Exoribonuclease activity of purified reverse transcriptase preparations from retroviruses

Yo Kikuchi, Yumiko Ando, Nobuko Ichimura, Akihiro Noda

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Highly purified and commercially available preparations of reverse transcriptases from retroviruses contain a 3′ to 5′ exoribonuclease activity capable of hydrolyzing synthetic homopolyribonucleotides having a 3′ -OH end. The exoribonuclease activity of reverse transcriptase preparations from Rous associated virus-2 was further characterized. This exoribonuclease activity cleaves poly(C) and poly(U) exonucleolytically from the 3′-OH end to produce nucleoside 5′-phosphates. Poly(A), poly(G), circular polyribonucleotide, and double-stranded polyribonucleotide were not hydrolyzed by the activity. This is a novel type of exoribonuclease activity.

Original languageEnglish
Pages (from-to)974-978
Number of pages5
JournalJournal of Biochemistry
Issue number6
Publication statusPublished - 1989 Jun
Externally publishedYes


ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

Kikuchi, Y., Ando, Y., Ichimura, N., & Noda, A. (1989). Exoribonuclease activity of purified reverse transcriptase preparations from retroviruses. Journal of Biochemistry, 105(6), 974-978.