Journal
NATURE COMMUNICATIONS
Volume 12, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-021-26016-1
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Funding
- Deutsche Forschungsgemeinschaft [SFB1190, SFB860]
- Max Planck Society
- PhD program Molecular Biology-International Max Planck Research School
- Gottingen Graduate School for Neurosciences and Molecular Biosciences (GGNB)
- Boehringer Ingelheim Fonds
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy [EXC 2067/1- 390729940]
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The TOM and TIM23 complexes facilitate the transport of nuclear-encoded proteins into the mitochondrial matrix. By using a stalled client protein, the authors purified the translocation supercomplex and gained insights into the TOM-TIM23 interface and the mechanism of protein handover from the TOM to the TIM23 complex.
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. The TOM and TIM23 complexes facilitate the transport of nuclear-encoded proteins into the mitochondrial matrix. Here, the authors use a stalled client protein to purify the translocation supercomplex and gain insight into the TOM-TIM23 interface and the mechanism of protein handover from the TOM to the TIM23 complex.
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