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Abstract

Bacterial cell division is arguably one of the most central processes in biology. Despite the identification of many important molecular players, surprisingly little is yet known about the underlying physicochemical mechanisms. However, self-organized protein patterns play key roles during division of Escherichia coli, where division is initiated by the directed localization of FtsZ to the cell middle by an inhibitor gradient arising from pole-to-pole oscillations of MinCDE proteins. In vitro reconstitution studies have established that both the Min system and FtsZ with its membrane adaptor FtsA form dynamic energy-dependent patterns on membranes. Furthermore, recent in vivo and in vitro approaches have shown that Min patterns display rich dynamics in diverse geometries and respond to the progress of cytokinesis.