Molecular interaction between PrP protein and the signal protein 14-3-3 beta.
- Author:
Guo-yong MEI
1
;
Yuan LI
;
Gui-rong WANG
;
Bao-yun ZHANG
;
Chan TIAN
;
Cao CHEN
;
Rui-min ZHOU
;
Xin WANG
;
Xiao-li LI
;
Ke-xia WANG
;
Jun HAN
;
Xiao-ping DONG
Author Information
1. Pathogenic Microorganisms Department, Medical School, Anhui University of Science and Technology, Huainan, 232001, China. 06mgy@163.com
- Publication Type:Journal Article
- MeSH:
14-3-3 Proteins;
metabolism;
Animals;
Brain;
metabolism;
Cricetinae;
Fluorescence Resonance Energy Transfer;
HeLa Cells;
Humans;
Immunoprecipitation;
Prions;
metabolism;
Protein Binding;
Rabbits
- From:
Chinese Journal of Virology
2009;25(3):208-212
- CountryChina
- Language:Chinese
-
Abstract:
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.
