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The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria

The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria

Science 266(5188): 1250-1253

ISSN/ISBN: 0036-8075

PMID: 7973708

DOI: 10.1126/science.7973708

The entry of segments of preproteins of defined lengths into the matrix space of mitochondria was studied. The mitochondrial chaperone Hsp70 (mtHsp70) interacted with proteins emerging from the protein import channel and stabilized translocation intermediates across the membranes in an adenosine triphosphate-dependent fashion. The chaperone bound to the presequence and mature parts of preproteins. In the absence of mtHsp 70 binding, preproteins with less than 30 to 40 residues in the matrix diffused out of mitochondria. Thus, protein translocation was reversible up to a late stage. The import channels in both mitochondrial membranes constitute a passive pore that interacts weakly with polypeptide chains entering the matrix.

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Accession: 009618428

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