RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17922846http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17922846http://www.w3.org/2000/01/rdf-schema#comment"Members of the YidC/Oxa1/Alb3 protein family function in the biogenesis of membrane proteins in bacteria, mitochondria and chloroplasts. In Escherichia coli, YidC plays a key role in the integration and assembly of many inner membrane proteins. Interestingly, YidC functions both in concert with the Sec-translocon and as a separate insertase independent of the translocon. Mitochondria of higher eukaryotes contain two distant homologues of YidC: Oxa1 and Cox18/Oxa2. Oxa1 is required for the insertion of membrane proteins into the mitochondrial inner membrane. Cox18/Oxa2 plays a poorly defined role in the biogenesis of the cytochrome c oxidase complex. Employing a genetic complementation approach by expressing the conserved region of yeast Cox18 in E. coli, we show here that Cox18 is able to complement the essential Sec-independent function of YidC. This identifies Cox18 as a bona fide member of the YidC/Oxa1/Alb3 family."xsd:string
http://purl.uniprot.org/citations/17922846http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2007.06094.x"xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/author"Koningstein G."xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/author"Herrmann J.M."xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/author"Luirink J."xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/author"van Bloois E."xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/author"Bauerschmitt H."xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/name"FEBS J"xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/pages"5704-5713"xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/title"Saccharomyces cerevisiae Cox18 complements the essential Sec-independent function of Escherichia coli YidC."xsd:string
http://purl.uniprot.org/citations/17922846http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/17922846http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17922846
http://purl.uniprot.org/citations/17922846http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17922846
http://purl.uniprot.org/uniprot/#_A0A8H4C0E7-mappedCitation-17922846http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17922846
http://purl.uniprot.org/uniprot/#_P53239-mappedCitation-17922846http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17922846
http://purl.uniprot.org/uniprot/A0A8H4C0E7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17922846
http://purl.uniprot.org/uniprot/P53239http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17922846