文献类型： 外文期刊
作者： Su, Liang 1 ; Zhou, Peng 2 ; Guo, Lin 2 ; Jia, Xiaolin 4 ; Wang, Shaoci 4 ; Gao, Jianwei 6 ; Li, Hongyu 2 ; Liu, Bin 2 ; Song, Meifang 1 ; Yang, Jianping 2 ;
作者机构： 1.Beijing Acad Sci & Technol, Inst Radiat Technol, 12 Xueyuan Shouth Rd, Beijing 100875, Peoples R China
2.Chinese Acad Agr Sci, Inst Crop Sci, Beijing, Peoples R China
3.China Agr Sci & Technol Press, Beijing, Peoples R China
4.Henan Agr Univ, State Key Lab Wheat & Maize Crop Sci, Coll Agron, Zhengzhou, Peoples R China
5.Henan Agr Univ, Ctr Crop Genome Engn, Zhengzhou, Peoples R China
6.Shandong Acad Agr Sci, Shandong Branch, Inst Vegetable Res, Natl Vegetable Improvement Ctr, Jinan, Peoples R China
关键词： Arabidopsis thaliana; cryptochrome 1; photomorphogenesis; phytochrome A; phytochrome B; SPA2
期刊名称：PLANT DIRECT （ 影响因子：3.369； 五年影响因子：3.457 ）
ISSN：
年卷期： 2022 年 6 卷 5 期
页码：
收录情况： SCI
摘要： In Arabidopsis, phytochrome (phy) A, phyB, and cryptochrome 1 (cry1) are representative far-red, red, and blue light photoreceptors, respectively. Members of the SUPPRESSOR OF PHYA-105 (SPA) protein family (SPA1-SPA4) form E3 ubiquitin ligase complexes with CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1), which mediates the degradation of photomorphogenesis-promoting factors to desensitize light signaling. SPA2 has been reported to promote seedling etiolation in the dark. However, the unique roles of SPA2 and its three functional domains in suppressing photomorphogenesis under different light conditions are largely unknown. Here, we demonstrate that overexpression of the full-length or the central coiled-coil and C-terminal WD-repeat domains of SPA2 cause hyper-etiolation phenotypes under several light conditions. The SPA2 central coiled-coil and C-terminal WD-repeat domains are necessary and sufficient for repressing seedling de-etiolation, cotyledon unfolding, and promoting hypocotyl negative gravitropism under several light conditions. Furthermore, phyA, phyB, cry1, and COP1 repress protein accumulation or nuclear translocation of SPA2 through direct interactions with its kinase-like and coiled-coil domains located in the N-terminus in response to far-red, red, and blue light treatments, respectively. Taken together, our results demonstrate that SPA2 functions under multiple light conditions; moreover, light-activated photoreceptors rapidly suppress SPA2 activity via direct interactions in response to different light treatments.
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