The essential function of Tim12 in vivo is ensured by the assembly interactions of its C-terminal domain

Lionaki, E., de Marcos Lousa, C., Baud, C., Vougioukalaki, M., Panayotou, G. and Tokatlidis, K. (2008) The essential function of Tim12 in vivo is ensured by the assembly interactions of its C-terminal domain. Journal of Biological Chemistry, 283(23), pp. 15747-15753. (doi:10.1074/jbc.M800350200)

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Abstract

The small Tims chaperone hydrophobic precursors across the mitochondrial intermembrane space. Tim9 and Tim10 form the soluble TIM10 complex that binds precursors exiting from the outer membrane. Tim12 functions downstream, as the only small Tim peripherally attached on the inner membrane. We show that Tim12 has an intrinsic affinity for inner mitochondrial membrane lipids, in contrast to the other small Tims. We find that the C-terminal end of Tim12 is essential in vivo. Its deletion crucially abolishes assembly of Tim12 in complexes with the other Tims. The N-terminal end contains targeting information and also mediates direct binding of Tim12 to the transmembrane segments of the carrier substrates. These results provide a molecular basis for the concept that the essential role of Tim12 relies on its unique assembly properties that allow this subunit to bridge the soluble and membrane-embedded translocases in the carrier import pathway.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Tokatlidis, Professor Kostas
Authors: Lionaki, E., de Marcos Lousa, C., Baud, C., Vougioukalaki, M., Panayotou, G., and Tokatlidis, K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology, Inc.
ISSN:0021-9258

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