MinE conformational switching confers robustness on self-organized Min protein patterns
Many fundamental cellular processes are spatially regulated by self-organized protein patterns, which are often based on nucleotide-binding proteins that switch their nucleotide state upon interaction with a second, activating protein. For reliable function, these protein patterns must be robust against parameter changes, although the basis for such robustness is generally elusive. Here, we take a combined theoretical and experimental approach to the E. coli Min system, a paradigmatic system for protein self-organization.
By mathematical modeling and in vitro reconstitution of mutant proteins, we demonstrate that the robustness of pattern formation is dramatically enhanced by an interlinked functional switching of both proteins, rather than one. Such interlinked functional switching could be a generic means of obtaining robustness in biological pattern-forming systems.