RNA editing by base deamination: more enzymes, more targets, new mysteries

Trends Biochem Sci. 2001 Jun;26(6):376-84. doi: 10.1016/s0968-0004(01)01827-8.

Abstract

The posttranscriptional modification of messenger RNA precursors (pre-mRNAs) by base deamination can profoundly alter the physiological function of the encoded proteins. The recent identification of tRNA-specific adenosine deaminases (ADATs) has led to the suggestion that these enzymes, as well as the cytidine and adenosine deaminases acting on pre-mRNAs (CDARs and ADARs), belong to a superfamily of RNA-dependent deaminases. This superfamily might have evolved from an ancient cytidine deaminase. This article reviews the reactions catalysed by these enzymes and discusses their evolutionary relationships.

Publication types

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

MeSH terms

  • Adenosine Deaminase / chemistry
  • Adenosine Deaminase / metabolism*
  • Amino Acid Sequence
  • Base Sequence
  • Cytidine Deaminase / chemistry
  • Cytidine Deaminase / metabolism*
  • Deamination
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Nucleotides / metabolism*
  • RNA / chemistry
  • RNA / metabolism
  • RNA Editing*
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Nucleotides
  • RNA
  • Adenosine Deaminase
  • Cytidine Deaminase