Preferential selection of adenosines for modification by double-stranded RNA adenosine deaminase

EMBO J. 1994 Dec 1;13(23):5701-11. doi: 10.1002/j.1460-2075.1994.tb06908.x.


Double-stranded RNA adenosine deaminase (dsRAD), previously called the double-stranded RNA (dsRNA) unwinding/modifying activity, modifies adenosines to inosines within dsRNA. We used ribonuclease U2 and a mutant of ribonuclease T1 to map the sites of modification in several RNA duplexes. We found that dsRAD had a 5' neighbor preference (A = U > C > G) but no apparent 3' neighbor preference. Further, the proximity of the strand termini affected whether an adenosine was modified. Most importantly, dsRAD exhibited selectivity, modifying a minimal number of adenosines in short dsRNAs. Our results suggest that the specific editing of glutamate receptor subunit B mRNA could be performed in vivo by dsRAD without the aid of specificity factors, and support the hypothesis that dsRAD is responsible for hypermutations in certain RNA viruses.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine / metabolism*
  • Adenosine Deaminase / metabolism*
  • Base Sequence
  • Deamination
  • Endoribonucleases / metabolism
  • Inosine / metabolism
  • Molecular Sequence Data
  • Oligoribonucleotides
  • RNA / chemical synthesis
  • RNA / metabolism
  • RNA Editing
  • RNA-Binding Proteins / metabolism*
  • Receptors, Glutamate / genetics
  • Receptors, Glutamate / metabolism
  • Ribonuclease T1 / metabolism


  • Oligoribonucleotides
  • RNA-Binding Proteins
  • Receptors, Glutamate
  • Inosine
  • RNA
  • Endoribonucleases
  • Ribonuclease T1
  • ribonuclease U2
  • ADAR protein, human
  • ADARB1 protein, human
  • Adenosine Deaminase
  • Adenosine