The Program for the R-GIRO Research from the Ritsumeikan Global Innovation Research Organization, Ritsumeikan University
日本
JEOL YOKOGUSHI Research Alliance Laboratories of Osaka University
日本
The Cooperative Research Program of the Institute for Protein Research, Osaka University
CR-22-02
日本
The Cooperative Research Program of the Institute for Protein Research, Osaka University
CR-23-02
日本
引用
ジャーナル: Nat Commun / 年: 2025 タイトル: Structural basis for the interaction between the bacterial cell division proteins FtsZ and ZapA. 著者: Junso Fujita / Kazuki Kasai / Kota Hibino / Gota Kagoshima / Natsuki Kamimura / Shungo Tobita / Yuki Kato / Ryo Uehara / Keiichi Namba / Takayuki Uchihashi / Hiroyoshi Matsumura / 要旨: 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 ...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.