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

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

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  • 1Department of Biochemistry, University of Rochester, School of Medicine and Dentistry, New York 14642.


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.

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