2012
DOI: 10.1126/science.1218091
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Plant UVR8 Photoreceptor Senses UV-B by Tryptophan-Mediated Disruption of Cross-Dimer Salt Bridges

Abstract: The recently identified plant photoreceptor UVR8 triggers regulatory changes in gene expression in response to ultraviolet-B (UV-B) light via 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. β-propeller subunits form a remarkable, tryptophan-dominated, dimer interface stitched together by a complex salt-bridge network. Salt-bridging … Show more

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Cited by 412 publications
(640 citation statements)
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“…This is despite the fact that the band migrates at a lower apparent molecular mass than is expected for the denatured Cr-UVR8 homodimer. Such band patterns have been previously extensively described, including for highly purified recombinant homodimeric At-UVR8 (Rizzini et al, 2011;Christie et al, 2012;Heilmann and Jenkins, 2013). Thus, there is substantial evidence that Cr-UVR8, like At-UVR8, is homodimeric in the absence of UV-B.…”
Section: Discussion the Uvr8-cop1 Uv-b Perception And Signaling Pathwmentioning
confidence: 83%
See 1 more Smart Citation
“…This is despite the fact that the band migrates at a lower apparent molecular mass than is expected for the denatured Cr-UVR8 homodimer. Such band patterns have been previously extensively described, including for highly purified recombinant homodimeric At-UVR8 (Rizzini et al, 2011;Christie et al, 2012;Heilmann and Jenkins, 2013). Thus, there is substantial evidence that Cr-UVR8, like At-UVR8, is homodimeric in the absence of UV-B.…”
Section: Discussion the Uvr8-cop1 Uv-b Perception And Signaling Pathwmentioning
confidence: 83%
“…The plant photoreceptor UV RESISTANCE LOCUS8 (UVR8) specifically perceives UV-B via an intrinsic tryptophan-based mechanism, mainly involving Trp-285 and Trp-233 (Rizzini et al, 2011;Christie et al, 2012;Wu et al, 2012). UVR8 is a seven-bladed b-propeller protein that exists as a homodimer maintained by interactions of charged amino acids across the dimer interaction surface (Rizzini et al, 2011;Christie et al, 2012;Wu et al, 2012;Zeng et al, 2015). The charged amino acids that maintain the homodimer are adjacent to the tryptophans involved in photoreception, suggesting that excitation of these tryptophans by UV-B neutralizes dimer-maintaining interactions Wu et al, 2012;Mathes et al, 2015).…”
Section: Introductionmentioning
confidence: 99%
“…The W77F and W328F data, together with the unusually strict dependence of LITE-1 photoabsorption on its protein conformation, raises the intriguing possibility that LITE-1 may not have a prosthetic chromophore. Interestingly, the plant-specific protein UVR8, a soluble protein which is completely unrelated to LITE-1, also requires tryptophan residues for UVB light detection and lacks a prosthetic chromophore (Christie et al, 2012;Rizzini et al, 2011;Wu et al, 2012). This prompted us to speculate that the two tryptophan residues W77 and W328 may contribute to the formation of the chromophore of LITE-1, which may underlie its high photon-capturing efficiency.…”
Section: Discussionmentioning
confidence: 99%
“…UVR8 exists as a homodimer in plants and rapidly monomerizes in response to UV-B (Rizzini et al, 2011;Christie et al, 2012;Wu et al, 2012). Photoactivated UVR8 then interacts with the E3 ubiquitin ligase CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1) (Favory et al, 2009;Rizzini et al, 2011;Cloix et al, 2012;Huang et al, 2014), which is a well-known repressor of photomorphogenesis and also plays an important role in UV-B signaling (Oravecz et al, 2006).…”
Section: Introductionmentioning
confidence: 99%