Abstract:
:The hepadnavirus reverse transcriptase is a multifunction enzyme. In addition to its role in DNA synthesis, the polymerase is required for RNA packaging and also functions as the primer for minus-strand DNA synthesis. Previously, we demonstrated that the protein-priming activity of the polymerase requires a viral RNA segment, termed epsilon, which serves as a template for the synthesis of a short DNA oligomer that is covalently attached to the reverse transcriptase (G.-H. Wang and C. Seeger, J. Virol. 67:6507-6512, 1993). We now report that epsilon is sufficient for activation of the reverse transcriptase to prime DNA synthesis through the formation of a stable RNA-protein (RNP) complex. We also demonstrate that the binding reaction depends on sequence-specific determinants on epsilon. Moreover, our results indicate that two genetically separated domains of the reverse transcriptase are required for formation of the RNP complex. Finally, we show that the polymerase has a DNA polymerase activity in the absence of epsilon which does not depend on the protein-priming mechanism.
journal_name
J Viroljournal_title
Journal of virologyauthors
Wang GH,Zoulim F,Leber EH,Kitson J,Seeger Cdoi
10.1128/JVI.68.12.8437-8442.1994subject
Has Abstractpub_date
1994-12-01 00:00:00pages
8437-42issue
12eissn
0022-538Xissn
1098-5514journal_volume
68pub_type
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pub_type: 杂志文章
doi:10.1128/JVI.8.3.303-310.1971
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pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
doi:10.1128/JVI.68.11.7570-7574.1994
更新日期:1994-11-01 00:00:00
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journal_title:Journal of virology
pub_type: 杂志文章
doi:10.1128/JVI.63.11.4744-4755.1989
更新日期:1989-11-01 00:00:00