Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.

ABSTRACT: Cell division in Escherichia coli relies on the Z ring, a cytoskeletal structure that acts as a scaffold for the assembly of the divisome. To date, the detailed mechanisms underlying the assembly and stabilization of the Z ring remain elusive. This study highlights the role of the FtsZ-associated protein (Zap) ZapD in the assembly and stabilization of Z-ring-like structures via filament crosslinking. Using cryo-electron tomography and biochemical analysis, we show that, at equimolar concentrations of ZapD and FtsZ, ZapD induces the formation of toroidal structures composed of short, curved FtsZ filaments that are crosslinked vertically, but also laterally and diagonally. At higher concentrations of ZapD, regularly spaced ZapD dimers crosslink FtsZ filaments from above, resulting in

SUBMITTER: Merino-Salomon A 

PROVIDER: S-EPMC12435895 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature