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The structure of a 15-stranded actin-like filament from Clostridium botulinum

Author

Listed:
  • Fujiet Koh

    (Biopolis
    National University of Singapore)

  • Akihiro Narita

    (Nagoya University)

  • Lin Jie Lee

    (Biopolis
    National University of Singapore)

  • Kotaro Tanaka

    (Nagoya University
    Kyushu Institute of Technology)

  • Yong Zi Tan

    (Columbia University
    New York Structural Biology Center)

  • Venkata P. Dandey

    (New York Structural Biology Center)

  • David Popp

    (Biopolis
    Ebino)

  • Robert C. Robinson

    (Biopolis
    School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC)
    Okayama University)

Abstract

Microfilaments (actin) and microtubules represent the extremes in eukaryotic cytoskeleton cross-sectional dimensions, raising the question of whether filament architectures are limited by protein fold. Here, we report the cryoelectron microscopy structure of a complex filament formed from 15 protofilaments of an actin-like protein. This actin-like ParM is encoded on the large pCBH Clostridium botulinum plasmid. In cross-section, the ~26 nm diameter filament comprises a central helical protofilament surrounded by intermediate and outer layers of six and eight twisted protofilaments, respectively. Alternating polarity of the layers allows for similar lateral contacts between each layer. This filament design is stiffer than the actin filament, and has likely been selected for during evolution to move large cargos. The comparable sizes of microtubule and pCBH ParM filaments indicate that larger filament architectures are not limited by the protomer fold. Instead, function appears to have been the evolutionary driving force to produce broad, complex filaments.

Suggested Citation

  • Fujiet Koh & Akihiro Narita & Lin Jie Lee & Kotaro Tanaka & Yong Zi Tan & Venkata P. Dandey & David Popp & Robert C. Robinson, 2019. "The structure of a 15-stranded actin-like filament from Clostridium botulinum," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10779-9
    DOI: 10.1038/s41467-019-10779-9
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