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Structural basis of ultraviolet-B perception by UVR8

Nature volume 484, pages 214–219 (2012)Cite this article

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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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Figure 1: Characterization and structure of the ultraviolet-sensing protein UVR8.
Figure 2: Structural basis of UVR8 homodimer formation.
Figure 3: Structural features of the ultraviolet-B-sensing amino acids.
Figure 4: Identification of Trp 285 and Trp 233 as the ultraviolet-B chromophore.

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Accession codes

Primary accessions

Protein Data Bank

Data deposits

The atomic coordinates and structure factor files of UVR8 wild type, W285A and W285F have been deposited in the Protein Data Bank under accession codes 4DNW, 4DNU and 4DNV, respectively.

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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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Author notes

  1. Di Wu, Qi Hu and Zhen Yan: These authors contributed equally to this work.

Authors and Affiliations

  1. Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, 100084, China

    Di Wu, Qi Hu, Zhen Yan, Jing Zhang, Haiteng Deng & Yigong Shi

  2. College of Life Sciences, Peking University, Beijing, 100871, China

    Wen Chen, Xi Huang, Panyu Yang & XingWang Deng

  3. State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, 100084, China

    Chuangye Yan & Jiawei Wang

  4. Peking-Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, State Key Laboratory of Protein and Plant Gene Research, Peking University, Beijing, 100871, China

    Xi Huang, Panyu Yang & XingWang Deng

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Contributions

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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Correspondence to Yigong Shi.

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This file contains Supplementary Figures 1-14 with legends, Supplementary Table 1 and additional references. (PDF 1491 kb)

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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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