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Structural insight into UV-B–activated UVR8 bound to COP1

信息来源:     发布时间:2022-04-25

YIDONG WANGHTTPS://ORCID.ORG/0000-0002-5914-6165LIXIA WANGHTTPS://ORCID.ORG/0000-0002-7542-4671ZEYUAN GUANHTTPS://ORCID.ORG/0000-0002-8909-866XHONGFEI CHANGLING MACUICUI SHENLIANG QIUJUNJIE YAN, HTTPS://ORCID.ORG/0000-0001-9748-7246DELIN ZHANG, HTTPS://ORCID.ORG/0000-0002-5299-0718JIAN LIHTTPS://ORCID.ORG/0000-0002-1287-8932XING WANG DENG HTTPS://ORCID.ORG/0000-0001-8709-1467 AND PING YIN 

SCIENCE ADVANCES20 Apr 2022Vol 8, Issue 16

Abstract

The CONSTITUTIVE PHOTOMORPHOGENIC 1-SUPPRESSOR OF PHYA-105 (COP1-SPA) complex is a central repressor of photomorphogenesis. This complex acts as an E3 ubiquitin ligase downstream of various light signaling transduced from multiple photoreceptors in plants. How the COP1-SPA activity is regulated by divergent light-signaling pathways remains largely elusive. Here, we reproduced the regulation pathway of COP1-SPA in ultraviolet-B (UV-B) signaling in vitro and determined the cryo-electron microscopy structure of UV-B receptor UVR8 in complex with COP1. The complex formation is mediated by two-interface interactions between UV-B-activated UVR8 and COP1. Both interfaces are essential for the competitive binding of UVR8 against the signaling hub component HY5 to the COP1-SPA complex. We also show that RUP2 dissociates UVR8 from the COP1-SPA41–464-UVR8 complex and facilitates its redimerization. Our results support a UV-B signaling model that the COP1-SPA activity is repressed by UV-B-activated UVR8 and derepressed by RUP2, owing to competitive binding, and provide a framework for studying the regulatory roles of distinct photoreceptors on photomorphogenesis.


全文链接:https://www.science.org/doi/10.1126/sciadv.abn3337

HTTPS://ORCID.ORG/0000-0001-8001-221X

 


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