Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5

Christian Sirrenberg, Maxi Endres, Heike Fölsch, Rosemary A. Stuart, Walter Neupert () and Michael Brunner
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Christian Sirrenberg: Institut für Physiologische Chemie der Universität München
Maxi Endres: Institut für Physiologische Chemie der Universität München
Heike Fölsch: Institut für Physiologische Chemie der Universität München
Rosemary A. Stuart: Institut für Physiologische Chemie der Universität München
Walter Neupert: Institut für Physiologische Chemie der Universität München
Michael Brunner: Institut für Physiologische Chemie der Universität München

Nature, 1998, vol. 391, issue 6670, 912-915

Abstract: Abstract Import of nuclear-encoded precursor proteins into mitochondria and their subsequent sorting into mitochondrial subcompartments is mediated by translocase enzymes in the mitochondrial outer and inner membranes1,2,3. Precursor proteins carrying amino-terminal targeting signals are translocated into the matrix by the integral inner membrane proteins Tim23 and Tim17 in cooperation with Tim44 and mitochondrial Hsp70 (4-7). We describe here the discovery of a new pathway for the transport of members of the mitochondrial carrier family and other inner membrane proteins that contain internal targeting signals. Two related proteins in the intermembrane space, Tim10/Mrs11 (ref. 8) and Tim12/Mrs5 (ref. 9), interact sequentially with these precursors and facilitate their translocation across the outer membrane, irrespective of the membrane potential. Tim10 and Tim12 are found in a complex with Tim22, which takes over the precursor and mediates its membrane-potential-dependent insertion into the inner membrane. This interaction of Tim10 and Tim12 with the precursors depends on the presence of divalent metal ions. Both proteins contain a zinc-finger-like motif with four cysteines and bind equimolar amounts of zinc ions.

Date: 1998
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DOI: 10.1038/36136

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