Cysteines have a role in conformation of the UVR8 photoreceptor.

ABSTRACT: The UV RESISTANCE LOCUS 8 (UVR8) photoreceptor mediates plant responses to Ultraviolet-B (UV-B) wavelengths. The UVR8 dimer dissociates into monomers following UV-B photoreception, a process accompanied by conformational changes that facilitate interaction of UVR8 with proteins that initiate responses. However, the importance of particular amino acids in maintaining UVR8 conformation and modulating protein interactions is poorly understood. Here we examine the roles of cysteine amino acids C231 and C335 in UVR8 structure and function. UVR8^C231S,C335S mutant protein forms dimers and monomerizes similarly to wild-type UVR8. UVR8^C231S,C335S interacts with CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1) in plants to initiate photomorphogenic responses to UV-B, although the inter

SUBMITTER: Liao X 

PROVIDER: S-EPMC9546227 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature