Fine‐Tuning Protein Self‐Organization by Orthogonal Chemo‐Optogenetic Tools

A universal gain-of-function approach for the spatiotemporal control of protein activity is highly desirable when reconstituting biological modules in vitro. Here we used orthogonal translation with a photocaged amino acid to map and elucidate molecular mechanisms self-organization prokaryotic filamentous cell-division (FtsZ) that relevant assembly division ring bacteria. We masked tyrosine residue FtsZ by site-specific incorporation analogue. While mutant still shows self-assembly into filaments, dynamic patterns can no longer be observed. UV-mediated uncaging revealed 222 essential regulation protein's GTPase activity, self-organization, treadmilling dynamics. Thus, light-mediated functional appears promising minimal-regulation strategy building up complexity towards minimal cell.