Journal
SCIENCE
Volume 335, Issue 6075, Pages 1492-1496Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1218091
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Funding
- National Institutes of Health [GM37684]
- Skaggs Institute for Chemical Biology
- National Science Foundation
- Royal Society
- Leverhulme Trust [F/00179/AZ]
- UK Biotechnology and Biological Sciences Research Council
- Department of Energy, Office of Biological and Environmental Research
- Biotechnology and Biological Sciences Research Council [BB/F014961/1] Funding Source: researchfish
- BBSRC [BB/F014961/1] Funding Source: UKRI
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The recently identified plant photoreceptor UVR8 (UV RESISTANCE LOCUS 8) triggers regulatory changes in gene expression in response to ultraviolet-B (UV-B) light through an unknown mechanism. Here, crystallographic and solution structures of the UVR8 homodimer, together with mutagenesis and far-UV circular dichroism spectroscopy, reveal its mechanisms for UV-B perception and signal transduction. beta-propeller subunits form a remarkable, tryptophan-dominated, dimer interface stitched together by a complex salt-bridge network. Salt-bridging arginines flank the excitonically coupled cross-dimer tryptophan pyramid responsible for UV-B sensing. Photoreception reversibly disrupts salt bridges, triggering dimer dissociation and signal initiation. Mutation of a single tryptophan to phenylalanine retunes the photoreceptor to detect UV-C wavelengths. Our analyses establish how UVR8 functions as a photoreceptor without a prosthetic chromophore to promote plant development and survival in sunlight.
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