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. 1989 Jun;105(6):974-8.
doi: 10.1093/oxfordjournals.jbchem.a122790.

Exoribonuclease activity of purified reverse transcriptase preparations from retroviruses

Y Kikuchi  1 , Y Ando, N Ichimura, A Noda
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Free article

Exoribonuclease activity of purified reverse transcriptase preparations from retroviruses

Y Kikuchi et al. J Biochem. 1989 Jun.
Free article

Abstract

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.

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