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Science 18 November 1994:
Vol. 266. no. 5188, pp. 1250 - 1253
DOI: 10.1126/science.7973708

Articles

Science, Vol 266, Issue 5188, 1250-1253
Copyright © 1994 by American Association for the Advancement of Science


articles

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

C Ungermann, W Neupert, and DM Cyr

Institut fur Physiologische Chemie, Universitat Munchen, Germany.

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 mtHsp70 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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