Source:http://linkedlifedata.com/resource/pubmed/id/11926067
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2002-4-2
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pubmed:abstractText |
We analyzed the protein components contained in the mitochondrial nucleoid (mt-nucleoid) fraction of the yeast Saccharomyces cerevisiae. Immunoblotting with anti-Abf2p antibody demonstrated the association of Abf2p, a major mitochondrial DNA-binding protein, with the mt-nucleoids. In contrast, porin and cytochrome c oxidase subunit III (CoxIIIp) were not detected by immunoblotting in the mt-nucleoid fraction. The YMN-1 monoclonal antibody recognized a 48 kDa protein of the mt-nucleoid fraction. The N-terminal amino acid sequence of the protein and immunological evidence showed that the YMN-1 monoclonal antibody recognizes dihydrolipoyl transsuccinylase (KE2), which is one of the constituents of the alpha-ketoglutarate dehydrogenase complex (KGDC). alpha-Ketoglutarate dehydrogenase (KE1) and dihydrolipoyl dehydrogenase (E3), which are other subunits of KGDC, were also detected in the mt-nucleoid fraction. An enzyme assay of the mt-nucleoid fraction showed that cytochrome c oxidase and fumarase activity were barely detected in the fraction, but the specific activity of KGDC in the mt-nucleoid fraction was relatively high and was approximately 60% of the specific activity in the mitochondrial fraction. Three components of KGDC were detected in the DNA-binding protein fractions after DNA-cellulose column chromatography of mt-nucleoid proteins. These results suggested that a part of KGDC in the mitochondrial matrix is associated with mt-nucleoids in vivo.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/Dihydrolipoamide Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Ketoglutarate Dehydrogenase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/dihydrolipoamide succinyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0033-183X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
219
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11926067-Acyltransferases,
pubmed-meshheading:11926067-Amino Acid Sequence,
pubmed-meshheading:11926067-Antibodies, Monoclonal,
pubmed-meshheading:11926067-Antigens, Fungal,
pubmed-meshheading:11926067-Dihydrolipoamide Dehydrogenase,
pubmed-meshheading:11926067-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:11926067-Immunoblotting,
pubmed-meshheading:11926067-Ketoglutarate Dehydrogenase Complex,
pubmed-meshheading:11926067-Mitochondria,
pubmed-meshheading:11926067-Molecular Sequence Data,
pubmed-meshheading:11926067-Molecular Weight,
pubmed-meshheading:11926067-Protein Subunits,
pubmed-meshheading:11926067-Saccharomyces cerevisiae,
pubmed-meshheading:11926067-Saccharomyces cerevisiae Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Identification of the YMN-1 antigen protein and biochemical analyses of protein components in the mitochondrial nucleoid fraction of the yeast Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Physics, Biology and Informatics, Faculty of Science, Yamaguchi University, Yamaguchi, 753-8512, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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