RNA editing by base deamination: more enzymes, more targets, new mysteries.
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.
Gerber
A P
AP
Dept of Cell Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
Keller
W
W
D000243:Adenosine Deaminase / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003564:Cytidine Deaminase / Q000737:chemistry / Q000378:metabolism*; D003641:Deamination; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D009711:Nucleotides / Q000378:metabolism*; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D017393:RNA Editing; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D009711:Nucleotides; D012313:RNA; D000243:Adenosine Deaminase; D003564:Cytidine Deaminase