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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6752
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pubmed:dateCreated |
1999-10-22
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pubmed:abstractText |
Mitochondrial preproteins are imported by a multisubunit translocase of the outer membrane (TOM), including receptor proteins and a general import pore. The central receptor Tom22 binds preproteins through both its cytosolic domain and its intermembrane space domain and is stably associated with the channel protein Tom40 (refs 11-13). Here we report the unexpected observation that a yeast strain can survive without Tom22, although it is strongly reduced in growth and the import of mitochondrial proteins. Tom22 is a multifunctional protein that is required for the higher-level organization of the TOM machinery. In the absence of Tom22, the translocase dissociates into core complexes, representing the basic import units, but lacks a tight control of channel gating. The single membrane anchor of Tom22 is required for a stable interaction between the core complexes, whereas its cytosolic domain serves as docking point for the peripheral receptors Tom20 and Tom70. Thus a preprotein translocase can combine receptor functions with distinct organizing roles in a multidomain protein.
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pubmed:commentsCorrections |
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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/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
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/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TOM20 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/TOM22 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/TOM70 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrahydrofolate Dehydrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0028-0836
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pubmed:author |
pubmed-author:BrimAA,
pubmed-author:DekkerP JPJ,
pubmed-author:GuiardBB,
pubmed-author:HönlingerAA,
pubmed-author:HillKK,
pubmed-author:MaarseA CAC,
pubmed-author:MeijerMM,
pubmed-author:MeisingerCC,
pubmed-author:MoczkoMM,
pubmed-author:PfannerNN,
pubmed-author:RyanM TMT,
pubmed-author:WagnerRR,
pubmed-author:van WilpeSS
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
401
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
485-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10519552-Biological Transport,
pubmed-meshheading:10519552-Carrier Proteins,
pubmed-meshheading:10519552-Electrophysiology,
pubmed-meshheading:10519552-Fungal Proteins,
pubmed-meshheading:10519552-Gene Deletion,
pubmed-meshheading:10519552-Intracellular Membranes,
pubmed-meshheading:10519552-Ion Channels,
pubmed-meshheading:10519552-Membrane Proteins,
pubmed-meshheading:10519552-Membrane Transport Proteins,
pubmed-meshheading:10519552-Mitochondria,
pubmed-meshheading:10519552-Mitochondrial ADP, ATP Translocases,
pubmed-meshheading:10519552-Mitochondrial Membrane Transport Proteins,
pubmed-meshheading:10519552-Polymerase Chain Reaction,
pubmed-meshheading:10519552-Protein Binding,
pubmed-meshheading:10519552-Protein Precursors,
pubmed-meshheading:10519552-Receptors, Cell Surface,
pubmed-meshheading:10519552-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:10519552-Recombinant Fusion Proteins,
pubmed-meshheading:10519552-Saccharomyces cerevisiae,
pubmed-meshheading:10519552-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10519552-Spores, Fungal,
pubmed-meshheading:10519552-Tetrahydrofolate Dehydrogenase
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pubmed:year |
1999
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pubmed:articleTitle |
Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase.
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pubmed:affiliation |
Institute for Molecular Cell Biology, BioCentrum Amsterdam, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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