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Journal Article

Signal recognition initiates reorganization of the presequence translocase during protein import.

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1739196.pdf
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Supplementary Material (public)

1739196_Suppl_1.doc
(Supplementary material), 4MB

Citation

Lytofchenko, O., Melin, J., Schulz, C., Kilisch, M., Hutu, D. P., & Rehling, P. (2013). Signal recognition initiates reorganization of the presequence translocase during protein import. EMBO Journal, 32(6), 886-898. doi:10.1038/emboj.2013.23.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000E-F735-1
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.