Transient States with Long-Term Effects on Pattern Formation

Protein patterning is vital for many cellular processes. A prototypical example is the bacterial Min system, where self-organized pole-to-pole oscillations of MinCDE proteins guide the cell division machinery to midcell. These oscillations are based on the cycling of the ATPase MinD and its activating protein MinE between the membrane and cytoplasm. Recent biochemical evidence suggests that MinE switches between a latent and reactive conformational state, dependent on MinD. Combining mathematical modeling and in vitro reconstitution of mutant proteins, we show that the MinD-dependent conformational switch of MinE is essential for patterns to emerge over a broad and physiological range of protein concentrations. Our results suggest that conformational switching of an ATPase activating protein can lead to the dynamic sequestration of its distinct functional states and thereby confer robustness to an intracellular protein network with vital roles in bacterial cell division.