Abstract
The Arabidopsis thaliana protein UVR8 is a photoreceptor for ultraviolet-B. Upon ultraviolet-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, which triggers a signalling pathway for ultraviolet protection. The mechanism by which UVR8 senses ultraviolet-B remains largely unknown. Here we report the crystal structure of UVR8 at 1.8 Å resolution, revealing a symmetric homodimer of seven-bladed β-propeller that is devoid of any external cofactor as the chromophore. Arginine residues that stabilize the homodimeric interface, principally Arg 286 and Arg 338, make elaborate intramolecular cation–π interactions with surrounding tryptophan amino acids. Two of these tryptophans, Trp 285 and Trp 233, collectively serve as the ultraviolet-B chromophore. Our structural and biochemical analyses identify the molecular mechanism for UVR8-mediated ultraviolet-B perception, in which ultraviolet-B radiation results in destabilization of the intramolecular cation–π interactions, causing disruption of the critical intermolecular hydrogen bonds mediated by Arg 286 and Arg 338 and subsequent dissociation of the UVR8 homodimer.
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Acknowledgements
We thank J. He and S. Huang at SSRF, and K. Hasegawa and T. Kumasaka at the SPring-8 beamline BL41XU, for assistance. This work was supported by funds from the Ministry of Science and Technology (grant no. 2009CB918801 to Y.S., and 2012CB910900 to X.W.D.), the National Natural Science Foundation, and the Beijing Municipal Commissions of Education and Science and Technology.
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D.W., Q.H., H.D., X.W.D. and Y.S. designed all experiments. D.W., Q.H., Z.Y., W.C., C.Y. and J.Z. performed the experiments. D.W., Q.H., Z.Y., W.C., C.Y., X.H., J.Z., P.Y., H.D., J.W., X.W.D. and Y.S. contributed to technical work and data analysis. D.W., Q.H., Z.Y., W.C., C.Y., J.W., X.W.D. and Y.S. contributed to manuscript preparation. Y.S. wrote the manuscript.
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Di Wu, Hu, Q., Yan, Z. et al. Structural basis of ultraviolet-B perception by UVR8. Nature 484, 214–219 (2012). https://doi.org/10.1038/nature10931
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DOI: https://doi.org/10.1038/nature10931
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