Mitochondrial Hsp70/MIM44 complex facilitates protein import.
Protein translocation into mitochondria requires the mitochondrial protein Hsp70. This molecular chaperone of the mitochondrial matrix is recruited to the protein import machinery by MIM44, a component associated with the inner membrane of the mitochondria. Formation of the mt-Hsp70/MIM44 complex is regulated by ATP. MIM44 and mt-Hsp 70 interact in ... a sequential manner with incoming segments of unfolded preproteins and thereby facilitate stepwise vectorial translocation of proteins across the mitochondrial membranes. The complex appears to act as a molecular ratchet which is energetically driven by the hydrolysis of ATP.
Mesh Terms:
Adenosine Triphosphate, Base Sequence, Biological Transport, Carrier Proteins, Cross-Linking Reagents, DNA, HSP70 Heat-Shock Proteins, Intracellular Membranes, Membrane Proteins, Mitochondria, Mitochondrial Membrane Transport Proteins, Molecular Sequence Data, Mutation, Protein Precursors, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Succinimides, Tetrahydrofolate Dehydrogenase
Adenosine Triphosphate, Base Sequence, Biological Transport, Carrier Proteins, Cross-Linking Reagents, DNA, HSP70 Heat-Shock Proteins, Intracellular Membranes, Membrane Proteins, Mitochondria, Mitochondrial Membrane Transport Proteins, Molecular Sequence Data, Mutation, Protein Precursors, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Succinimides, Tetrahydrofolate Dehydrogenase
Nature
Date: Oct. 27, 1994
PubMed ID: 7935837
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