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  Mapping protein interactions in the active TOM-TIM23 supercomplex

Gomkale, R., Linden, A., Neumann, P., Schendzielorz, A. B., Stoldt, S., Dybkov, O., et al. (2021). Mapping protein interactions in the active TOM-TIM23 supercomplex. Nature Communications, 12: 5715. doi:10.1038/s41467-021-26016-1.

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 Creators:
Gomkale, R., Author
Linden, A.1, Author              
Neumann, P., Author
Schendzielorz, A. B., Author
Stoldt, S.2, Author              
Dybkov, O.3, Author              
Kilisch, M., Author
Schulz, C., Author
Cruz-Zaragoza, L. D., Author
Schwappach, B., Author
Ficner, R., Author
Jakobs, S.2, Author              
Urlaub, H.1, Author              
Rehling, P.4, Author              
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              
2Research Group of Mitochondrial Structure and Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578566              
3Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578576              
4Max Planck Fellow Peter Rehling, ou_1298545              

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Free keywords: Membrane proteins; Mitochondria; Mitochondrial proteins; Molecular modelling; Protein translocation
 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.

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Language(s): eng - English
 Dates: 2021-09-29
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-26016-1
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Title: Nature Communications
Source Genre: Journal
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Pages: 17 Volume / Issue: 12 Sequence Number: 5715 Start / End Page: - Identifier: ISSN: 2041-1723