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rdf:type |
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lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0033684,
umls-concept:C0035203,
umls-concept:C0036025,
umls-concept:C0041536,
umls-concept:C0056077,
umls-concept:C0439659,
umls-concept:C0542341,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2700640
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pubmed:issue |
52
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pubmed:dateCreated |
2005-12-26
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pubmed:abstractText |
Deletion of the Saccharomyces cerevisiae gene YOL008W, here referred to as COQ10, elicits a respiratory defect as a result of the inability of the mutant to oxidize NADH and succinate. Both activities are restored by exogenous coenzyme Q2. Respiration is also partially rescued by COQ2, COQ7, or COQ8/ABC1, when these genes are present in high copy. Unlike other coq mutants, all of which lack Q6, the coq10 mutant has near normal amounts of Q6 in mitochondria. Coq10p is widely distributed in bacteria and eukaryotes and is homologous to proteins of the "aromatic-rich protein family" Pfam03654 and to members of the START domain superfamily that have a hydrophobic tunnel implicated in binding lipophilic molecules such as cholesterol and polyketides. Analysis of coenzyme Q in polyhistidine-tagged Coq10p purified from mitochondria indicates the presence 0.032-0.034 mol of Q6/mol of protein. We propose that Coq10p is a Q6-binding protein and that in the coq10 mutant Q6 it is not able to act as an electron carrier, possibly because of improper localization.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Coenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NADH oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/Succinates,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquinone,
http://linkedlifedata.com/resource/pubmed/chemical/coenzyme Q10,
http://linkedlifedata.com/resource/pubmed/chemical/polyhistidine,
http://linkedlifedata.com/resource/pubmed/chemical/ubiquinone 6
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
42627-35
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16230336-Amino Acid Sequence,
pubmed-meshheading:16230336-Chromatography, High Pressure Liquid,
pubmed-meshheading:16230336-Coenzymes,
pubmed-meshheading:16230336-Cytochrome Reductases,
pubmed-meshheading:16230336-DNA, Complementary,
pubmed-meshheading:16230336-DNA Primers,
pubmed-meshheading:16230336-Electron Transport,
pubmed-meshheading:16230336-Electron Transport Complex IV,
pubmed-meshheading:16230336-Electrons,
pubmed-meshheading:16230336-Gene Expression Regulation, Fungal,
pubmed-meshheading:16230336-Genetic Complementation Test,
pubmed-meshheading:16230336-Genotype,
pubmed-meshheading:16230336-Histidine,
pubmed-meshheading:16230336-Humans,
pubmed-meshheading:16230336-Lipids,
pubmed-meshheading:16230336-Mitochondria,
pubmed-meshheading:16230336-Models, Genetic,
pubmed-meshheading:16230336-Molecular Sequence Data,
pubmed-meshheading:16230336-Multienzyme Complexes,
pubmed-meshheading:16230336-Mutation,
pubmed-meshheading:16230336-NAD,
pubmed-meshheading:16230336-NADH, NADPH Oxidoreductases,
pubmed-meshheading:16230336-Open Reading Frames,
pubmed-meshheading:16230336-Oxygen,
pubmed-meshheading:16230336-Oxygen Consumption,
pubmed-meshheading:16230336-Phenotype,
pubmed-meshheading:16230336-Plasmids,
pubmed-meshheading:16230336-Protein Binding,
pubmed-meshheading:16230336-Protein Biosynthesis,
pubmed-meshheading:16230336-Protein Structure, Tertiary,
pubmed-meshheading:16230336-Quinones,
pubmed-meshheading:16230336-Saccharomyces cerevisiae,
pubmed-meshheading:16230336-Sequence Homology, Amino Acid,
pubmed-meshheading:16230336-Succinates,
pubmed-meshheading:16230336-Ubiquinone
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pubmed:year |
2005
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pubmed:articleTitle |
The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration.
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pubmed:affiliation |
Department of Genetics, Instituto de Biociencias de Botucatu-Universidade Estadual Paulista, Botucatu/SP 18607-741, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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