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作 者:Xinyu Zhang Junling Huai Shuangrong Liu Jing Bo Jin Rongcheng Lin
机构地区:[1]Key Laboratory of Photobiology,Institute of Botany,Chinese Academy of Sciences,Beijing 100093,China [2]University of Chinese Academy of Sciences,Beijing 100049,China [3]Key Laboratory of Plant Molecular Physiology,Institute of Botany,Chinese Academy of Sciences,Beijing 100093,China [4]Present address:Department of Plant Sciences,University of Oxford,South Parks Road,Oxford OX13RB,UK
出 处:《Plant Communications》2020年第5期73-84,共12页植物通讯(英文)
基 金:supported by grants from the National Key Research and Development Program of China(2016YFD0100405;2017YFA0503800);the Strategic Priority Research Program of the Chinese Academy of Sciences(XDB27030205);the National Natural Science Foundation of China(31800235).
摘 要:Small ubiquitin-like modifier(SUMO)post-translational modification(SUMOylation)plays essential roles in regulating various biological processes;however,its function and regulation in the plant light signaling pathway are largely unknown.SEUSS(SEU)is a transcriptional co-regulator that integrates light and temperature signaling pathways,thereby regulating plant growth and development in Arabidopsis thaliana.Here,we show that SEU is a substrate of SUMO1,and that substitution of four conserved lysine residues disrupts the SUMOylation of SEU,impairs its function in photo-and thermomorphogenesis,and enhances its interaction with PHYTOCHROME-INTERACTING FACTOR 4 transcription factors.Furthermore,the SUMO E3 ligase SIZ1 interacts with SEU and regulates its SUMOylation.Moreover,SEU directly interacts with phytochrome B photoreceptors,and the SUMOylation and stability of SEU are activated by light.Our study reveals a novel post-translational modification mechanism of SEU in which light regulates plant growth and development through SUMOylation-mediated protein stability.
关 键 词:light signaling PHYTOCHROME PIF4 SUMOYLATION
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