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Phosphorylation of purified recombinant hepatitis B virus-X protein by mitogen-activated protein kinase and protein kinase C in vitro

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Author(s)
Young I. LeeSun O. KimHyok J. KwonJong G. ParkMi J. SohnSoon S. Jeong
Keimyung Author(s)
Park, Jong Gu
Department
Dept. of Molecular Medicine (분자의학)
Institute for Medical Science (의과학연구소)
Journal Title
Journal of Virological Methods
Issued Date
2001
Volume
95
Issue
1-2
Keyword
Hepatitis B virus-X proteinCircular dichroismProtein kinase CMitogen-activated protein kinase
Abstract
The recombinant human hepatitis B virus-X protein (rhHBx) has been expressed as inclusion bodies in Escherichia coli and purified. By sequential dialysis of urea, rhHBx was folded into the native structure, which was demonstrated by both the efficacy of its transcriptional activation of the adenovirus major late promoter, fluorescence and circular dichroism (CD) analysis. The increase in CD values at 220 nm and a corresponding blue shift of the intrinsic fluorescence emission confirmed the ability of HBx to refold in lower concentrations of urea to produce the active protein. After purification and renaturation, the rhHBx protein was found to be phosphorylated by protein kinase C (PKC) and mitogen-activated protein kinase (MAPK). In vivo phosphorylation of HBx was also demonstrated. Although PKC and MAPK enhance the HBx phosphorylation in vitro, neither protein kinase A nor caseine kinase II (CKII) phosphorylate HBx protein, though there are possible substrate residues of both kinases in HBx protein. Phosphoamino acid analysis of the total acid hydrolyzed HBx showed that serine residues can be phosphorylated by PKC or MAPK.
Keimyung Author(s)(Kor)
박종구
Publisher
School of Medicine
Citation
Young I. Lee et al. (2001). Phosphorylation of purified recombinant hepatitis B virus-X
protein by mitogen-activated protein kinase and protein
kinase C in vitro. Journal of Virological Methods, 95(1–2), 1–10. doi: 10.1016/S0166-0934(00)00282-2
Type
Article
ISSN
0166-0934
Source
https://www.sciencedirect.com/science/article/pii/S0166093400002822?via%3Dihub
DOI
10.1016/S0166-0934(00)00282-2
URI
https://kumel.medlib.dsmc.or.kr/handle/2015.oak/34304
Appears in Collections:
1. School of Medicine (의과대학) > Dept. of Molecular Medicine (분자의학)
3. Research Institutues (연구소) > Institute for Medical Science (의과학연구소)
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