UVR8 (UV RESISTANCE LOCUS 8) proteins are a class of UV-B photoreceptors in high plants. UVR8 is a homodimer that dissociates into monomers upon UV-B irradiation (280 to 315 nm), which triggers various protective mechanisms against UV damages. Uniquely, UVR8 does not contain any external chromophores and utilizes the natural amino acid tryptophan (Trp) to perceive UV-B light. Each UVR8 monomer has 14 tryptophan residues. However, only the two Trp (W285 W233) residues are critical to the light-induced dimer-to-monomer transformation. Here, combining time-resolved spectroscopy and extensive site-directed mutations, we have revealed the entire dynamics of UV perception to lead to monomerization, including a series of critical dynamic processes of a striking energy-flow network, exciton charge separation and recombination, charge neutralization, salt-bridge unzipping, and protein solvation, providing a complete molecular picture of the initial biological function.

Dynamics mechanism of dimer dissociation of UVR8 photoreceptor

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