Tyrosine phosphorylation-dependent localization of TmaR that controls activity of a major bacterial sugar regulator by polar sequestration
Tamar Szoke, Nitsan Albocher, Sutharsan Govindarajan, Anat Nussbaum‐Shochat, Orna Amster‐Choder
Abstract
Significance In recent years, we have learned that bacterial cells have intricate spatial organization despite the lack of membrane-bounded organelles. The endcaps of rod-shaped bacteria, termed poles, are emerging as hubs for sensing and responding, but the processes involved in positioning macromolecules there are largely unknown. We discovered a protein, TmaR, whose polar localization depends on a phospho-tyrosine modification. We show that TmaR controls the activity of EI, the major regulator of sugar metabolism in most bacteria, by polar sequestration and release. Notably, TmaR is essential for survival in conditions that Escherichia coli often encounters in nature. Hence, TmaR is a key regulator that connects tyrosine phosphorylation, spatial regulation, sugar metabolism, and survival in bacteria.