The C-terminal 17 amino acids of the photoreceptor UVR8 is involved in the fine-tuning of UV-B signaling

Plant UV-B responses are mediated by the photoreceptor UV RESISTANCE LOCUS 8 (UVR8). In response to UV-B irradiation, UVR8 homodimers dissociate into monomers that bind to the E3 ubiquitin ligase CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1). The interaction of the C27 domain in the C-terminal tail of UVR8 with the WD40 domain of COP1 is critical for UV-B signaling. However, the function of the last 17 amino acids (C17) of the C-terminus of UVR8, which are adjacent to C27, is unknown, although they are largely conserved in land plants. In this study, we established thatArabidopsis thalianaUVR8 C17 binds to full-length UVR8, but not to COP1, and reduces COP1 binding to the remaining portion of UVR8, including C27. We hypothesized that overexpression of C17 in a wild-type background would have a dominant negative effect on UVR8 activity; however, C17 overexpression caused strong silencing of endogenousUVR8, precluding a detailed analysis. We therefore generated YFP-UVR8(N423)transgenic lines, in which C17 was deleted, to examine C17 function indirectly. YFP-UVR8(N423)was more active than YFP-UVR8, suggesting that C17 inhibits UV-B signaling by attenuating binding between C27 and COP1. Our study reveals an inhibitory role for UVR8 C17 in fine-tuning UVR8-COP1 interactions during UV-B signaling.