Mammalian RNA-dependent deaminases and edited mRNAs

Curr Opin Cell Biol. 1997 Jun;9(3):343-9. doi: 10.1016/s0955-0674(97)80006-3.


The past year has witnessed major progress in the field of mammalian nuclear RNA editing. Two new sequence-related RNA-dependent adenosine deaminases, distantly related to the previously characterized double-stranded RNA adenosine deaminase DRADA/dsRAD, have been molecularly characterized. One of these deaminases edits in vitro with precision for the molecular determinant that controls the Ca2+ permeability of fast synaptic glutamate-gated cation channels. This deaminase, like DRADA, is expressed in many tissues and the search is now on for more substrates of these RNA-editing enzymes. Moreover, the physiological role of the apolipoprotein B RNA editing enzyme APOBEC-1 has been investigated in genetically manipulated mice.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • APOBEC-1 Deaminase
  • Adenosine Deaminase / metabolism*
  • Animals
  • Animals, Genetically Modified
  • Apolipoproteins B / genetics
  • Cytidine Deaminase / metabolism*
  • Ion Channels / genetics
  • Mammals
  • Mice
  • RNA Editing*
  • RNA, Messenger / metabolism
  • Receptors, AMPA / genetics
  • Substrate Specificity


  • Apolipoproteins B
  • Ion Channels
  • RNA, Messenger
  • Receptors, AMPA
  • AICDA (activation-induced cytidine deaminase)
  • APOBEC-1 Deaminase
  • Apobec1 protein, mouse
  • Adenosine Deaminase
  • Cytidine Deaminase
  • glutamate receptor ionotropic, AMPA 2