Abstract
We have reconstituted the protein insertion machinery of the yeast mitochondrial inner membrane into proteoliposomes. The reconstituted proteoliposomes have a distinct morphology and protein composition and correctly insert the ADP/ATP carrier (AAC) and Tim23p, two multi-spanning integral proteins of the mitochondrial inner membrane. The reconstituted system requires a membrane potential, but not Tim44p or mhsp70, both of which are required for the ATP-driven translocation of proteins into the matrix. The protein insertion machinery can thus operate independently of the energy-transducing Tim44p-mhsp70 complex.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Biological Transport, Active
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Carrier Proteins / antagonists & inhibitors
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Carrier Proteins / immunology
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Carrier Proteins / metabolism
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Chlorates / metabolism
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Detergents
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Diffusion
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Energy Metabolism
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Fungal Proteins / metabolism*
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Immunoglobulin G / pharmacology
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Intracellular Membranes / metabolism
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Membrane Proteins / antagonists & inhibitors
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Membrane Proteins / immunology
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Membrane Proteins / metabolism
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Membrane Transport Proteins*
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Mitochondria / metabolism*
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Mitochondrial ADP, ATP Translocases / metabolism
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Mitochondrial Precursor Protein Import Complex Proteins
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Proteolipids / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins*
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Solubility
Substances
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Carrier Proteins
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Chlorates
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Detergents
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Fungal Proteins
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Immunoglobulin G
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Membrane Proteins
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Membrane Transport Proteins
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Mitochondrial Precursor Protein Import Complex Proteins
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Proteolipids
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Saccharomyces cerevisiae Proteins
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TIM23 protein, S cerevisiae
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proteoliposomes
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Mitochondrial ADP, ATP Translocases