拟南芥AtDWD与DDB1相互作用研究

The research of AtDWD interacting with DDB1

摘要:

泛素化—蛋白酶体途径是包括植物在内的真核生物调控细胞内蛋白质稳定性的一条主要通路。E3泛素连接酶是泛素化—蛋白酶体途径中起着特异性募集并泛素化底物的作用。DDB1起着桥接CUL4和CUL4型E3连接酶的底物识别亚基的作用。本文通过酵母双杂交实验和BIFC实验分别从体外和体内条件下检测了AtDWD与DDB1a和DDB1b的相互作用，以及AtDWD截段与DDB1b的相互作用，发现AtDWD与DDB1b在体外和体内条件下都有明显的相互作用，相互作用区域位于AtDWD后半段，说明了AtDWD是CUL4型E3连接酶的底物识别亚基。

Abstract:

Ubiquitin-proteasome pathway is a major pathway to regulate cell protein stability in eukaryotes including plants. E3 ubiquitin ligase in the ubiquitin- proteasome pathway is responsible for recruiting specific target proteins for ubiquitination. DDB1 acts together with a second protein, the substrate receptor, totarget substrates for CUL4-based E3 ligase. The yeast two-hybrid assay and BIFC have been applied to check the interaction between AtDWD and DDB1a/DDB1b in vitro and in vivo. Experimental results have shown that interaction between AtDWD and DDB1b is strong in vitro and in vivo，and the C-terminal of AtDWD is where the interaction happens. Support that AtDWD has the potential to be a substrate receptor protein of CUL4-based E3 ligase.