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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.

Pubmed ID: 7935837

Authors

  • Schneider HC
  • Berthold J
  • Bauer MF
  • Dietmeier K
  • Guiard B
  • Brunner M
  • Neupert W

Journal

Nature

Publication Data

October 27, 1994

Associated Grants

None

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