Abstract
The Alphaproteobacterial general stress response (GSR) crucially handles responses to an array of stressors. In a typical photosensitive GSR pathway, blue light illumination stimulates light-oxygen-voltage histidine kinase (LOV-HK) phosphorylation of a single PhyR response regulator, regulating downstream stress gene transcription. The GSR regulators highlighted in this study expand this signaling paradigm at three levels: 1) The LOV-HK RT-HK is dark-activated, 2) only one of two PhyR homologs is apparently accessible to HK phosphodonors, and 3) the other PhyR homolog shows negative cooperativity for activation and partner binding. Our work enhances the current understanding of this complex stress response, introduces novel regulatory modes, and underscores the necessity of testing structural and functional models derived from homology.
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