Reference: Zillmann M, et al. (1992) HeLa cells contain a 2'-phosphate-specific phosphotransferase similar to a yeast enzyme implicated in tRNA splicing. J Biol Chem 267(15):10289-94

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Abstract


We have previously shown that HeLa cells contain activities implicated in tRNA splicing in yeast, a ligase capable of joining tRNA half-molecules and an NAD-dependent activity capable of removing the 2'-phosphate created at the splice junction by the ligase (Zillmann, M., Gorovsky, M.A., and Phizicky, E.M. (1991) Mol. Cell. Biol. 11, 5410-5416). We show here that removal of the splice junction 2'-phosphate is, as in yeast, a 2'-phosphate-specific phosphotransfer reaction that produces the same, as yet unidentified, small molecule. This enzyme is highly specific for oligomeric substrates having internal 2'-phosphates. Oligomers bearing terminal 2'-phosphates are at least 50-fold less reactive and those bearing 5'- or 3'-terminal phosphates are at least 600-fold less reactive. The requirement for an internal 2'-phosphate can be satisfied by a substrate as small as a dimer.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, Non-P.H.S.
Authors
Zillmann M, Gorovsky MA, Phizicky EM
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