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Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody

Author

Listed:
  • Junso Fujita

    (Osaka University
    Osaka University
    Osaka University)

  • Hiroshi Amesaka

    (Kyoto Prefectural University)

  • Takuya Yoshizawa

    (Ritsumeikan University)

  • Kota Hibino

    (Ritsumeikan University)

  • Natsuki Kamimura

    (Ritsumeikan University)

  • Natsuko Kuroda

    (Ritsumeikan University)

  • Takamoto Konishi

    (Ritsumeikan University)

  • Yuki Kato

    (Ritsumeikan University)

  • Mizuho Hara

    (Kyoto Prefectural University)

  • Tsuyoshi Inoue

    (Osaka University
    Osaka University
    dotAqua Inc.)

  • Keiichi Namba

    (Osaka University
    Osaka University
    RIKEN Center for Biosystems Dynamics Research and SPring-8 Center)

  • Shun-ichi Tanaka

    (Kyoto Prefectural University)

  • Hiroyoshi Matsumura

    (Ritsumeikan University)

Abstract

FtsZ polymerizes into protofilaments to form the Z-ring that acts as a scaffold for accessory proteins during cell division. Structures of FtsZ have been previously solved, but detailed mechanistic insights are lacking. Here, we determine the cryoEM structure of a single protofilament of FtsZ from Klebsiella pneumoniae (KpFtsZ) in a polymerization-preferred conformation. We also develop a monobody (Mb) that binds to KpFtsZ and FtsZ from Escherichia coli without affecting their GTPase activity. Crystal structures of the FtsZ–Mb complexes reveal the Mb binding mode, while addition of Mb in vivo inhibits cell division. A cryoEM structure of a double-helical tube of KpFtsZ–Mb at 2.7 Å resolution shows two parallel protofilaments. Our present study highlights the physiological roles of the conformational changes of FtsZ in treadmilling that regulate cell division.

Suggested Citation

  • Junso Fujita & Hiroshi Amesaka & Takuya Yoshizawa & Kota Hibino & Natsuki Kamimura & Natsuko Kuroda & Takamoto Konishi & Yuki Kato & Mizuho Hara & Tsuyoshi Inoue & Keiichi Namba & Shun-ichi Tanaka & H, 2023. "Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39807-5
    DOI: 10.1038/s41467-023-39807-5
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    References listed on IDEAS

    as
    1. Joshua W. McCausland & Xinxing Yang & Georgia R. Squyres & Zhixin Lyu & Kevin E. Bruce & Melissa M. Lamanna & Bill Söderström & Ethan C. Garner & Malcolm E. Winkler & Jie Xiao & Jian Liu, 2021. "Treadmilling FtsZ polymers drive the directional movement of sPG-synthesis enzymes via a Brownian ratchet mechanism," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    2. Jan Löwe & Linda A. Amos, 1998. "Crystal structure of the bacterial cell-division protein FtsZ," Nature, Nature, vol. 391(6663), pages 203-206, January.
    3. Kevin D. Whitley & Calum Jukes & Nicholas Tregidgo & Eleni Karinou & Pedro Almada & Yann Cesbron & Ricardo Henriques & Cees Dekker & Séamus Holden, 2021. "FtsZ treadmilling is essential for Z-ring condensation and septal constriction initiation in Bacillus subtilis cell division," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
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