Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring.

Deprivation of FtsN, the last protein in the hierarchy of divisome assembly, causes the disassembly of other elements from the division ring, even extending to already assembled proto-ring proteins. Therefore the stability and function of the divisome to produce rings active in septation is not guaranteed until FtsN is recruited. Disassembly follows an inverse sequential pathway relative to assembly. In the absence of FtsN, the frequencies of FtsN and FtsQ rings are affected similarly. Among the proto-ring components, ZipA are more sensitive than FtsZ or FtsA rings. In contrast, removal of FtsZ leads to an almost simultaneous disappearance of the other elements from rings. Although restoration of FtsN allows for a quick reincorporation of ZipA into proto-rings, the de novo joint assembly of the three components when FtsZ levels are restored to FtsZ-deprived filaments is even faster. This suggests that the recruitment of ZipA into FtsZ-FtsA incomplete proto-rings may require first a period for the reversal of these partial assemblies.