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Araiso, Yuhei; Tsutsumi, Akihisa; Qiu, Jian; Imai, Kenichiro; Shiota, Takuya; Song, Jiyao; Lindau, Caroline; Wenz, Lena-Sophie; Sakaue, Haruka; Yunoki, Kaori; Kawano, Shin; Suzuki, Junko; Wischnewski, Marilena; Schütze, Conny; Ariyama, Hirotaka; Ando, Toshio; Becker, Thomas; Lithgow, Trevor; Wiedemann, Nils; Pfanner, Nikolaus; Kikkawa, Masahide; Endo, Toshiya
Nature (London), 11/2019, Volume: 575, Issue: 7782Journal Article
The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins . Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex 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 eukaryotes . 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.
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