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

Tom J. Guilfoyle | Zendy

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

Author(s) -

Tom J. Guilfoyle

Publication year - 1989

Publication title -

the plant cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.324

H-Index - 341

eISSN - 1532-298X

pISSN - 1040-4651

DOI - 10.1105/tpc.1.8.827

Subject(s) - biology , protein subunit , phosphorylation , polymerase , biochemistry , microbiology and biotechnology , protein kinase a , rna polymerase , kinase , rna polymerase ii , rna , enzyme , gene , gene expression , promoter

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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