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rdf:type |
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lifeskim:mentions |
umls-concept:C0013682,
umls-concept:C0043393,
umls-concept:C0073434,
umls-concept:C0439064,
umls-concept:C1314939,
umls-concept:C1335439,
umls-concept:C1514562,
umls-concept:C1704675,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2245743
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pubmed:issue |
20
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pubmed:dateCreated |
2003-5-12
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pubmed:abstractText |
The amino-terminal domain (ATD) of Saccharomyces cerevisiae mitochondrial RNA polymerase has been shown to provide a functional link between transcription and post-transcriptional events during mitochondrial gene expression. This connection is mediated in large part by its interactions with the matrix protein Nam1p and, based on genetic phenotypes, the mitochondrial membrane protein Sls1p. These observations led us to propose previously that mtRNA polymerase, Nam1p, and Sls1p work together to coordinate transcription and translation of mtDNA-encoded gene products. Here we demonstrate by specific labeling of mitochondrial gene products in vivo that Nam1p and Sls1p indeed work together in a pathway that is required globally for efficient mitochondrial translation. Likewise, mutations in the ATD result in similar global reductions in mitochondrial translation efficiency and sensitivity to the mitochondrial translation inhibitor erythromycin. These data, coupled with the observation that the ATD is required to co-purify Sls1p in association with mtDNA nucleoids, suggest that efficient expression of mtDNA-encoded genes in yeast involves a complex series of interactions that localize active transcription complexes to the inner membrane in order to coordinate translation with transcription.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-10393945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-10521287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-10869431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-10887179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-11118450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-11805046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-11909521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-12024022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-12529447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-1706458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-2005794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-2183001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-2651895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-3308116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-3513839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-3517858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-360043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-4271498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-7004642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-8200349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-8206703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-8232290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-8413192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-8917313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-8965710,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-8988256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12637560-9755179
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Erythromycin,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MTF2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, mitochondrial,
http://linkedlifedata.com/resource/pubmed/chemical/SLS1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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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 |
16
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18695-701
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:12637560-Blotting, Southern,
pubmed-meshheading:12637560-Blotting, Western,
pubmed-meshheading:12637560-Carrier Proteins,
pubmed-meshheading:12637560-Cell Nucleus,
pubmed-meshheading:12637560-DNA-Directed RNA Polymerases,
pubmed-meshheading:12637560-Erythromycin,
pubmed-meshheading:12637560-Fungal Proteins,
pubmed-meshheading:12637560-Membrane Proteins,
pubmed-meshheading:12637560-Mitochondria,
pubmed-meshheading:12637560-Mitochondrial Proteins,
pubmed-meshheading:12637560-Models, Biological,
pubmed-meshheading:12637560-Mutation,
pubmed-meshheading:12637560-Phenotype,
pubmed-meshheading:12637560-Plasmids,
pubmed-meshheading:12637560-Protein Biosynthesis,
pubmed-meshheading:12637560-Protein Structure, Tertiary,
pubmed-meshheading:12637560-RNA,
pubmed-meshheading:12637560-Saccharomyces cerevisiae,
pubmed-meshheading:12637560-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12637560-Transcription, Genetic,
pubmed-meshheading:12637560-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Multiple interactions involving the amino-terminal domain of yeast mtRNA polymerase determine the efficiency of mitochondrial protein synthesis.
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pubmed:affiliation |
Department of Biochemistry and the Graduate Program in Biochemistry, Cell and Developmental Biology, Rollins Research Center, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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