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Originally published In Press as doi:10.1074/jbc.M202310200 on July 22, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36100-36108, September 27, 2002
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Assembly of Tim9 and Tim10 into a Functional Chaperone*

Sarah VialDagger §, Hui LuDagger , Scott AllenDagger , Peter SavoryDagger , David Thornton||, John Sheehan||**, and Kostas TokatlidisDagger Dagger Dagger §§

From the Dagger  School of Biological Sciences and || The Wellcome Trust Centre for Cell Matrix Research, University of Manchester, Manchester M13 9PT, United Kingdom and the §§ Department of Chemistry, University of Crete and Institute of Molecular Biology and Biotechnology, Heraklion, Greece

The TIM10 complex is localized in the mitochondrial intermembrane space and mediates insertion of hydrophobic proteins at the inner membrane. We have characterized TIM10 assembly and analyzed the structural properties of its subunits, Tim9 and Tim10. Both proteins are alpha -helical with a protease-resistant central domain, and each self-associates to form mainly dimers and trimers in solution. Tim9 and Tim10 bound to one another with submicromolar affinity in equimolar amounts and assembled in a stable, significantly extended complex that was indistinguishable from the native mitochondrial TIM10 complex. Importantly, the reconstituted TIM10 complex is functional because it bound to the physiological substrate ADP/ATP carrier and displayed chaperone activity in refolding the model substrate firefly luciferase. These data demonstrate that the individual subunits can exist as independent, dynamically self-associating proteins. Assembly into the thermodynamically stable hexameric complex is necessary for the TIM10 chaperone function.

* This work was supported in part by the Wellcome Trust and a Medical Research Council cooperative group grant (to K. T. and J. S.) and by the UK Medical Research Council and the UK Biotechnology and Biological Sciences Research Council (to K. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a European Union Marie Curie postdoctoral fellowship.

Supported by a Biotechnology and Biological Sciences Research Council studentship.

** Present address: Thurston Bowles Bldg., University of North Carolina, Chapel Hill, NC 27514.

Dagger Dagger Lister Institute Research Fellow. To whom correspondence should be addressed: School of Biological Sciences, University of Manchester, 2.205 Stopford Bldg., Oxford Rd., Manchester M13 9PT, UK. Tel.: 44-161-275-5687; Fax: 44-161-275-5082; E-mail: tokatlidis@man.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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