ArticleJournal of virology1997
Transcomplementation of nucleotide priming and reverse transcription between independently expressed TP and RT domains of the hepatitis B virus reverse transcriptase.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Hepatitis B Virus Nucleocapsid Assembly.Journal of molecular biology · 2025Review
- The HBV variant CpF97L supports the secretion of pgRNA-containing virions at a level much greater than WT HBV.Journal of virology · 2025Article
- Generation of Replication-Competent Hepatitis B Virus Harboring Tagged Polymerase for Visualization and Quantification of the Infection.Microbiology and immunology · 2025Article
- A molecular standard for circulating HBV RNA detection and quantification assays in patients with chronic hepatitis B.JHEP reports : innovation in hepatology · 2024Article
- Epitranscriptomic cytidine methylation of the hepatitis B viral RNA is essential for viral reverse transcription and particle production.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Significance of hepatitis B virus capsid dephosphorylation via polymerase.Journal of biomedical science · 2024Article
- Predicted structure of the hepatitis B virus polymerase reveals an ancient conserved protein fold.Protein science : a publication of the Protein Society · 2022Article
- Relaxing the restricted structural dynamics in the human hepatitis B virus RNA encapsidation signal enables replication initiation in vitro.PLoS pathogens · 2022Article
- Conservation of the HBV RNA element epsilon in nackednaviruses reveals ancient origin of protein-primed reverse transcription.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- DNA Engineering and Hepatitis B Virus Replication.Frontiers in microbiology · 2021Article
- Characterization of the Termini of Cytoplasmic Hepatitis B Virus Deproteinated Relaxed Circular DNA.Journal of virology · 2020Article
- Establishment of a system for finding inhibitors of ε RNA binding with the HBV polymerase.Genes to cells : devoted to molecular & cellular mechanisms · 2020Article
- Review
- Mapping of Functional Subdomains in the Terminal Protein Domain of Hepatitis B Virus Polymerase.Journal of virology · 2017Article
- In Vitro Assays for RNA Binding and Protein Priming of Hepatitis B Virus Polymerase.Methods in molecular biology (Clifton, N.J.) · 2017Article
- MicroRNA miR-204 and miR-1236 inhibit hepatitis B virus replication via two different mechanisms.Scientific reports · 2016Article
- Hepatitis B virus reverse transcriptase - Target of current antiviral therapy and future drug development.Antiviral research · 2015Review
- The Dual Role of an ESCRT-0 Component HGS in HBV Transcription and Naked Capsid Secretion.PLoS pathogens · 2015Article
- Hepadnavirus Genome Replication and Persistence.Cold Spring Harbor perspectives in medicine · 2015Review
- Sequences in the terminal protein and reverse transcriptase domains of the hepatitis B virus polymerase contribute to RNA binding and encapsidation.Journal of viral hepatitis · 2014Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Hepadnavirus polymerases initiate reverse transcription in a protein-primed reaction that involves the covalent linkage of the first deoxyribonucleotide to the polymerase polypeptide. We recently expressed human hepatitis B virus (HBV) reverse transcriptase (pol) in insect cells by using the recombinant baculovirus system. The purified protein is active in nucleotide priming and reverse transcription reactions. In this report, we demonstrate that the tyrosine residue at amino acid number 63 within the TP (terminal protein) domain of the polymerase is the site of covalent linkage of the first nucleotide of minus-strand DNA. Analysis of pol polypeptides with mutations in the TP and RT (reverse transcriptase) domains indicated that both domains were required for in vitro nucleotide priming activity. Polymerase proteins with mutations in the TP and RT domains were not capable of complementing each other in the nucleotide priming reaction, suggesting that transcomplementation between full-length polypeptides was not possible. However, when the TP and RT domains were expressed as separate polypeptides, they formed a highly stable complex that was active in nucleotide priming and reverse transcription. The presence of an epsilon stem-loop dramatically increased the nucleotide priming activity in transcomplementation assays, even though full-length pol displayed similar activities in the absence and presence of epsilon. These data raise the possibility that in the transcomplementation assay, epsilon may play a role in the formation of a functional complex between TP and RT, rather than being required only as the template for nucleotide priming. The results indicate that using the baculovirus system, it is possible to dissect the protein-protein and protein-RNA interactions required for HBV genome replication.
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