Dynamic polarity control by a tunable protein oscillator in bacteria.

In bacteria, cell polarization involves the controlled targeting of specific proteins to the poles, defining polar identity and function. How a specific protein is targeted to one pole and what are the processes that facilitate its dynamic relocalization to the opposite pole is still unclear. The Myxococcus xanthus polarization example illustrates how the dynamic and asymmetric localization of polar proteins enable a controlled and fast switch of polarity. In M. xanthus, the opposing polar distribution of the small GTPase MglA and its cognate activating protein MglB defines the direction of movement of the cell. During a reversal event, the switch of direction is triggered by the Frz chemosensory system, which controls polarity reversals through a so-called gated relaxation oscillator. In this review, we discuss how this genetic architecture can provoke sharp behavioral transitions depending on Frz activation levels, which is central to multicellular behaviors in this bacterium.