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Updated: Jul 13, 2026

RNA Catalyst as a Reporter for Screening Drugs against RNA Editing in Trypanosomes
Published on: July 22, 2014
RNA editing uridylyltransferases of trypanosomatids
Ruslan Aphasizhev1, Inna Aphasizheva
1Department of Microbiology and Molecular Genetics, University of California, Irvine, California, USA.
Abstract:
Terminal RNA uridylyltransferases (TUTases) catalyze the transfer of UMP residues to the 3' hydroxyl group of RNA. These enzymes belong to the DNA polymerase beta superfamily, which also includes poly(A) polymerases, CCA-adding enzymes, and other nucleotidyltransferases. Studies of uridylyl insertion/deletion RNA editing in mitochondria of trypanosomatids provided the first examples of biological functions for TUTases: posttranscriptional uridylylation of guide RNAs by RNA editing TUTase 1 (RET1) and U-insertion mRNA editing by RNA editing TUTase 2 (RET2). The editing TUTases are unified by the presence of conserved catalytic and nucleotide base recognition domains, yet differ substantially in auxiliary function-specific domains, quaternary structure, RNA substrate specificity, and processivity. This chapter describes isolation of TUTases and their complexes from trypanosomatids, methods used for analysis of interactions involving RET1 and RET2, purification of recombinant proteins, and enzyme kinetic assays.
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