Role of the antiparallel double-stranded filament form of FtsA in activating the divisome.

The actin-like FtsA protein is essential for function of the cell division machinery, or divisome, in many bacteria including . Previous studies demonstrated that purified wild-type FtsA assembles into closed mini-rings on lipid membranes, but oligomeric variants of FtsA such as FtsA and FtsA can bypass certain divisome defects and form arc and double-stranded (DS) oligomeric states, respectively, which may reflect conversion of an inactive to an active form of FtsA. However, it remains unproven which oligomeric forms of FtsA are responsible for assembling and activating the divisome.

Role of the antiparallel double-stranded filament form of FtsA in activating the divisome.

The actin-like FtsA protein is essential for function of the cell division machinery, or divisome, in many bacteria including . Previous studies demonstrated that purified wild-type FtsA assembles into closed mini-rings on lipid membranes, but oligomeric variants of FtsA such as FtsA and FtsA can bypass certain divisome defects and form arc and double-stranded (DS) oligomeric states, respectively, which may reflect conversion of an inactive to an active form of FtsA. Yet, it remains unproven which oligomeric forms of FtsA are responsible for assembling and activating the divisome.