PrP protein can bind to protein kinase CK2 both in native and recombinant forms in vitro.
- Author:
Jian-Ming CHEN
1
;
Chen GAO
;
Qi SHI
;
Yong-Jun GAO
;
Yan-Jun LEI
;
Bing SHAN
;
Chen-Fang DONG
;
Gui-Rong WANG
;
Song SHI
;
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.
- Publication Type:Journal Article
- MeSH:
Animals;
Casein Kinase II;
chemistry;
physiology;
Cricetinae;
Humans;
Immunoprecipitation;
Phosphorylation;
Prion Diseases;
etiology;
Prions;
chemistry;
Recombinant Proteins;
chemistry
- From:
Chinese Journal of Virology
2008;24(5):335-339
- CountryChina
- Language:Chinese
-
Abstract:
To explore the possible molecular interaction between CK2 and PrP, the full length sequences of human CK2alpha and CK2beta genes were amplified with RT-PCR using the mRNA from cell line SH-SY5Y as the template, and then the fusion proteins HIS-CK2alpha and GST-HIS-CK2beta were expressed in E. coli. The interaction between CK2 and PrP was evaluated with immunoprecipitation and pull-down assays. The results demonstrated that recombinant PrP bound specifically with CK2alpha, but not with CK2beta. The native CK2 and PrP in the hamster brains interacted each other, forming protein complexes. The domain responsible for interacting with CK2alpha was located at the C-terminal segment of PrP (residues 90-231). This study proposed reliable experimental data for the molecular interaction between PrP and CK2alpha, both in recombinant and native categories. These results supply scientific clues for further assessing the potential biological significance of the interaction of PrP with CK2 and possible role of CK2 in the pathogenesis of prion diseases.
