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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2002-8-22
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pubmed:abstractText |
Most mitochondrial proteins are synthesized in the cytosol as precursor proteins and are imported into mitochondria. The targeting signals for mitochondria are encoded in the presequences or in the mature parts of the precursor proteins, and are decoded by the receptor sites in the translocator complex in the mitochondrial outer membrane. The recently determined NMR structure of the general import receptor Tom20 in a complex with a presequence peptide reveals that, although the amphiphilicity and positive charges of the presequence is essential for the import ability of the presequence, Tom20 recognizes only the amphiphilicity, but not the positive charges. This leads to a new model that different features associated with the mitochondrial targeting sequence of the precursor protein can be recognized by the mitochondrial protein import system in different steps during the import.
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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/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Membrane Transport...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
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/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/TOM5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/TOM70 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/TOM71 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
1592
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3-14
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pubmed:dateRevised |
2009-7-28
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pubmed:meshHeading |
pubmed-meshheading:12191763-Amino Acid Sequence,
pubmed-meshheading:12191763-Animals,
pubmed-meshheading:12191763-Binding Sites,
pubmed-meshheading:12191763-Carrier Proteins,
pubmed-meshheading:12191763-Fungal Proteins,
pubmed-meshheading:12191763-Intracellular Membranes,
pubmed-meshheading:12191763-Magnetic Resonance Spectroscopy,
pubmed-meshheading:12191763-Membrane Proteins,
pubmed-meshheading:12191763-Membrane Transport Proteins,
pubmed-meshheading:12191763-Mitochondria,
pubmed-meshheading:12191763-Mitochondrial Membrane Transport Proteins,
pubmed-meshheading:12191763-Mitochondrial Proteins,
pubmed-meshheading:12191763-Models, Molecular,
pubmed-meshheading:12191763-Molecular Sequence Data,
pubmed-meshheading:12191763-Protein Precursors,
pubmed-meshheading:12191763-Protein Transport,
pubmed-meshheading:12191763-Receptors, Cell Surface,
pubmed-meshheading:12191763-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:12191763-Saccharomyces cerevisiae Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Functions of outer membrane receptors in mitochondrial protein import.
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pubmed:affiliation |
Department of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya, 464-8602, Japan. endo@biochem.chem.nagoya-u.ac.jp
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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