Abstract
The small Tims are chaperones that facilitate insertion of hydrophobic precursors into the inner mitochondrial membrane. We purified Tim12 and found it forms dimers that bind to Tim9. In this interaction, Tim12 undergoes structural changes that may be important for transport of its substrates in the mitochondrial carrier import pathway.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Biological Transport
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Dimerization
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Membrane Proteins / chemistry
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism*
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Membrane Transport Proteins / chemistry
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Membrane Transport Proteins / isolation & purification
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Membrane Transport Proteins / metabolism*
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Mitochondria / metabolism
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Mitochondrial Membrane Transport Proteins / chemistry
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Mitochondrial Membrane Transport Proteins / isolation & purification
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Mitochondrial Membrane Transport Proteins / metabolism*
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Mitochondrial Membranes / metabolism
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Mitochondrial Precursor Protein Import Complex Proteins
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Mitochondrial Proteins / chemistry
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Mitochondrial Proteins / isolation & purification
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Mitochondrial Proteins / metabolism*
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Molecular Chaperones / metabolism
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Protein Subunits / chemistry
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Protein Subunits / metabolism
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Recombinant Proteins / biosynthesis
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / isolation & purification
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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Membrane Proteins
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Membrane Transport Proteins
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Mitochondrial Membrane Transport Proteins
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Mitochondrial Precursor Protein Import Complex Proteins
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Mitochondrial Proteins
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Molecular Chaperones
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Protein Subunits
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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TIM12 protein, S cerevisiae
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Tim9 protein, S cerevisiae