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

Junso Fujita, Kazuki Kasai, Kota Hibino, Gota Kagoshima, Natsuki Kamimura, Shungo Tobita, Yuki Kato, Ryo Uehara, Keiichi Namba, Takayuki Uchihashi () and Hiroyoshi Matsumura ()
Additional contact information
Junso Fujita: University of Osaka
Kazuki Kasai: 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
Takayuki Uchihashi: Nagoya University
Hiroyoshi Matsumura: Ritsumeikan University

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: 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.

Date: 2025
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-60940-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60940-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-60940-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().