Interaction analysis between various PrP fusion proteins and the tubulin in vitro.
- Author:
Chen-Fang DONG
1
;
Xiao-Fan WANG
;
Run AN
;
Jian-Ming CHEN
;
Bing SHAN
;
Lu HAN
;
Yan-Jun LEI
;
Jun HAN
;
Xiao-Ping DONG
Author Information
1. State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China. dcf466@yahoo.com.cn
- Publication Type:Journal Article
- MeSH:
Animals;
Binding Sites;
genetics;
Blotting, Western;
Electrophoresis, Polyacrylamide Gel;
Humans;
Immunoprecipitation;
Prions;
genetics;
isolation & purification;
metabolism;
Protein Binding;
Rabbits;
Recombinant Fusion Proteins;
genetics;
metabolism;
Tubulin;
metabolism
- From:
Chinese Journal of Virology
2007;23(1):28-32
- CountryChina
- Language:Chinese
-
Abstract:
In order to further study the potential interaction between PrP protein and the tubulin and identify the binding region in PrP with tubulin, native tubulin was extracted from rabbit brian tissues, while various recombinant PrP proteins were expressed and purified. The possible molecular interaction between various PrP fusion proteins and tubulin was tested by pull-down and immunoprecipitation assays. Remarkable molecular interaction between the full length PrP and tubulin was observed by pull-down and immunoprecipitation assays. Subsequently, the binding regions within PrP with tubulin were firstly mapped in the aa 23 -- 91 region within N-terminus of PrP peptide. The studies of the association of PrP with tubulin may further provide insight into the unresolved mechanism of active transport of PrP protein in neurons and possible cellular pathways by which prion causes disease.
