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rdf:type |
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lifeskim:mentions |
umls-concept:C0025252,
umls-concept:C0026237,
umls-concept:C0030940,
umls-concept:C0162871,
umls-concept:C0205102,
umls-concept:C0205148,
umls-concept:C0205681,
umls-concept:C0243125,
umls-concept:C0596901,
umls-concept:C0597304,
umls-concept:C0699900,
umls-concept:C1521805
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pubmed:issue |
16
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pubmed:dateCreated |
1996-12-16
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pubmed:abstractText |
The mechanism of selective protein degradation of membrane proteins in mitochondria has been studied employing a model protein that is subject to rapid proteolysis within the inner membrane. Protein degradation was mediated by two different proteases: (i) the m-AAA protease, a protease complex consisting of multiple copies of the ATP-dependent metallopeptidases Yta1Op (Afg3p) and Yta12p (Rcalp); and (ii) by Ymelp (Ytallp) that also is embedded in the inner membrane. Ymelp, highly homologous to Yta1Op and Yta12p, forms a complex of approximately 850 kDa in the inner membrane and exerts ATP-dependent metallopeptidase activity. While the m-AAA protease exposes catalytic sites to the mitochondrial matrix, Ymelp is active in the intermembrane space. The Ymelp complex was therefore termed 'i-AAA protease'. Analysis of the proteolytic fragments indicated cleavage of the model polypeptide at the inner and outer membrane surface and within the membrane-spanning domain. Thus, two AAA proteases with their catalytic sites on opposite membrane surfaces constitute a novel proteolytic system for the degradation of membrane proteins in mitochondria.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-1104589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-1943808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-2265750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-3521657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7559511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7589436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7592959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7623837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7646486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7724592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7753838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7754704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7781608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7803857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7814360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7900428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7926051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7926052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-7929327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-8106504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-8355690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-8507683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-8641436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-8681382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8861950-8688560
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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/AFG3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Dependent Proteases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV,
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/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrahydrofolate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/YME1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/YTA12 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4218-29
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8861950-ATP-Dependent Proteases,
pubmed-meshheading:8861950-Adenosine Triphosphatases,
pubmed-meshheading:8861950-Adenosine Triphosphate,
pubmed-meshheading:8861950-Binding Sites,
pubmed-meshheading:8861950-Electron Transport Complex IV,
pubmed-meshheading:8861950-Fungal Proteins,
pubmed-meshheading:8861950-Intracellular Membranes,
pubmed-meshheading:8861950-Membrane Proteins,
pubmed-meshheading:8861950-Metalloendopeptidases,
pubmed-meshheading:8861950-Mitochondria,
pubmed-meshheading:8861950-Mitochondrial Proteins,
pubmed-meshheading:8861950-Mutagenesis, Site-Directed,
pubmed-meshheading:8861950-Recombinant Fusion Proteins,
pubmed-meshheading:8861950-Saccharomyces cerevisiae,
pubmed-meshheading:8861950-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8861950-Tetrahydrofolate Dehydrogenase
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pubmed:year |
1996
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pubmed:articleTitle |
AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria.
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pubmed:affiliation |
Institut für Physiologische Chemie der Universität München, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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