RUP2 facilitates UVR8 redimerization via two interfaces

被引:10
|
作者
Wang, Lixia [1 ]
Wang, Yidong [1 ]
Chang, Hongfei [1 ]
Ren, Hui [2 ]
Wu, Xinquan [2 ]
Wen, Jia [2 ]
Guan, Zeyuan [1 ]
Ma, Ling [1 ]
Qiu, Liang [1 ]
Yan, Junjie [1 ]
Zhang, Delin [1 ]
Huang, Xi [2 ]
Yin, Ping [1 ]
机构
[1] Huazhong Agr Univ, Natl Key Lab Crop Genet Improvement, Hubei Hongshan Lab, Wuhan 430070, Peoples R China
[2] Xiamen Univ, Fac Med & Life Sci, Sch Life Sci, State Key Lab Cellular Stress Biol, Xiamen 361102, Peoples R China
基金
中国国家自然科学基金; 国家重点研发计划; 中国博士后科学基金;
关键词
photomorphogenesis; UV-B photoreceptor; UVR8; RUP2; COP1; B-INDUCED PHOTOMORPHOGENESIS; ULTRAVIOLET-B; PHOTORECEPTOR UVR8; SIGNAL-TRANSDUCTION; STRESS ACCLIMATION; GENE-EXPRESSION; TRANSCRIPTION; PERCEPTION; COP1; MECHANISM;
D O I
10.1016/j.xplc.2022.100428
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom). RUP2 and UVR8(W285A) 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.
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页数:12
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