Mei Guo-yong, Li Yuan, Wang Gui-rong, Zhang Bao-yun, Tian Chan, Chen Cao, Zhou Rui-min, Wang Xin, Li Xiao-li, Wang Ke-xia, Han Jun, Dong Xiao-ping
Pathogenic Microorganisms Department, Medical School, Anhui University of Science and Technology, Huainan, 232001, China.
Bing Du Xue Bao. 2009 May;25(3):208-12.
The molecular interaction between PrP and 14-3-3 beta and the possible interactional domain between two proteins were studied by co-immunoprecipitation, pull down and FRET assays. The results showed that PrP protein could interact with 14-3-3 beta in vitro and in vivo. The domain which responded for the interaction was located at C-terminal of PrP (amino acid residues 106 to 126). This study of the interaction between PrP and 14-3-3 protein further provided the insight into the potential role of 14-3-3 in the biological function of PrP and the pathogenesis of prion disease.
通过免疫共沉淀、下拉实验和荧光共振能量转移(FRET)分析,研究了朊蛋白(PrP)与14-3-3β之间的分子相互作用以及两种蛋白之间可能的相互作用结构域。结果表明,PrP蛋白在体外和体内均能与14-3-3β相互作用。负责这种相互作用的结构域位于PrP的C末端(氨基酸残基106至126)。对PrP与14-3-3蛋白之间相互作用的这项研究,进一步深入了解了14-3-3在PrP生物学功能及朊病毒疾病发病机制中的潜在作用。