Kikuchi Y, Ando Y, Ichimura N, Noda A
Laboratory of Molecular Genetics, Mitsubishi Kasei Institute of Life Sciences, Machida, Tokyo.
J Biochem. 1989 Jun;105(6):974-8. doi: 10.1093/oxfordjournals.jbchem.a122790.
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.
从逆转录病毒中高度纯化并可商购的逆转录酶制剂含有一种3'至5'外切核糖核酸酶活性，能够水解具有3'-OH末端的合成同聚核糖核苷酸。对劳斯相关病毒2逆转录酶制剂的外切核糖核酸酶活性进行了进一步表征。这种外切核糖核酸酶活性从3'-OH末端以核酸外切方式切割聚（C）和聚（U），产生核苷5'-磷酸。聚（A）、聚（G）、环状聚核糖核苷酸和双链聚核糖核苷酸不会被该活性水解。这是一种新型的外切核糖核酸酶活性。
