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Christie, John M.; Arvai, Andrew S.; Baxter, Katherine J.; Heilmann, Monika; Pratt, Ashley J.; O'Hara, Andrew; Kelly, Sharon M.; Hothorn, Michael; Smith, Brian O.; Hitomi, Kenichi; Jenkins, Gareth I.; Getzoff, Elizabeth D.
Science (American Association for the Advancement of Science), 03/2012, Volume: 335, Issue: 6075Journal Article
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, cristallographie 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. ß-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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