Abstract
Z-ring is a ring-shaped machinery which consists of FtsZ. The E.coli cell replication and division would occur after the Z-ring formation. Deficient Z-ring formation can block the cell division. FtsA and ZipA are the two proteins that attach the Z-ring to the cell membrane, make the Z-ring stable and recruit the downstream proteins to the Z-ring. FtsA can also strongly self–interact with each other. It has been proposed that the FtsA self-interaction regulates late division steps. The ObgE is a conserved GTPase critical for the survival and the growth of E.coli cells. With the depletion of ObgE, cells will filament and have more or none Z-rings, suggesting that ObgE can affect the Z-ring assembly. ObgE also shows the functions that are similar to the replication checkpoint in Eukaryotes. We hypothesize that ObgE is responsible for the conversion between the FtsA monomers and FtsA oligomers. We used the yeast two hybrid system, the split-GFP technique and the cell length measurement to confirm the prediction of this hypothesis. Consequently we believe that ObgE does influence the FtsA and regulate the FtsA monomer oligomer conversion. ObgE may have other important roles in addition to this function of the cell division checkpoint.