Structure of the mitochondrial import gate reveals distinct preprotein paths

Yuhei Araiso, Akihisa Tsutsumi, Jian Qiu, Kenichiro Imai, Takuya Shiota, Jiyao Song, Caroline Lindau, Lena-Sophie Wenz, Haruka Sakaue, Kaori Yunoki, Shin Kawano, Junko Suzuki, Marilena Wischnewski, Conny Schütze, Hirotaka Ariyama, Toshio Ando, Thomas Becker, Trevor Lithgow, Nils Wiedemann, Nikolaus Pfanner, Masahide Kikkawa and Toshiya Endo ()
Additional contact information
Yuhei Araiso: Kyoto Sangyo University
Akihisa Tsutsumi: The University of Tokyo
Jian Qiu: University of Freiburg
Kenichiro Imai: National Institute of Advanced Industrial Science and Technology (AIST)
Takuya Shiota: Monash University
Jiyao Song: University of Freiburg
Caroline Lindau: University of Freiburg
Lena-Sophie Wenz: University of Freiburg
Haruka Sakaue: Kyoto Sangyo University
Kaori Yunoki: Kyoto Sangyo University
Shin Kawano: Kyoto Sangyo University
Junko Suzuki: Kyoto Sangyo University
Marilena Wischnewski: University of Freiburg
Conny Schütze: University of Freiburg
Hirotaka Ariyama: Kanazawa University
Toshio Ando: Kanazawa University
Thomas Becker: University of Freiburg
Trevor Lithgow: Monash University
Nils Wiedemann: University of Freiburg
Nikolaus Pfanner: University of Freiburg
Masahide Kikkawa: The University of Tokyo
Toshiya Endo: Kyoto Sangyo University

Nature, 2019, vol. 575, issue 7782, 395-401

Abstract: Abstract The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins1–4. Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex5–9 at 3.8-Å resolution. The structure reveals the high-resolution architecture of the translocator consisting of two Tom40 β-barrel channels and α-helical transmembrane subunits, providing insight into critical features that are conserved in all eukaryotes1–3. Each Tom40 β-barrel is surrounded by small TOM subunits, and tethered by two Tom22 subunits and one phospholipid. The N-terminal extension of Tom40 forms a helix inside the channel; mutational analysis reveals its dual role in early and late steps in the biogenesis of intermembrane-space proteins in cooperation with Tom5. Each Tom40 channel possesses two precursor exit sites. Tom22, Tom40 and Tom7 guide presequence-containing preproteins to the exit in the middle of the dimer, whereas Tom5 and the Tom40 N extension guide preproteins lacking a presequence to the exit at the periphery of the dimer.

Date: 2019
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DOI: 10.1038/s41586-019-1680-7

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