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

A P Gerber, W Keller

Journal: Trends in biochemical sciences 2001;26(6):376-84

PMID: 11406411

Full Text on Elsevier Science View on PubMed

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.

Address: Dept of Cell Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.

DOI: 10.1016/s0968-0004(01)01827-8

Link outs

Free resources

Other Literature Sources:

https://www.lens.org/lens/search/patent/list?q=ref...

Molecular Biology Databases:

http://flybase.org/cgi-bin/uniq.html?db=fbrf&field...

Subscription / membership required

Full Text Sources:

https://linkinghub.elsevier.com/retrieve/pii/S0968...

MeSH Terms: Adenosine Deaminase, Amino Acid Sequence, Base Sequence, Cytidine Deaminase, Deamination, Molecular Sequence Data, Nucleic Acid Conformation, Nucleotides, RNA, RNA Editing, Sequence Homology, Amino Acid, Substrate Specificity