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J. Biol. Chem., Vol. 261, Issue 15, 6684-6693, 05, 1986
L Pick and J Hurwitz
An RNA ligase that catalyzes the formation of a 2'-phosphomonoester-
3',5'-phosphodiester bond in the presence of ATP and Mg2+ was purified
approximately 6000-fold from raw wheat germ. A 5'-hydroxyl polynucleotide
kinase activity copurified with RNA ligase through all chromatographic
steps. Both activities cosedimented upon glycerol gradient centrifugation
even in the presence of high salt and urea. RNA ligase and kinase
activities sedimented as a single peak on glycerol gradients with a
sedimentation coefficient of 6.2 S. The purified polynucleotide kinase
activity required dithiothreitol and a divalent cation for activity and was
inhibited by pyrophosphate and by ADP. The kinase phosphorylated a variety
of 5'-hydroxyl-terminated polynucleotide chains including some that were
substrates for the RNA ligase (e.g. 2',3'-cyclic phosphate-terminated
poly(A)) and others that were not ligase substrates (e.g. DNA or RNA
containing 3'-hydroxyl termini). RNA molecules containing either
5'-hydroxyl or 5'-phosphate and 2',3'-cyclic or 2'-phosphate termini were
substrates for the purified RNA ligase activity. The rate of ligation of
5'-hydroxyl- terminated RNA chains was greater than that of
5'-phosphate-terminated molecules, suggesting that an interaction between
the wheat germ kinase and ligase activities occurs during the course of
ligation.
Purification of wheat germ RNA ligase. I. Characterization of a ligase- associated 5'-hydroxyl polynucleotide kinase activity
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