Redesignation of the RNase D activity associated with retroviral reverse transcriptase as RNase H.
In the presence of Mn2+, reverse transcriptase of both human immunodeficiency virus and murine leukemia virus hydrolyzes duplex RNA. However, designating this novel activity RNase D conflicts with Escherichia coli RNase D, which participates in tRNA processing. On the basis of its location in the RNase H domain, we propose that this novel retroviral activity be redesignated RNase H*.
Hostomsky
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Agouron Pharmaceuticals Inc., San Diego, California 92121.
Hughes
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Goff
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Le Grice
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SF
D004722:Endoribonucleases / Q000145:classification; D029968:Escherichia coli Proteins; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D012190:Retroviridae / Q000201:enzymology*; D016914:Ribonuclease H / Q000145:classification; D043244:Ribonuclease III; D012260:Ribonucleases / Q000145:classification*
D029968:Escherichia coli Proteins; D012194:RNA-Directed DNA Polymerase; D004722:Endoribonucleases; D012260:Ribonucleases; D043244:Ribonuclease III; C468366:ribonuclease III, E coli; D016914:Ribonuclease H