Abstract
Most of our knowledge regarding the process of protein import into mitochondria has come from research employing Saccharomyces cerevisiae as a model system. Recently, several mammalian homologues of the mitochondrial motor proteins were identified. Of particular interest for us is the human Tim14/Pam18-Tim16/Pam16 complex. We chose a structural approach in order to examine the evolutionary conservation between yeast Tim14/Pam18-Tim16/Pam16 proteins and their human homologues. For this purpose, we examined the structural properties of the purified human proteins and their interaction with their yeast homologues, in vitro. Our results show that the soluble domains of the human Tim14/Pam18 and Tim16/Pam16 proteins interact with their yeast counterparts, forming heterodimeric complexes and that these complexes interact with yeast mtHsp70.
Keywords:
Tim14 (also known as Pam18); Tim16 (also known as Pam16); mtHsp70; translocation motor.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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HSP70 Heat-Shock Proteins / metabolism*
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Humans
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Membrane Transport Proteins / metabolism*
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Mitochondria / metabolism
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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 / metabolism
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Mitochondrial Proteins / pharmacokinetics*
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Mitochondrial Proton-Translocating ATPases / metabolism
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Protein Structure, Secondary
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Protein Transport
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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HSP70 Heat-Shock 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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Pam16 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Tim14 protein, S cerevisiae
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Mitochondrial Proton-Translocating ATPases