Multiple terminal uridylyltransferases of trypanosomes

FEBS Lett. 2004 Aug 13;572(1-3):15-8. doi: 10.1016/j.febslet.2004.07.004.

Abstract

The transferase activities that add uridylyl residues to RNA have been reported in several unicellular and metazoan organisms. Thus far, the two terminal uridylyltransferases (TUTases) involved in uridine insertion/deletion mRNA editing in mitochondria of trypanosomes were the only known enzymes with confirmed UTP specificity. Here, we demonstrate that protein sequences of editing TUTases may be used to predict novel UTP-specific enzymes by data mining. The highest-scoring open reading frame from Trypanosoma brucei was expressed and recombinant protein purified. This enzyme catalyzes a processive UMP incorporation and is not localized to the mitochondria suggesting a non-editing biological function.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Conserved Sequence
  • Leishmania / enzymology
  • Molecular Sequence Data
  • Open Reading Frames / genetics
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism
  • RNA Nucleotidyltransferases / chemistry
  • RNA Nucleotidyltransferases / genetics*
  • RNA Nucleotidyltransferases / metabolism*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Trypanosoma brucei brucei / enzymology*
  • Trypanosoma brucei brucei / genetics
  • Uridine Triphosphate / metabolism*

Substances

  • Protozoan Proteins
  • RNA Nucleotidyltransferases
  • UTP-RNA uridylyltransferase
  • Uridine Triphosphate

Associated data

  • GENBANK/AY672414
  • GENBANK/BK005536