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B12-based photoreceptors: from structure and function to applications in optogenetics and synthetic biology
S Padmanabhan1, Ricardo Pérez-Castaño2, Montserrat Elías-Arnanz2
1Instituto de Química Física "Rocasolano", Consejo Superior de Investigaciones Científicas, 28006, Madrid, Spain.
Abstract:
Vitamin B12-based photoreceptor proteins sense ultraviolet (UV), blue or green light using 5'-deoxyadenosylcobalamin (AdoCbl). The prototype of this widespread bacterial photoreceptor family, CarH, controls light-dependent gene expression in photoprotective cellular responses. It represses transcription in the dark by binding to operator DNA as an AdoCbl-bound tetramer, whose disruption by light relieves operator binding to allow transcription. Structures of the 'dark' (free and DNA-bound) and 'light' CarH states and studies on the unusual AdoCbl photochemistry have provided fundamental insights into these photoreceptors. We highlight these, the plasticity within a conserved mode of action among CarH homologs, their distribution, and their promising applications in optogenetics and synthetic biology.
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