Cookies Disclaimer

OK Our site saves small pieces of text information (cookies) on your device in order to deliver better content and for statistical purposes. You can disable the usage of cookies by changing the settings of your browser. By browsing our website without changing the browser settings you grant us permission to store that information on your device.


Bibliographic Data

  • Authors: Gomkale R., Linden A., Neumann P., Schendzielorz A.B., Stoldt S., Dybkov O., Kilisch M., Schulz C., Cruz-Zaragoza L.D., Schwappach B., Ficner R., Jakobs S., Urlaub H., Rehling P.
  • Title: Mapping protein interactions in the active TOM-TIM23 supercomplex
  • Journal: Nature Communications
  • Volume: 12
  • Volume: 5715
  • DOI: 10.1038/s41467-021-26016-1


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.