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http://purl.uniprot.org/citations/24841564http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24841564http://www.w3.org/2000/01/rdf-schema#comment"Mitochondrial respiratory chain complexes convert chemical energy into a membrane potential by connecting electron transport with charge separation. Electron transport relies on redox cofactors that occupy strategic positions in the complexes. How these redox cofactors are assembled into the complexes is not known. Cytochrome b, a central catalytic subunit of complex III, contains two heme bs. Here, we unravel the sequence of events in the mitochondrial inner membrane by which cytochrome b is hemylated. Heme incorporation occurs in a strict sequential process that involves interactions of the newly synthesized cytochrome b with assembly factors and structural complex III subunits. These interactions are functionally connected to cofactor acquisition that triggers the progression of cytochrome b through successive assembly intermediates. Failure to hemylate cytochrome b sequesters the Cbp3-Cbp6 complex in early assembly intermediates, thereby causing a reduction in cytochrome b synthesis via a feedback loop that senses hemylation of cytochrome b."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201401009"xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/author"Ott M."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/author"Hegg E.L."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/author"Meunier B."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/author"Stephan K."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/author"Gruschke S."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/author"Hildenbeutel M."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/name"J Cell Biol"xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/pages"511-524"xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/title"Assembly factors monitor sequential hemylation of cytochrome b to regulate mitochondrial translation."xsd:string
http://purl.uniprot.org/citations/24841564http://purl.uniprot.org/core/volume"205"xsd:string
http://purl.uniprot.org/citations/24841564http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24841564
http://purl.uniprot.org/citations/24841564http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24841564
http://purl.uniprot.org/uniprot/#_P21560-mappedCitation-24841564http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24841564
http://purl.uniprot.org/uniprot/#_P07253-mappedCitation-24841564http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24841564
http://purl.uniprot.org/uniprot/P21560http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24841564
http://purl.uniprot.org/uniprot/P07253http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24841564