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J. Biol. Chem., Vol. 280, Issue 8, 6434-6440, February 25, 2005

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Assembly of the TOB Complex of Mitochondria^*

Shukry J. Habib, Thomas Waizenegger, Maciej Lech, Walter Neupert, and Doron Rapaport

From the Institut für Physiologische Chemie der Universität München, Butenandtstrasse 5, D-81377 Munich, Germany

All mitochondrial precursor proteins studied so far are recognized initially at the surface of the organelle by the translocase of the outer membrane (TOM complex). Precursors of -barrel proteins are transferred further to another complex in the outer membrane that mediates their topogenesis (TOB complex). Tob55 is an essential component of the TOB complex in that it constitutes the core element of the protein-conducting pore. The other two components of the TOB complex are Tob38, which builds a functional TOB core complex with Tob55, and Mas37, a peripheral member of the complex. We have investigated the biogenesis of the TOB complex. Reduced insertion of the Tob55 precursor in the absence of Tom20 and Tom70 argues for initial recognition of the precursor of Tob55 by the import receptors. Next, it is transferred through the import channel formed by Tom40. Variants of the latter protein influenced the insertion of Tob55. Assembly of newly synthesized Tob55 into preexisting TOB complexes, as analyzed by blue native gel electrophoresis, depended on Tob38 but did not require Mas37. Surprisingly, both the association of Mas37 precursor with mitochondria and its assembly into the TOB complex were not affected by mutation in the TOM complex. Mas37 assembled directly with the TOB core complex. Hence, the biogenesis of Mas37 represents a novel import pathway of mitochondrial proteins.

Received for publication, October 8, 2004 , and in revised form, November 30, 2004.

^* This work was supported by the Deutsche Forschungsgemeinschaft (to D. R.), Sonderforschungsbereich 594, the Fonds der Chemischen Industrie (to W. N.), and predoctoral fellowships from the Boehringer Ingelheim Fonds (to T. W.) and the Minerva Stiftung (to S. J. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Institut für Physiologische Chemie der Universität München, Butenandtstr. 5, Haus B, D-81377 Munich, Germany. Tel.: 49-89-2180-77128; Fax: 49-89-2180-77093; E-mail: rapaport{at}bio.med.uni-muenchen.de.

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