Binding and dissociation of human topoisomerase I with hairpin-loop RNAs: implications for the regulation of HIV-1 replication

Biochem Biophys Res Commun. 2002 Sep 27;297(3):593-9. doi: 10.1016/s0006-291x(02)02247-7.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Base Sequence
  • Binding Sites
  • DNA Primers
  • DNA Replication*
  • DNA Topoisomerases, Type I / chemistry*
  • DNA Topoisomerases, Type I / metabolism*
  • HIV-1* / genetics*
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • RNA, Viral / chemistry*
  • RNA, Viral / genetics
  • RNA, Viral / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Transcription, Genetic
  • Virion / enzymology
  • Virion / genetics
  • Virus Replication / physiology*

Substances

  • DNA Primers
  • RNA, Viral
  • Recombinant Proteins
  • Adenosine Triphosphate
  • DNA Topoisomerases, Type I