Abstract
Cellular topoisomerase I has been reported to be present in retroviral particles and to enhance viral cDNA synthesis; however, the mechanisms involved remain unknown. In the present study, it has been demonstrated that human topoisomerase I combines with a stem-loop RNA and that the bound topoisomerase I can be dissociated from RNA substrates in the presence of ATP. In addition, in vitro cleaved synthetic RNA bound by topoisomerase I is subsequently relegated when the topoisomerase I is dissociated by ATP. A mechanism is proposed in which human topoisomerase I is carried into virions and regulates the repair of genomic RNA by its ligation activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Base Sequence
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Binding Sites
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DNA Primers
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DNA Replication*
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DNA Topoisomerases, Type I / chemistry*
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DNA Topoisomerases, Type I / metabolism*
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HIV-1* / genetics*
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Humans
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Kinetics
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Molecular Sequence Data
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Nucleic Acid Conformation
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RNA, Viral / chemistry*
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RNA, Viral / genetics
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RNA, Viral / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Transcription, Genetic
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Virion / enzymology
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Virion / genetics
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Virus Replication / physiology*
Substances
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DNA Primers
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RNA, Viral
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Recombinant Proteins
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Adenosine Triphosphate
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DNA Topoisomerases, Type I