Exoribonuclease activity of purified reverse transcriptase preparations from retroviruses.
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.
Kikuchi
Y
Y
Laboratory of Molecular Genetics, Mitsubishi Kasei Institute of Life Sciences, Machida, Tokyo.
Ando
Y
Y
Ichimura
N
N
Noda
A
A
D002021:Buffers; D002852:Chromatography, Ion Exchange; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism; D005095:Exoribonucleases / Q000378:metabolism*; D006868:Hydrolysis; D011072:Poly U / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase / Q000302:isolation & purification / Q000378:metabolism*; D012190:Retroviridae / Q000201:enzymology*; D013379:Substrate Specificity
D002021:Buffers; D012367:RNA, Viral; D011072:Poly U; D012194:RNA-Directed DNA Polymerase; D004259:DNA-Directed DNA Polymerase; D005095:Exoribonucleases