Protein translocation into mitochondria requires the mitochondrial pro
tein Hsp70. This molecular chaperone of the mitochondrial matrix is re
cruited to the protein import machinery by MIM44, a component associat
ed with the inner membrane of the mitochondria. Formation of the mt-Hs
p70/MIM44 complex is regulated by ATP. MIM44 and mt-Hsp70 interact in
a sequential manner with incoming segments of unfolded preproteins and
thereby facilitate stepwise vectorial translocation of proteins acros
s the mitochondrial membranes. The complex appears to act as a molecul
ar ratchet which is energetically driven by the hydrolysis of ATP.