This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gerlich, W H Articles by Wolff, W Search for Related Content PubMed PubMed Citation Articles by Gerlich, W H Articles by Wolff, W

Next Article 

J Virol. 1982 June; 42(3): 761-766

Specificity and localization of the hepatitis B virus-associated protein kinase.

ABSTRACT

The nature of the protein kinase (PK) which phosphorylates the core protein of hepatitis B virus in vitro was studied. The PK copurified with the core particles during rate zonal centrifugation and gel chromatography. It showed the same size heterogeneity as the core particles, which consisted of a main fraction of 28-nm particles and a subfraction of 22- to 26-nm particles. DNA-containing heavy core particles with a density of 1.33 to 1.35 g/ml and less endogenous PK than did the light cores. The phosphorylation reaction had a rapid initial phase (several minutes) and a slow but long-lasting second phase (many hours). The PK had a high affinity for ATP (KM = 0.5 mumol/liter). Only few of the several hundred P21.9 subunits in one core particle were phosphorylated in vitro. The only amino acid which was phosphorylated in vitro was serine. The resistance of the introduced phospho group against alkaline phosphatase showed that the PK acceptor, and probably the enzyme itself, was located inside the core particle.

This article has been cited by other articles:

• Kock, J., Kann, M., Putz, G., Blum, H. E., von Weizsacker, F. (2003). Central Role of a Serine Phosphorylation Site within Duck Hepatitis B Virus Core Protein for Capsid Trafficking and Genome Release. J. Biol. Chem. 278: 28123-28129 [Abstract] [Full Text]  
• Daub, H., Blencke, S., Habenberger, P., Kurtenbach, A., Dennenmoser, J., Wissing, J., Ullrich, A., Cotten, M. (2002). Identification of SRPK1 and SRPK2 as the Major Cellular Protein Kinases Phosphorylating Hepatitis B Virus Core Protein. J. Virol. 76: 8124-8137 [Abstract] [Full Text]  
• Koschel, M., Oed, D., Gerelsaikhan, T., Thomssen, R., Bruss, V. (2000). Hepatitis B Virus Core Gene Mutations Which Block Nucleocapsid Envelopment. J. Virol. 74: 1-7 [Abstract] [Full Text]  
• Hui, E. K.-W., Yi, Y. S., Lo, S. J. (1999). Hepatitis B viral core proteins with an N-terminal extension can assemble into core-like particles but cannot be enveloped. J. Gen. Virol. 80: 2647-2659 [Abstract] [Full Text]  
• Hui, E. K.-W., Chen, K.-L., Lo, S. J. (1999). Hepatitis B virus maturation is affected by the incorporation of core proteins having a C-terminal substitution of arginine or lysine stretches. J. Gen. Virol. 80: 2661-2671 [Abstract] [Full Text]  
• Cartier, C., Sivard, P., Tranchat, C., Decimo, D., Desgranges, C., Boyer, V. (1999). Identification of Three Major Phosphorylation Sites within HIV-1 Capsid. ROLE OF PHOSPHORYLATION DURING THE EARLY STEPS OF INFECTION. J. Biol. Chem. 274: 19434-19440 [Abstract] [Full Text]  
• Kann, M., Sodeik, B., Vlachou, A., Gerlich, W. H., Helenius, A. (1999). Phosphorylation-dependent Binding of Hepatitis B Virus Core Particles to the Nuclear Pore Complex. J. Cell Biol. 145: 45-55 [Abstract] [Full Text]  
• Kau, J.-H., Ting, L.-P. (1998). Phosphorylation of the Core Protein of Hepatitis B Virus by a 46-Kilodalton Serine Kinase. J. Virol. 72: 3796-3803 [Abstract] [Full Text]  
• Milich, D., McLachlan, A (1986). The nucleocapsid of hepatitis B virus is both a T-cell-independent and a T-cell-dependent antigen. Science 234: 1398-1401 [Abstract]