A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II - PubMed (original) (raw)

A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II

T J Guilfoyle. Plant Cell. 1989 Aug.

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.

PubMed Disclaimer

References

    1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
    1. Biochemistry. 1975 Oct 21;14(21):4639-45 - PubMed
    1. FEBS Lett. 1976 Dec 1;71(2):205-8 - PubMed
    1. Biochemistry. 1978 May 16;17(10):1860-6 - PubMed
    1. Biochemistry. 1978 Apr 4;17(7):1322-7 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources