Reconstitution of the protein insertion machinery of the mitochondrial inner membrane.
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.
Mesh Terms:
Biological Transport, Active, Carrier Proteins, Chlorates, Detergents, Diffusion, Energy Metabolism, Fungal Proteins, Immunoglobulin G, Intracellular Membranes, Membrane Proteins, Membrane Transport Proteins, Mitochondria, Mitochondrial ADP, ATP Translocases, Proteolipids, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Solubility
Biological Transport, Active, Carrier Proteins, Chlorates, Detergents, Diffusion, Energy Metabolism, Fungal Proteins, Immunoglobulin G, Intracellular Membranes, Membrane Proteins, Membrane Transport Proteins, Mitochondria, Mitochondrial ADP, ATP Translocases, Proteolipids, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Solubility
EMBO J.
Date: Aug. 01, 1997
PubMed ID: 9303300
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