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Mitochondrial Hsp70/MIM44 complex facilitates protein import.

Nature | Oct 27, 1994

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.

Pubmed ID: 7935837 RIS Download

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