
In most bacteria, cytokinesis is initiated at midcell by a dynamic ring formed by the tubulin-homolog, FtsZ, called the Z-ring. The Z-ring establishes the division site and creates an essential framework for the recruitment of a multi-protein division machinery at midcell. Furthermore, treadmilling FtsZ filaments contribute to cell wall synthesis around the division plane. A number of proteins bind FtsZ and regulate the architectural stability of the Z-ring during the bacterial cell cycle. Yet the precise molecular interactions of the FtsZ-associated proteins with FtsZ that allow the formation of a stable yet dynamic Z-ring at midcell are not completely understood. Using E. coli, we aim to address the underlying mechanisms that govern the robustness of cell division.