Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China; Life Sciences Institute, Zheijiang University, Hangzhou, China
Jiayu Yu
The State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China
Jie Yu
Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China; Life Sciences Institute, Zheijiang University, Hangzhou, China
Yang Liu
The State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China
Ying Li
Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China
Xin-Hua Feng
Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China; Life Sciences Institute, Zheijiang University, Hangzhou, China
Kerwyn Casey Huang
Department of Bioengineering, Stanford University, Stanford, United States; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, United States; Chan Zuckerberg Biohub, San Francisco, United States
Zengyi Chang
The State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China
The prokaryotic tubulin homolog FtsZ polymerizes into protofilaments, which further assemble into higher-order structures at future division sites to form the Z-ring, a dynamic structure essential for bacterial cell division. The precise nature of interactions between FtsZ protofilaments that organize the Z-ring and their physiological significance remain enigmatic. In this study, we solved two crystallographic structures of a pair of FtsZ protofilaments, and demonstrated that they assemble in an antiparallel manner through the formation of two different inter-protofilament lateral interfaces. Our in vivo photocrosslinking studies confirmed that such lateral interactions occur in living cells, and disruption of the lateral interactions rendered cells unable to divide. The inherently weak lateral interactions enable FtsZ protofilaments to self-organize into a dynamic Z-ring. These results have fundamental implications for our understanding of bacterial cell division and for developing antibiotics that target this key process.
