Mapping protein interactions in the active TOM-TIM23 supercomplex

Ridhima Gomkale, Andreas Linden, Piotr Neumann, Alexander Benjamin Schendzielorz, Stefan Stoldt, Olexandr Dybkov, Markus Kilisch, Christian Schulz, Luis Daniel Cruz-Zaragoza, Blanche Schwappach, Ralf Ficner, Stefan Jakobs, Henning Urlaub and Peter Rehling ()
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Ridhima Gomkale: University Medical Center Göttingen
Andreas Linden: University Medical Center Göttingen
Piotr Neumann: Georg-August-Universität Göttingen
Alexander Benjamin Schendzielorz: University Medical Center Göttingen
Stefan Stoldt: Max Planck Institute for Biophysical Chemistry
Olexandr Dybkov: Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry
Markus Kilisch: University Medical Center Göttingen
Christian Schulz: University Medical Center Göttingen
Luis Daniel Cruz-Zaragoza: University Medical Center Göttingen
Blanche Schwappach: University Medical Center Göttingen
Ralf Ficner: Georg-August-Universität Göttingen
Stefan Jakobs: Max Planck Institute for Biophysical Chemistry
Henning Urlaub: University Medical Center Göttingen
Peter Rehling: University Medical Center Göttingen

Nature Communications, 2021, vol. 12, issue 1, 1-17

Abstract: Abstract Nuclear-encoded mitochondrial proteins destined for the matrix have to be transported across two membranes. The TOM and TIM23 complexes facilitate the transport of precursor proteins with N-terminal targeting signals into the matrix. During transport, precursors are recognized by the TIM23 complex in the inner membrane for handover from the TOM complex. However, we have little knowledge on the organization of the TOM-TIM23 transition zone and on how precursor transfer between the translocases occurs. Here, we have designed a precursor protein that is stalled during matrix transport in a TOM-TIM23-spanning manner and enables purification of the translocation intermediate. Combining chemical cross-linking with mass spectrometric analyses and structural modeling allows us to map the molecular environment of the intermembrane space interface of TOM and TIM23 as well as the import motor interactions with amino acid resolution. Our analyses provide a framework for understanding presequence handover and translocation during matrix protein transport.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26016-1

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DOI: 10.1038/s41467-021-26016-1

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