Redesignation of the RNase D activity associated with retroviral reverse transcriptase as RNase H

J Virol. 1994 Mar;68(3):1970-1. doi: 10.1128/JVI.68.3.1970-1971.1994.

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*.

MeSH terms

  • Endoribonucleases / classification
  • Escherichia coli Proteins*
  • RNA-Directed DNA Polymerase / metabolism*
  • Retroviridae / enzymology*
  • Ribonuclease H / classification
  • Ribonuclease III
  • Ribonucleases / classification*

Substances

  • Escherichia coli Proteins
  • RNA-Directed DNA Polymerase
  • Endoribonucleases
  • Ribonucleases
  • Ribonuclease III
  • ribonuclease III, E coli
  • Ribonuclease H