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Signal recognition initiates reorganization of the presequence translocase during protein import |
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| Authors: | Oleksandr Lytovchenko Jonathan Melin Christian Schulz Markus Kilisch Dana P Hutu Peter Rehling |
| Institution: | 1. Department of Biochemistry II, University of G?ttingen, , G?ttingen, Germany;2. Department of Biochemistry I, University of G?ttingen, , G?ttingen, Germany;3. Institute for Biochemistry and Molecular Biology, Center for Biochemistry and Molecular Cell Science, University of Freiburg, , Freiburg, Germany;4. Max‐Planck Institute for Biophysical Chemistry, , G?ttingen, Germany |
| Abstract: | The mitochondrial presequence translocase interacts with presequence‐containing precursors at the intermembrane space (IMS) side of the inner membrane to mediate their translocation into the matrix. Little is known as too how these matrix‐targeting signals activate the translocase in order to initiate precursor transport. Therefore, we analysed how signal recognition by the presequence translocase initiates reorganization among Tim‐proteins during import. Our analyses revealed that the presequence receptor Tim50 interacts with Tim21 in a signal‐sensitive manner in a process that involves the IMS‐domain of the Tim23 channel. The signal‐driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor‐associated form of the TIM23 complex required for matrix transport. |
| Keywords: | import mitochondria presequence TIM23 complex |