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Structural basis for the interaction between the bacterial cell division proteins FtsZ and ZapA

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  • Junso Fujita

    (University of Osaka
    University of Osaka
    University of Osaka)

  • Kazuki Kasai

    (University of Osaka
    University of Osaka)

  • Kota Hibino

    (Ritsumeikan University)

  • Gota Kagoshima

    (Nagoya University)

  • Natsuki Kamimura

    (Ritsumeikan University)

  • Shungo Tobita

    (Ritsumeikan University)

  • Yuki Kato

    (Ritsumeikan University)

  • Ryo Uehara

    (Ritsumeikan University)

  • Keiichi Namba

    (University of Osaka
    University of Osaka)

  • Takayuki Uchihashi

    (Nagoya University
    National Institutes of Natural Sciences
    Nagoya University)

  • Hiroyoshi Matsumura

    (Ritsumeikan University)

Abstract

Cell division in most bacteria is regulated by the tubulin homolog FtsZ as well as ZapA, a FtsZ-associated protein. However, how FtsZ and ZapA function coordinately has remained elusive. Here we report the cryo-electron microscopy structure of the ZapA-FtsZ complex at 2.73 Å resolution. The complex forms an asymmetric ladder-like structure, in which the double antiparallel FtsZ protofilament on one side and a single protofilament on the other side are tethered by ZapA tetramers. In the complex, the extensive interactions of FtsZ with ZapA cause a structural change of the FtsZ protofilament, and the formation of the double FtsZ protofilament increases electrostatic repulsion. High-speed atomic force microscopy analysis revealed cooperative interactions of ZapA with FtsZ at a molecular level. Our findings not only provide a structural basis for the interaction between FtsZ and ZapA but also shed light on how ZapA binds to FtsZ protofilaments without disturbing FtsZ dynamics to promote cell division.

Suggested Citation

  • Junso Fujita & Kazuki Kasai & Kota Hibino & Gota Kagoshima & Natsuki Kamimura & Shungo Tobita & Yuki Kato & Ryo Uehara & Keiichi Namba & Takayuki Uchihashi & Hiroyoshi Matsumura, 2025. "Structural basis for the interaction between the bacterial cell division proteins FtsZ and ZapA," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60940-w
    DOI: 10.1038/s41467-025-60940-w
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