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SUMOylation facilitates the assembly of a Nuclear Factor-Y complex to enhance thermotolerance in Arabidopsis 被引量:1
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作者 Junwen Huang Junjie Huang +10 位作者 Qiyi Feng Yaqiao Shi Feige Wang kaiyong zheng Qize Huang Jieming Jiang Siyi Luo Yun Xie Danlu Han Jianbin Lai Chengwei Yang 《Journal of Integrative Plant Biology》 SCIE CAS CSCD 2023年第3期692-702,共11页
Heat stress(HS) has serious negative effects on plant development and has become a major threat to agriculture. A rapid transcriptional regulatory cascade has evolved in plants in response to HS. Nuclear Factor-Y(NF-Y... Heat stress(HS) has serious negative effects on plant development and has become a major threat to agriculture. A rapid transcriptional regulatory cascade has evolved in plants in response to HS. Nuclear Factor-Y(NF-Y) complexes are critical for this mechanism, but how NF-Y complexes are regulated remains unclear.In this study, we identified NF-YC10(NF-Y subunit C10), a central regulator of the HS response in Arabidopsis thaliana, as a substrate of SUMOylation, an important post-translational modification. Biochemical analysis showed that the SUMO ligase SIZ1(SAP AND MIZ1 DOMAINCONTAINING LIGASE1) interacts with NF-YC10and enhances its SUMOylation during HS. The SUMOylation of NF-YC10 facilitates its interaction with and the nuclear translocation of NF-YB3, in which the SUMO interaction motif(SIM)is essential for its efficient association with NF-YC10. Further functional analysis indicated that the SUMOylation of NF-YC10 and the SIM of NF-YB3 are critical for HS-responsive gene expression and plant thermotolerance. These findings uncover a role for the SIZ1-mediated SUMOylation of NF-YC10 in NF-Y complex assembly under HS, providing new insights into the role of a post-translational modification in regulating transcription during abiotic stress responses in plants. 展开更多
关键词 ARABIDOPSIS complex assembly heat stress Nuclear Factor-Y SIZ1 SUMOYLATION
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植物蛋白质SUMO化修饰体外高效检测系统
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作者 黄俊文 冯琦伊 +5 位作者 郑凯勇 黄俊杰 王林博 赖瑞强 赖建彬 阳成伟 《植物学报》 CAS CSCD 北大核心 2022年第4期490-499,共10页
蛋白质SUMO化修饰是一种调控蛋白命运的关键修饰方式,广泛参与植物生长发育及逆境胁迫响应。SUMO化修饰过程主要由激活酶(E1)-结合酶(E2)-连接酶(E3)组成的级联酶促反应催化,其关键酶组分将SUMO分子缀合至底物蛋白的赖氨酸残基,形成共... 蛋白质SUMO化修饰是一种调控蛋白命运的关键修饰方式,广泛参与植物生长发育及逆境胁迫响应。SUMO化修饰过程主要由激活酶(E1)-结合酶(E2)-连接酶(E3)组成的级联酶促反应催化,其关键酶组分将SUMO分子缀合至底物蛋白的赖氨酸残基,形成共价异肽键以完成SUMO化修饰过程。该文报道了1种植物蛋白质SUMO化修饰体外高效检测系统,通过在大肠杆菌(Escherichia coli)中构建拟南芥(Arabidopsis thaliana) SUMO化修饰的关键通路实现对底物蛋白的SUMO化修饰,结果可通过免疫印迹进行检测。该系统可以简化植物蛋白质SUMO化修饰的检测流程,为植物细胞SUMO化修饰的功能研究提供了有力工具。 展开更多
关键词 SUMO化修饰 体外 检测系统 植物
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