D881http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19338496
http://purl.uniprot.org/uniprot/P19536http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19338496