Guiding divisome assembly and controlling its activity

Cell division in bacteria requires the construction of two new polar caps for the daughter cells. To constrict the cell membrane and build these new surface layers, bacteria employ a multiprotein machine called the divisome. Over the years, most of the essential division proteins have been identified and localized to the ring-like divisome apparatus. The challenge now is to determine the molecular function of these factors, how they cooperate to bring about the dramatic transformation of the mother cell envelope, and what coordinates their activity with other major cell cycle events. In this review, we discuss recent progress in these areas with an emphasis on results from the model organisms Escherichia coli and Bacillus subtilis.