ArticleProceedings of the National Academy of Sciences of the United States of America1993
Expression of functional hepatitis B virus polymerase in yeast reveals it to be the sole viral protein required for correct initiation of reverse transcription.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Pregenomic RNA Launch Hepatitis B Virus Replication System Facilitates the Mechanistic Study of Antiviral Agents and Drug-Resistant Variants on Covalently Closed Circular DNA Synthesis.Journal of virology · 2022Article
- Predicted structure of the hepatitis B virus polymerase reveals an ancient conserved protein fold.Protein science : a publication of the Protein Society · 2022Article
- The Molecular and Structural Basis of HBV-resistance to Nucleos(t)ide Analogs.Journal of clinical and translational hepatology · 2014Review
- The hepatitis B virus ribonuclease H is sensitive to inhibitors of the human immunodeficiency virus ribonuclease H and integrase enzymes.PLoS pathogens · 2013Article
- TP-RT domain interactions of duck hepatitis B virus reverse transcriptase in cis and in trans during protein-primed initiation of DNA synthesis in vitro.Journal of virology · 2012Article
- In vitro epsilon RNA-dependent protein priming activity of human hepatitis B virus polymerase.Journal of virology · 2012Article
- The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication.Journal of virology · 2011Article
- High-level production of a functional recombinant hepatitis B virus polymerase in insect cells with a baculovirus expression system.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2007Article
- Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase.Journal of virology · 2005Article
- The 113th and 117th charged amino acids in the 5th alpha-helix of the HBV core protein are necessary for pgRNA encapsidation.Virus genes · 2003Article
- Viral strategies of translation initiation: ribosomal shunt and reinitiation.Progress in nucleic acid research and molecular biology · 2002Review
- Human hepatitis B virus polymerase interacts with the molecular chaperonin Hsp60.Journal of virology · 2001Article
- Evidence that the RNAseH activity of the duck hepatitis B virus is unable to act on exogenous substrates.BMC microbiology · 2001Article
- The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure.Journal of virology · 2000Article
- Hepatitis B virus biology.Microbiology and molecular biology reviews : MMBR · 2000Review
- The yeast retrotransposon Ty5 uses the anticodon stem-loop of the initiator methionine tRNA as a primer for reverse transcription.RNA (New York, N.Y.) · 1999Article
- Properties of monoclonal antibodies directed against hepatitis B virus polymerase protein.Journal of virology · 1999Article
- Mapping of the hepatitis B virus reverse transcriptase TP and RT domains by transcomplementation for nucleotide priming and by protein-protein interaction.Journal of virology · 1999Article
- Active human hepatitis B viral polymerase expressed in rabbit reticulocyte lysate system.Virus genes · 1999Article
- Duck hepatitis B virus nucleocapsids formed by N-terminally extended or C-terminally truncated core proteins disintegrate during viral DNA maturation.Journal of virology · 1998Article
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2 authors.
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Abstract
Replication of hepatitis B viruses proceeds by reverse transcription of an RNA intermediate, a reaction catalyzed by the virus-encoded polymerase (P protein). The reaction product is a partially duplex DNA whose (-)-strand is covalently linked to the P protein. Efforts to understand the mechanism of the reaction have been severely retarded by an inability to express functional polymerase outside of viral particles. Here we report the successful expression of enzymatically active polymerase in yeast cells, by fusing the P gene to coding sequences of the retrotransposon Ty1. The enzyme initiates correctly on viral RNA in yeast cells in vivo, producing nascent DNA chains covalently linked to protein, exactly as found in virus-infected cells. Replication complexes isolated from these yeast are enzymatically active in vitro, synthesizing DNA in a reaction that is actinomycin D-resistant but sensitive to RNase pretreatment. These results indicate that P protein is the sole viral protein required for the correct priming of reverse transcription and establish a tractable system for the biochemical dissection of the reaction.
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