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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2008-6-2
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pubmed:abstractText |
The mitochondrial intermembrane space contains a family of small Tim proteins that function as essential chaperones for protein import. The soluble Tim9-Tim10 complex transfers hydrophobic precursor proteins through the aqueous intermembrane space to the carrier translocase of the inner membrane (TIM22 complex). Tim12, a peripheral membrane subunit of the TIM22 complex, is thought to recruit a portion of Tim9-Tim10 to the inner membrane. It is not known, however, how Tim12 is assembled. We have identified a new intermediate in the biogenesis pathway of Tim12. A soluble form of Tim12 first assembles with Tim9 and Tim10 to form a Tim12-core complex. Tim12-core then docks onto the membrane-integrated subunits of the TIM22 complex to form the holo-translocase. Thus, the function of Tim12 in linking soluble and membrane-integrated subunits of the import machinery involves a sequential assembly mechanism of the translocase through a soluble intermediate complex of the three essential small Tim proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-11723465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-11864609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-12391147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-12637749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-15232570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-15359280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-15473843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-16387659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-17122363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-17263664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-17329230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-17627602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-9430585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-9495346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-9774667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-9822593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18421298-9889188
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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/MRS11 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/MRS5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial ADP, ATP Translocases,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Membrane Transport...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tim9 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1469-3178
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
548-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18421298-Membrane Proteins,
pubmed-meshheading:18421298-Membrane Transport Proteins,
pubmed-meshheading:18421298-Mitochondrial ADP, ATP Translocases,
pubmed-meshheading:18421298-Mitochondrial Membrane Transport Proteins,
pubmed-meshheading:18421298-Mitochondrial Proteins,
pubmed-meshheading:18421298-Multiprotein Complexes,
pubmed-meshheading:18421298-Protein Precursors,
pubmed-meshheading:18421298-Protein Subunits,
pubmed-meshheading:18421298-Saccharomyces cerevisiae,
pubmed-meshheading:18421298-Saccharomyces cerevisiae Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Assembly of the three small Tim proteins precedes docking to the mitochondrial carrier translocase.
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pubmed:affiliation |
Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Freiburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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