拟南芥AtDWD与DDB1相互作用研究  

The research of AtDWD interacting with DDB1

作　　者：吴叶天 李德款[1] 杨毅[1] 

机构地区：[1]四川大学生命科学学院生物资源与生态环境教育部重点实验室,成都610064

出　　处：《四川大学学报（自然科学版）》2017年第2期411-416,共6页Journal of Sichuan University(Natural Science Edition)

基　　金：国家自然科学基金(31171586);973计划(2015CB755702)

摘　　要：本文通过酵母双杂交实验(Y2H)和双荧光互补实验(BIFC)分别从体外和体内条件下检测了AtDWD与CUL4型E3连接酶的底物识别蛋白结合蛋白DDB1a和DDB1b的相互作用,发现AtDWD与DDB1b有较强的相互作用,而与DDB1a的相互作用较弱,相互作用区域位于AtDWD的C末端部位.说明了AtDWD是潜在的CUL4型E3连接酶的底物识别亚基.此外,本文中还发现AtDWD过表达植株对冷冻胁迫更加敏感.AtDWD可能参与冷胁迫信号通路.In our study, the yeasttwo-hybrid assay （Y2H） and bimolecular fluorescence complementation （BiFC） have been applied to investigate the interaction between AtDWD and DDB1a/DDB1b （the CUL4- based E3 ligase interacts with the substrate receptor to target special substrates ）in vitro and in vivo. It has shown strong interaction between AtDWD and DDB1b , but weak interaction between AtDWD and DDB1a. Moreover, the C-terminal of AtDWD was where the interaction happened. The results suggested that AtDWDmight be a substrate receptor protein of CUL4-based E3 ligase. On the other hand, the AtDWD-overexpression transgenic plants＇were sensitive to freeze. AtDWD may play a role in plant reacting in freezing stress.

关 键 词：DDB1 AtDWD E3连接酶 植物冷冻胁迫 

分 类 号：Q78[生物学—分子生物学]