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rdf:type |
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lifeskim:mentions |
umls-concept:C0001475,
umls-concept:C0017337,
umls-concept:C0020792,
umls-concept:C0043393,
umls-concept:C0521447,
umls-concept:C1425786,
umls-concept:C1425787,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1706853,
umls-concept:C1879748
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pubmed:issue |
13
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pubmed:dateCreated |
1990-8-15
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pubmed:abstractText |
Nuclear respiratory-deficient mutants of Saccharomyces cerevisiae (pet mutants) have been screened for defects in the mitochondrial ATPase. Mutants in two complementation groups were found to have 10% or less of wild-type ATPase activity. The two wild-type nuclear genes defined by the mutants have been designated ATP11 and ATP12. The proteins encoded by the two genes are not subunits of the ATPase but rather appear to exercise an important function at a late stage in the synthesis of F1 after transport of the subunits into the internal compartment of mitochondria. Mitochondria of atp11 and atp12 mutants have only marginally reduced levels of the alpha and beta subunits of F1. Both proteins are processed to their mature size but are not part of a native F1 structure or associated with the mitochondrial membrane. The most reasonable explanation for the mutant phenotype is a block in the assembly of the F1 oligomer.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-133820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-145825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-154672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-156363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-156843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-159297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-170284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2528694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2563898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2645524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2844766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2864455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2866186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2875070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2876995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2897629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-2999114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-4221250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-4231098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-4241924,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-4251997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-4358614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-4613841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-6223276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-6226867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-6254007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-6310324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-6400651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-6446405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2142305-7001447
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4986-90
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2142305-Cell Nucleus,
pubmed-meshheading:2142305-DNA, Fungal,
pubmed-meshheading:2142305-Genes, Fungal,
pubmed-meshheading:2142305-Genetic Complementation Test,
pubmed-meshheading:2142305-Genotype,
pubmed-meshheading:2142305-Macromolecular Substances,
pubmed-meshheading:2142305-Mitochondria,
pubmed-meshheading:2142305-Mutation,
pubmed-meshheading:2142305-Nucleic Acid Hybridization,
pubmed-meshheading:2142305-Protein Processing, Post-Translational,
pubmed-meshheading:2142305-Proton-Translocating ATPases,
pubmed-meshheading:2142305-Saccharomyces cerevisiae,
pubmed-meshheading:2142305-Submitochondrial Particles,
pubmed-meshheading:2142305-Transcription, Genetic
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pubmed:year |
1990
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pubmed:articleTitle |
Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase.
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pubmed:affiliation |
Department of Biological Sciences, Columbia University, New York, NY 10027.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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