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Electron cryo-microscopy reveals the structure of the archaeal thread filament

Author

Listed:
  • Matthew C. Gaines

    (University of Exeter
    Faculty of Health and Life Sciences)

  • Michail N. Isupov

    (Faculty of Health and Life Sciences, University of Exeter)

  • Shamphavi Sivabalasarma

    (University of Freiburg
    University of Freiburg)

  • Risat Ul Haque

    (University of Exeter
    Faculty of Health and Life Sciences)

  • Mathew McLaren

    (University of Exeter
    Faculty of Health and Life Sciences)

  • Clara L. Mollat

    (University of Freiburg)

  • Patrick Tripp

    (University of Freiburg)

  • Alexander Neuhaus

    (University of Exeter
    Faculty of Health and Life Sciences)

  • Vicki A. M. Gold

    (University of Exeter
    Faculty of Health and Life Sciences)

  • Sonja-Verena Albers

    (University of Freiburg
    University of Freiburg
    Faculty of Biology, University of Freiburg)

  • Bertram Daum

    (University of Exeter
    Faculty of Health and Life Sciences)

Abstract

Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named “thread”. Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism.

Suggested Citation

  • Matthew C. Gaines & Michail N. Isupov & Shamphavi Sivabalasarma & Risat Ul Haque & Mathew McLaren & Clara L. Mollat & Patrick Tripp & Alexander Neuhaus & Vicki A. M. Gold & Sonja-Verena Albers & Bertr, 2022. "Electron cryo-microscopy reveals the structure of the archaeal thread filament," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34652-4
    DOI: 10.1038/s41467-022-34652-4
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    References listed on IDEAS

    as
    1. Alvaro Alonso-Caballero & Jörg Schönfelder & Simon Poly & Fabiano Corsetti & David Sancho & Emilio Artacho & Raul Perez-Jimenez, 2018. "Mechanical architecture and folding of E. coli type 1 pilus domains," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    2. Minge Du & Zuanning Yuan & Glenn T. Werneburg & Nadine S. Henderson & Hemil Chauhan & Amanda Kovach & Gongpu Zhao & Jessica Johl & Huilin Li & David G. Thanassi, 2021. "Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    3. Alexander Neuhaus & Muniyandi Selvaraj & Ralf Salzer & Julian D. Langer & Kerstin Kruse & Lennart Kirchner & Kelly Sanders & Bertram Daum & Beate Averhoff & Vicki A. M. Gold, 2020. "Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    4. Michael Vetsch & Chasper Puorger & Thomas Spirig & Ulla Grauschopf & Eilika U. Weber-Ban & Rudi Glockshuber, 2004. "Pilus chaperones represent a new type of protein-folding catalyst," Nature, Nature, vol. 431(7006), pages 329-333, September.
    5. Fengbin Wang & Diana P. Baquero & Zhangli Su & Leticia C. Beltran & David Prangishvili & Mart Krupovic & Edward H. Egelman, 2020. "The structures of two archaeal type IV pili illuminate evolutionary relationships," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
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