An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the splice junction 2'-phosphate from ligated tRNA to an acceptor molecule

J Biol Chem. 1991 Jun 25;266(18):11986-92.


An enzyme from Saccharomyces cerevisiae which removes the splice junction 2'-phosphate from ligated tRNA appears to require NAD+. This two-component enzyme has been previously implicated in tRNA splicing because of its specificity for substrates bearing an internal 2'-phosphate and because of the absence of other observed proteins that can efficiently catalyze the same activity after fractionation of the extracts. We show here that component I of this enzyme is heat-stable, chromatographs as a small molecule, can be substituted efficiently by NAD+, and comigrates with NAD+ on a reversed-phase column. Dephosphorylation of ligated tRNA in the presence of component I or NAD+ is accompanied by stoichiometric transfer of the splice junction 2'-phosphate to an unidentified acceptor molecule.

Publication types

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

MeSH terms

  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • NAD / metabolism*
  • Organophosphorus Compounds / metabolism*
  • Phosphorylation
  • RNA Splicing*
  • RNA, Transfer / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Substrate Specificity


  • Organophosphorus Compounds
  • NAD
  • RNA, Transfer