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Voltage-coupled conformational dynamics of mitochondrial protein-import channel

Nature Structural & Molecular Biology volume 20, pages 915–917 (2013)Cite this article

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Mitochondria contain multisubunit translocases to import preproteins from the cytosol. The presequence translocase of the inner membrane operates in a voltage-gated manner, but how a preprotein-conducting channel responds to the membrane potential was unknown. A new study identifies a voltage-coupled conformational change in a transmembrane segment of the Tim23 import channel, representing a major step toward understanding the molecular basis of a voltage-gated protein translocase.

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Figure 1: The mitochondrial machinery for import of preproteins with positively charged presequences.
Figure 2: Molecular mechanism of the presequence translocase of the inner mitochondrial membrane (hypothetical model).

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Acknowledgements

We thank M. Bohnert and C. Mehnert for discussion. This work was supported by the Deutsche Forschungsgemeinschaft, Sonderforschungsbereich 746 and the Excellence Initiative of the German Federal and State Governments (EXC 294 BIOSS).

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Authors and Affiliations

  1. Martin van der Laan, Sandra G. Schrempp and Nikolaus Pfanner are at the Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, and the BIOSS Centre for Biological Signalling Studies, Universität Freiburg, Freiburg, Germany.,

    Martin van der Laan, Sandra G Schrempp & Nikolaus Pfanner

  2. Sandra G. Schrempp is also at the Fakultät für Biologie, Universität Freiburg, Freiburg, Germany.,

    Sandra G Schrempp

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  1. Martin van der Laan
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Correspondence to Martin van der Laan or Nikolaus Pfanner.

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van der Laan, M., Schrempp, S. & Pfanner, N. Voltage-coupled conformational dynamics of mitochondrial protein-import channel. Nat Struct Mol Biol 20, 915–917 (2013). https://doi.org/10.1038/nsmb.2643

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