RUP2 facilitates UVR8 redimerization via two interfaces.

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^W285A complex (2.0 Å). RUP2 and UVR8^W285A formed a heterodimer via two distinct interfaces, designated Interface 1 and 2. The previously characterized In

SUBMITTER: Wang L 

PROVIDER: S-EPMC9860181 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature