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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
42
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pubmed:dateCreated |
1994-11-22
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pubmed:databankReference | |
pubmed:abstractText |
Respiration-defective pet mutants of Saccharomyces cerevisiae, assigned to complementation group G25, are grossly deficient in mitochondrial respiratory and ATPase complexes. This phenotype is usually found in strains impaired in mitochondrial protein synthesis. The G25 mutants, however, synthesize all of the proteins encoded by mitochondrial DNA. The mutants are also able to import and process cytoplasmically derived subunits of these enzymes. These results are most compatible with the idea that the gene defined by G25 mutants (RCA1) codes for a protein essential for the assembly of functional respiratory and ATPase complexes. The RCA1 gene has been cloned by complementation of an rca1 mutant with a yeast genomic library. The sequence of the encoded product shows Rca1 protein to be a new member of a recently described family of ATPases. The Rca1 protein is a mitochondrial membrane protein and is the third known member of this family implicated to function in the biogenesis of mitochondria. The primary structure of Rca1 protein indicates several distinct domains in addition to the common purine nucleotide binding region shared by all members of this protein family. One, located in the amino-terminal half, contains two hydrophobic stretches of sufficient length to span a membrane lipid bilayer.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
269
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pubmed:geneSymbol |
rca1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26144-51
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7929327-Adenosine Triphosphatases,
pubmed-meshheading:7929327-Amino Acid Sequence,
pubmed-meshheading:7929327-Base Sequence,
pubmed-meshheading:7929327-Cloning, Molecular,
pubmed-meshheading:7929327-Electron Transport,
pubmed-meshheading:7929327-Fungal Proteins,
pubmed-meshheading:7929327-Membrane Proteins,
pubmed-meshheading:7929327-Metalloendopeptidases,
pubmed-meshheading:7929327-Mitochondria,
pubmed-meshheading:7929327-Mitochondrial Proteins,
pubmed-meshheading:7929327-Molecular Sequence Data,
pubmed-meshheading:7929327-Phenotype,
pubmed-meshheading:7929327-Proton-Translocating ATPases,
pubmed-meshheading:7929327-Saccharomyces cerevisiae,
pubmed-meshheading:7929327-Saccharomyces cerevisiae Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
A new member of a family of ATPases is essential for assembly of mitochondrial respiratory chain and ATP synthetase complexes in Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Biological Sciences, Columbia University, New York, New York 10027.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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