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• W1640179935 abstract "Phosphorylation of core particles derived either from hepatitis B viruses or from livers of hepatitis B-infected individuals has been long recognized, but the nature and function of the phosphorylating enzyme remained unknown. By immunoblotting with a monoclonal antibody, we have now detected protein kinase C within the liver-derived core particles. To study the significance of the encapsidated protein kinase C for the viral life cycle, we established an in vitro assembly system consisting of Escherichia coli-expressed core protein, protein kinase C, and in vitro-synthesized hepatitis B virus RNA. Phosphorylation of the core protein led to a reduced RNA encapsidation capacity of the core particles. Furthermore, RNA and protein kinase C competed for their target sequence, which is the carboxy-terminal arginine-rich domain of the core protein. This finding implies that phosphorylation of the nucleic acid binding site in the core protein occurs within the particles after encapsidation of protein kinase C, pregenomic RNA, and viral polymerase at a later step during viral genome maturation." @default.
• W1640179935 created "2016-06-24" @default.
• W1640179935 creator A5007549419 @default.
• W1640179935 creator A5043725161 @default.
• W1640179935 date "1994-12-01" @default.
• W1640179935 modified "2023-10-14" @default.
• W1640179935 title "Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus" @default.
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• W1640179935 doi "https://doi.org/10.1128/jvi.68.12.7993-8000.1994" @default.
• W1640179935 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/237262" @default.
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