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PMID: 2535525 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

The Plant cell ·Vol. 1 ·No. 8 ·1989-08-00 ·Pages 827-36

Guilfoyle TJ

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.

MeSH Terms
Adenosine Triphosphate/metabolism Amino Acid Sequence Electrophoresis, Gel, Two-Dimensional Kinetics Magnesium/metabolism Molecular Sequence Data Phosphorylation Plant Proteins/metabolism Protein Kinases/isolation & purification,metabolism RNA Polymerase II/chemistry,metabolism Triticum/enzymology
Chemicals
Plant Proteins Adenosine Triphosphate Protein Kinases RNA Polymerase II Magnesium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Guilfoyle T J
Department of Biochemistry, University of Missouri, Columbia, 65211.
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Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
DOI
10.1105/tpc.1.8.827
Published
1989-08-00
Pages
827-36
Language
English
Region
England
NLM ID
9208688
PMCID
PMC159820
Subset
IM
Grants
NIGMS NIH HHS · GM37950 · United States
External Links
PubMed source DOI: 10.1105/tpc.1.8.827 PMC Full Text View journal details
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