Optical control of protein pattern formation
Patterns formed by protein reactions and diffusion are the foundation for many phenomena in biology. Yet, the experimental study of reaction-diffusion (R-D) systems has so far been dominated by chemical oscillators, for which many manipulation tools are available. Here, we developed a photoswitch for the Min system of Escherichia coli, a versatile biological in vitro R-D system consisting of the antagonistic proteins MinD and MinE. A MinE-derived peptide of 19 amino acids is covalently modified with a photoisomerizable crosslinker based on azobenzene to externally control peptide-mediated depletion of MinD from the membrane. In addition to providing an on-off switch for pattern formation, we achieve frequency-locked entrainment with a precise 2D spatial memory, allowing new insights into Min protein action on the membrane. Taken together, we provide a tool to externally control protein patterns formed by self-organization.
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