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Originally published In Press as doi:10.1074/jbc.M208895200 on November 19, 2002

J. Biol. Chem., Vol. 278, Issue 2, 1201-1205, January 10, 2003
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Kinetics of Synthesis and Turnover of the Duck Hepatitis B Virus Reverse Transcriptase*

Ermei YaoDagger and John E. TavisDagger §

From the Dagger  Department of Molecular Microbiology and Immunology and from the § Saint Louis University Liver Center, Saint Louis University School of Medicine, St. Louis, Missouri 63104

Hepadnaviral reverse transcription occurs in subviral capsids in which the core protein surrounds the reverse transcriptase ("polymerase") and the pregenomic RNA. The pregenomic RNA is the template for reverse transcription and also the bicistronic mRNA for core and polymerase. The pregenomic RNA structure and the capsid stoichiometry imply that vastly more core would be translated than polymerase. Previously, we found that duck hepatitis B virus polymerase unexpectedly accumulates in the cytoplasm (Yao, E., Gong, Y., Chen, N., and Tavis, J. E. (2000) J. Virol. 74, 8648-8657). The production mechanism and function of the excess polymerase are unknown. Here, we determined the kinetics of expression and degradation of polymerase and core in cells producing virus. Polymerase was translated 10% as rapidly as core, the half-life of nonencapsidated polymerase was very short, core had a very long half-life, and very few polymerase molecules were encapsidated. The presence of excess polymerase indicates that the translation rate of the polymerase is not limiting for encapsidation. Therefore, encapsidation must be regulated by other events, most likely binding of the polymerase to the pregenomic RNA. These data support the hypothesis that polymerase may have functions beyond copying the viral genome by demonstrating that the polymerase is a cytoplasmic protein that is only rarely encapsidated.


* This work was supported by Grants AI38447 and CA91327 from the National Institutes of Health (to J. E. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, 1402 S. Grand Blvd., St. Louis, MO 63104. Tel.: 314-577-8441; Fax: 314-773-3403; E-mail: tavisje@slu.edu.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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