A General Mechanism for Initiating the General Stress Response in Bacteria

• DOI: 10.1101/2024.02.16.580724
• Publication Date: 2024-02-18T06:10:10Z
• Authors: Rishika Baral; Kristin Ho; Ramasamy P. Kumar; Jesse B. Hopkins; Maxwell B. Watkins; Salvatore LaRussa; Suhaily Caban-Penix; Logan A. Calderone; Niels Bradshaw

AbstractThe General Stress Response promotes survival of bacteria in adverse conditions, but how sensor proteins transduce species-specific signals to initiate the response is not known. The serine/threonine phosphatase RsbU initiates the General Stress Response inB. subtilisupon binding a partner protein (RsbT) that is released from sequestration by environmental stresses. We report that RsbT activates RsbU by inducing otherwise flexible linkers of RsbU to form a short coiled-coil that dimerizes and activates the phosphatase domains. Importantly, we present evidence that related coiled-coil linkers and phosphatase dimers transduce signals from diverse sensor domains to control the General Stress Response and other signaling across bacterial phyla. This coiled-coil linker transduction mechanism additionally suggests a resolution to the mystery of how shared sensory domains control serine/threonine phosphatases, diguanylate cyclases and histidine kinases. We propose that this provides bacteria with a modularly exchangeable toolkit for the evolution of diverse signaling pathways.