| http://purl.uniprot.org/citations/23270816 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23270816 | http://www.w3.org/2000/01/rdf-schema#comment | "Coenzyme Qn (ubiquinone or Qn) is a redox active lipid composed of a fully substituted benzoquinone ring and a polyisoprenoid tail of n isoprene units. Saccharomyces cerevisiae coq1-coq9 mutants have defects in Q biosynthesis, lack Q6, are respiratory defective, and sensitive to stress imposed by polyunsaturated fatty acids. The hallmark phenotype of the Q-less yeast coq mutants is that respiration in isolated mitochondria can be rescued by the addition of Q2, a soluble Q analog. Yeast coq10 mutants share each of these phenotypes, with the surprising exception that they continue to produce Q6. Structure determination of the Caulobacter crescentus Coq10 homolog (CC1736) revealed a steroidogenic acute regulatory protein-related lipid transfer (START) domain, a hydrophobic tunnel known to bind specific lipids in other START domain family members. Here we show that purified CC1736 binds Q2, Q3, Q10, or demethoxy-Q3 in an equimolar ratio, but fails to bind 3-farnesyl-4-hydroxybenzoic acid, a farnesylated analog of an early Q-intermediate. Over-expression of C. crescentus CC1736 or COQ8 restores respiratory electron transport and antioxidant function of Q6 in the yeast coq10 null mutant. Studies with stable isotope ring precursors of Q reveal that early Q-biosynthetic intermediates accumulate in the coq10 mutant and de novo Q-biosynthesis is less efficient than in the wild-type yeast or rescued coq10 mutant. The results suggest that the Coq10 polypeptide:Q (protein:ligand) complex may serve essential functions in facilitating de novo Q biosynthesis and in delivering newly synthesized Q to one or more complexes of the respiratory electron transport chain."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbalip.2012.12.007"xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Kawashima T."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Ji Z."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Hill S."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Loo J.A."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Hirano K."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Shepherd J.N."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Johnson J.S."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Allan C.M."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Clarke C.F."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Saiki R."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Liau W.S."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/author | "Morvaridi S."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/pages | "776-791"xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/title | "A conserved START domain coenzyme Q-binding polypeptide is required for efficient Q biosynthesis, respiratory electron transport, and antioxidant function in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://purl.uniprot.org/core/volume | "1831"xsd:string |
| http://purl.uniprot.org/citations/23270816 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23270816 |
| http://purl.uniprot.org/citations/23270816 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23270816 |
| http://purl.uniprot.org/uniprot/Q08058#attribution-2A3AA41922567B7669974684533AB93F | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/23270816 |
| http://purl.uniprot.org/uniprot/#_P56556-mappedCitation-23270816 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23270816 |
| http://purl.uniprot.org/uniprot/#_O15239-mappedCitation-23270816 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23270816 |