8GQE

Crystal structure of the W285A mutant of UVR8 in complex with RUP2

Summary for 8GQE

• Entry DOI: 10.2210/pdb8gqe/pdb
• Descriptor: WD repeat-containing protein RUP2, Ultraviolet-B receptor UVR8, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: signaling protein
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 2
• Total formula weight: 87701.10

Authors

Wang, Y.D.,Wang, L.X.,Guan, Z.Y.,chang, H.F.,Yin, P. (deposition date: 2022-08-30, release date: 2022-09-14, Last modification date: 2023-11-29)

Primary citation

Wang, L.,Wang, Y.,Chang, H.,Ren, H.,Wu, X.,Wen, J.,Guan, Z.,Ma, L.,Qiu, L.,Yan, J.,Zhang, D.,Huang, X.,Yin, P.
RUP2 facilitates UVR8 redimerization via two interfaces.
Plant Commun., 4:100428-100428, 2023

PubMed Abstract: The plant UV-B photoreceptor UV RESISTANCE LOCUS 8 (UVR8) exists as a homodimer in its inactive ground state. Upon UV-B exposure, UVR8 monomerizes and interacts with a downstream key regulator, the CONSTITUTIVE PHOTOMORPHOGENIC 1/SUPPRESSOR OF PHYA (COP1/SPA) E3 ubiquitin ligase complex, to initiate UV-B signaling. Two WD40 proteins, REPRESSOR OF UV-B PHOTOMORPHOGENESIS 1 (RUP1) and RUP2 directly interact with monomeric UVR8 and facilitate UVR8 ground state reversion, completing the UVR8 photocycle. Here, we reconstituted the RUP-mediated UVR8 redimerization process in vitro and reported the structure of the RUP2-UVR8 complex (2.0 Å). RUP2 and UVR8 formed a heterodimer via two distinct interfaces, designated Interface 1 and 2. The previously characterized Interface 1 is found between the RUP2 WD40 domain and the UVR8 C27 subregion. The newly identified Interface 2 is formed through interactions between the RUP2 WD40 domain and the UVR8 core domain. Disruption of Interface 2 impaired UV-B induced photomorphogenic development in Arabidopsis thaliana. Further biochemical analysis indicated that both interfaces are important for RUP2-UVR8 interactions and RUP2-mediated facilitation of UVR8 redimerization. Our findings suggest that the two-interface-interaction mode is adopted by both RUP2 and COP1 when they interact with UVR8, marking a step forward in understanding the molecular basis that underpins the interactions between UVR8 and its photocycle regulators.

PubMed: 36065466
DOI: 10.1016/j.xplc.2022.100428

Experimental method

X-RAY DIFFRACTION (2 Å)