Abstract
The majority of mitochondrial proteins are targeted to mitochondria by N-terminal presequences and use the TIM23 complex for their translocation across the mitochondrial inner membrane. During import, translocation through the channel in the inner membrane is coupled to the ATP-dependent action of an Hsp70-based import motor at the matrix face. How these two processes are coordinated remained unclear. We show here that the two domain structure of Tim44 plays a central role in this process. The N-terminal domain of Tim44 interacts with the components of the import motor whereas its C-terminal domain interacts with the translocation channel and is in contact with translocating proteins. Our data suggest that the translocation channel and the import motor of the TIM23 complex communicate through rearrangements of the two domains of Tim44 that are stimulated by translocating proteins.
Article and author information
Author details
Reviewing Editor
- Nikolaus Pfanner, Univ. of Freiburg, Germany
Publication history
- Received: September 26, 2015
- Accepted: December 28, 2015
- Accepted Manuscript published: December 29, 2015 (version 1)
- Version of Record published: February 1, 2016 (version 2)
Copyright
© 2015, Banerjee et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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