A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II. (original) (raw)
Journal Article
Department of Biochemistry, University of Missouri, Columbia, 65211.
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Published:
01 August 1989
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T J Guilfoyle, A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II., The Plant Cell, Volume 1, Issue 8, August 1989, Pages 827–836, https://doi.org/10.1105/tpc.1.8.827
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Abstract
A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase IIA has been partially purified and characterized. The kinase has a native molecular weight of about 200 kilodaltons. This kinase utilizes Mg2+ and ATP and transfers about 20 phosphates to the heptapeptide repeats Pro-Thr-Ser-Pro-Ser-Tyr-Ser in the carboxyl-terminal domain of the 220-kilodalton subunit of soybean RNA polymerase II. This phosphorylation results in a mobility shift of the 220-kilodalton subunits of a variety of eukaryotic RNA polymerases to polypeptides ranging in size from greater than 220 kilodaltons to 240 kilodaltons on sodium dodecyl sulfate-polyacrylamide gels. The phosphorylation is highly specific to the heptapeptide repeats since a degraded subunit polypeptide of 180 kilodaltons that lacks the heptapeptide repeats is poorly phosphorylated. Synthetic heptapeptide repeat multimers inhibit the phosphorylation of the 220-kilodalton subunit.
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© 1989 by American Society of Plant Biologists
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