title: Redesignation of the RNase D activity associated with retroviral reverse transcriptase as RNase H.
abstract: 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*.
authors.affiliation: Agouron Pharmaceuticals Inc., San Diego, California 92121.
authors.forename: Z
authors.initials: Z
authors.lastname: Hostomsky
authors.forename: S H
authors.initials: SH
authors.lastname: Hughes
authors.forename: S P
authors.initials: SP
authors.lastname: Goff
authors.forename: S F
authors.initials: SF
authors.lastname: Le Grice
mesh_terms: 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*
chemical_list: D029968:Escherichia coli Proteins; D012194:RNA-Directed DNA Polymerase; D004722:Endoribonucleases; D012260:Ribonucleases; D043244:Ribonuclease III; C468366:ribonuclease III, E coli; D016914:Ribonuclease H