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-Structure paper
タイトル | Structural insight into UV-B-activated UVR8 bound to COP1. |
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ジャーナル・号・ページ | Sci Adv, Vol. 8, Issue 16, Page eabn3337, Year 2022 |
掲載日 | 2022年4月22日 |
著者 | Yidong Wang / Lixia Wang / Zeyuan Guan / Hongfei Chang / Ling Ma / Cuicui Shen / Liang Qiu / Junjie Yan / Delin Zhang / Jian Li / Xing Wang Deng / Ping Yin / |
PubMed 要旨 | 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 ...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-SPA4-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. |
リンク | Sci Adv / PubMed:35442727 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.1 Å |
構造データ | EMDB-31968, PDB-7vgg: |
由来 |
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キーワード | SIGNALING PROTEIN / COP1 / UVR8 |