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Mitochondrial sorting and assembly machinery operates by β-barrel switching

Author

Listed:
  • Hironori Takeda

    (Kyoto Sangyo University, Kamigamo-motoyama)

  • Akihisa Tsutsumi

    (The University of Tokyo)

  • Tomohiro Nishizawa

    (The University of Tokyo)

  • Caroline Lindau

    (University of Freiburg
    University of Freiburg)

  • Jon V. Busto

    (University of Freiburg)

  • Lena-Sophie Wenz

    (University of Freiburg
    Sanofi Deutschland GmbH)

  • Lars Ellenrieder

    (University of Freiburg
    Novartis Pharma AG)

  • Kenichiro Imai

    (National Institute of Advanced Industrial Science and Technology (AIST)
    National Institute of Advanced Industrial Science and Technology (AIST))

  • Sebastian P. Straub

    (University of Freiburg
    University of Freiburg
    Sanofi-Aventis (Suisse) ag)

  • Waltraut Mossmann

    (University of Freiburg)

  • Jian Qiu

    (University of Freiburg
    University of Freiburg
    Central South University)

  • Yu Yamamori

    (National Institute of Advanced Industrial Science and Technology (AIST))

  • Kentaro Tomii

    (National Institute of Advanced Industrial Science and Technology (AIST)
    National Institute of Advanced Industrial Science and Technology (AIST))

  • Junko Suzuki

    (Kyoto Sangyo University, Kamigamo-motoyama)

  • Takeshi Murata

    (Chiba University)

  • Satoshi Ogasawara

    (Chiba University)

  • Osamu Nureki

    (The University of Tokyo)

  • Thomas Becker

    (University of Freiburg
    University of Freiburg
    University of Freiburg
    Faculty of Medicine, University of Bonn)

  • Nikolaus Pfanner

    (University of Freiburg
    University of Freiburg
    University of Freiburg)

  • Nils Wiedemann

    (University of Freiburg
    University of Freiburg
    University of Freiburg)

  • Masahide Kikkawa

    (The University of Tokyo)

  • Toshiya Endo

    (Kyoto Sangyo University, Kamigamo-motoyama
    Kyoto Sangyo University, Kamigamo-motoyama)

Abstract

The mitochondrial outer membrane contains so-called β-barrel proteins, which allow communication between the cytosol and the mitochondrial interior1–3. Insertion of β-barrel proteins into the outer membrane is mediated by the multisubunit mitochondrial sorting and assembly machinery (SAM, also known as TOB)4–6. Here we use cryo-electron microscopy to determine the structures of two different forms of the yeast SAM complex at a resolution of 2.8–3.2 Å. The dimeric complex contains two copies of the β-barrel channel protein Sam50—Sam50a and Sam50b—with partially open lateral gates. The peripheral membrane proteins Sam35 and Sam37 cap the Sam50 channels from the cytosolic side, and are crucial for the structural and functional integrity of the dimeric complex. In the second complex, Sam50b is replaced by the β-barrel protein Mdm10. In cooperation with Sam50a, Sam37 recruits and traps Mdm10 by penetrating the interior of its laterally closed β-barrel from the cytosolic side. The substrate-loaded SAM complex contains one each of Sam50, Sam35 and Sam37, but neither Mdm10 nor a second Sam50, suggesting that Mdm10 and Sam50b function as placeholders for a β-barrel substrate released from Sam50a. Our proposed mechanism for dynamic switching of β-barrel subunits and substrate explains how entire precursor proteins can fold in association with the mitochondrial machinery for β-barrel assembly.

Suggested Citation

  • Hironori Takeda & Akihisa Tsutsumi & Tomohiro Nishizawa & Caroline Lindau & Jon V. Busto & Lena-Sophie Wenz & Lars Ellenrieder & Kenichiro Imai & Sebastian P. Straub & Waltraut Mossmann & Jian Qiu & Y, 2021. "Mitochondrial sorting and assembly machinery operates by β-barrel switching," Nature, Nature, vol. 590(7844), pages 163-169, February.
  • Handle: RePEc:nat:nature:v:590:y:2021:i:7844:d:10.1038_s41586-020-03113-7
    DOI: 10.1038/s41586-020-03113-7
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    Citations

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    Cited by:

    1. Xu Wang & Sarah B. Nyenhuis & Harris D. Bernstein, 2024. "The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Shelby K. Williams & Jon Jerlström Hultqvist & Yana Eglit & Dayana E. Salas-Leiva & Bruce Curtis & Russell J. S. Orr & Courtney W. Stairs & Tuğba N. Atalay & Naomi MacMillan & Alastair G. B. Simpson &, 2024. "Extreme mitochondrial reduction in a novel group of free-living metamonads," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Helene Jahn & Ladislav Bartoš & Grace I. Dearden & Jeremy S. Dittman & Joost C. M. Holthuis & Robert Vácha & Anant K. Menon, 2023. "Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    4. Sarah E. Hanson & Tyrone Dowdy & Mioara Larion & Matthew Thomas Doyle & Harris D. Bernstein, 2024. "The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    5. Peng Shi & Xiaoyu Ren & Jie Meng & Chenlu Kang & Yihe Wu & Yingxue Rong & Shujuan Zhao & Zhaodi Jiang & Ling Liang & Wanzhong He & Yuxin Yin & Xiangdong Li & Yong Liu & Xiaoshuai Huang & Yujie Sun & B, 2022. "Mechanical instability generated by Myosin 19 contributes to mitochondria cristae architecture and OXPHOS," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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