Structural basis of ultraviolet-B perception by UVR8

Nature

Volumn 484, Issue 7393, 2012, Pages 214-219

  Di Wu, ^a   Hu, Qi ^a   Yan, Zhen ^a   Chen, Wen ^b   Yan, Chuangye ^a   Huang, Xi ^b   Zhang, Jing ^a   Yang, Panyu ^b   Deng, Haiteng ^a   Wang, Jiawei ^a   Deng, Xingwang ^b   Shi, Yigong ^a  

^a Tsinghua University   (China)

^b PEKING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; ARGININE; HOMODIMER; PROTEIN UVR8; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID; BIOCHEMISTRY; CHEMICAL BONDING; CRYSTAL STRUCTURE; DICOTYLEDON; IRRADIANCE; MOLECULAR ANALYSIS; PHOTORECEPTION; PROTEIN; ULTRAVIOLET B RADIATION;

ARABIDOPSIS; ARTICLE; CHEMICAL ANALYSIS; CHROMATOPHORE; CRYSTAL STRUCTURE; HYDROGEN BOND; NONHUMAN; PERCEPTION; PHOTORECEPTOR; PRIORITY JOURNAL; PROTEIN INTERACTION; STRUCTURE ANALYSIS; ULTRAVIOLET B RADIATION;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; CATIONS; CHROMOSOMAL PROTEINS, NON-HISTONE; CRYSTALLOGRAPHY, X-RAY; LIGHT SIGNAL TRANSDUCTION; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; TRYPTOPHAN; ULTRAVIOLET RAYS;

ARABIDOPSIS THALIANA;

EID: 84862776742     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10931     Document Type: Article

References (40)

1. Falciatore, A. & Bowler, C. The evolution and function of blue and red light photoreceptors. Curr. Top. Dev. Biol. 68, 317-350 (2005).
2. van der Linden, A. M. et al. Genome-wide analysis of light-and temperature-entrained circadian transcripts in Caenorhabditis elegans. PLoS Biol. 8, e1000503 (2010).
3. Fogle, K. J., Parson, K. G., Dahm, N. A. & Holmes, T. C. CRYPTOCHROME is a blue-light sensor that regulates neuronal firing rate. Science 331, 1409-1413 (2011).
4. Jiao, Y., Lau, O. S. & Deng, X. W. Light-regulated transcriptional networks in higher plants. Nature Rev. Genet. 8, 217-230 (2007).
5. Kami, C., Lorrain, S., Hornitschek, P. & Fankhauser, C. Light-regulated plant growth and development. Curr. Top. Dev. Biol. 91, 29-66 (2010).
6. Quail, P. H. Phytochrome photosensory signalling networks. Nature Rev. Mol. Cell Biol. 3, 85-93 (2002).
7. Briggs, W. R. & Christie, J. M. Phototropins 1 and 2: versatile plant blue-light receptors. Trends Plant Sci. 7, 204-210 (2002).
8. Chaves, I. et al. The cryptochromes: blue light photoreceptors in plants and animals. Annu. Rev. Plant Biol. 62, 335-364 (2011).
9. Cashmore, A. R., Jarillo, J. A., Wu, Y. J. & Liu, D. Cryptochromes: blue light receptors for plants and animals. Science 284, 760-765 (1999).
10. Christie, J. M. Phototropin blue-light receptors. Annu. Rev. Plant Biol. 58, 21-45 (2007).
11. Liu, H., Liu, B., Zhao, C., Pepper, M. & Lin, C. The action mechanisms of plant cryptochromes. Trends Plant Sci. 16, 684-691 (2011).
12. Rizzini, L. et al. Perception of UV-B by the Arabidopsis UVR8 protein. Science 332, 103-106 (2011).
13. Möglich, A., Yang, X., Ayers, R. A. & Moffat, K. Structure and function of plant photoreceptors. Annu. Rev. Plant Biol. 61, 21-47 (2010).
14. Kliebenstein, D. J., Lim, J. E., Landry, L. G. & Last, R. L. Arabidopsis UVR8 regulates ultraviolet-B signal transduction and tolerance and contains sequence similarity to human regulator of chromatin condensation 1. Plant Physiol. 130, 234-243 (2002).
15. Brown, B. A. et al. A UV-B-specific signaling component orchestrates plant UV protection. Proc. Natl Acad. Sci. USA 102, 18225-18230 (2005).
16. Brown, B. A. & Jenkins, G. I. UV-B signaling pathways with different fluence-rate response profiles are distinguished in mature Arabidopsis leaf tissue by requirement for UVR8, HY5, and HYH. Plant Physiol. 146, 576-588 (2008).
17. Kaiserli, E. & Jenkins, G. I. UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus. Plant Cell 19, 2662-2673 (2007).
18. Li, D. & Roberts, R. WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. Cell. Mol. Life Sci. 58, 2085-2097 (2001).
19. 2. Cell 83, 1047-1058 (1995).
20. Renault, L. et al. The 1. 7 A crystal structure of the regulator of chromosome condensation (RCC1) revealsaseven-bladedpropeller. Nature392, 97-101(1998).
21. Gallivan, J. P. & Dougherty, D. A. Cation-p interactions in structural biology. Proc. Natl Acad. Sci. USA 96, 9459-9464 (1999).
22. Gallivan, J. P. & Dougherty, D. A. A computational study of cation2p interactions vs salt bridges in aqueous media: implications for protein engineering. J. Am. Chem. Soc. 122, 870-874 (2000).
23. Dougherty, D. A. Cation2p interactions involving aromatic amino acids. J. Nutr. 137, 1504S-1508S (2007).
24. Sinnokrot, M. O., Valeev, E. F. & Sherrill, C. D. Estimates of the ab initio limit for p-p interactions: the benzene dimer. J. Am. Chem. Soc. 124, 10887-10893 (2002).
25. Wagner, J. R., Brunzelle, J. S., Forest, K. T. & Vierstra, R. D. A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature 438, 325-331 (2005).
26. Ulijasz, A. T. et al. Structural basis for the photoconversion of a phytochrome to the activated Pfr form. Nature 463, 250-254 (2010).
27. Brudler, R. et al. Identification of a new cryptochrome class. Structure, function, and evolution. Mol. Cell 11, 59-67 (2003).
28. Brautigam, C. A. et al. Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana. Proc. Natl Acad. Sci. USA 101, 12142-12147 (2004).
29. Crosson, S. & Moffat, K. Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction. Proc. Natl Acad. Sci. USA 98, 2995-3000 (2001).
30. Crosson, S. & Moffat, K. Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 14, 1067-1075 (2002).
31. Yu, H. T., Colucci, W. J., McLaughlin, M. L. & Barkley, M. D. Fluorescence quenching in indoles by excited-state proton transfer. J. Am. Chem. Soc. 114, 8449-8454 (1992).
32. Christie, J. M. et al. Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of cross-dimer salt bridges. Science http://dx.doi.org/10.1126/science.1218091 (9 February 2012).
33. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
34. Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
35. Schneider, T. R. & Sheldrick, G. M. Substructure solution with SHELXD. Acta Crystallogr. D 58, 1772-1779 (2002).
36. Cowtan, K. The Buccaneer software for automated model building. Acta Crystallogr. D 62, 1002-1011 (2006).
37. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
38. Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
39. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
40. DeLano, W. L. The PyMOL Molecular Graphics System. http://www.pymol.org (2002).