Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2

Nature. 1989 Jun 29;339(6227):679-84. doi: 10.1038/339679a0.


Actively transcribing eukaryotic RNA polymerase II is highly phosphorylated on its repetitive carboxyl-terminal domain. We have isolated a protein kinase that phosphorylates serine residues in this repetitive domain. A component of this kinase is cdc2, the product of a cell-cycle control gene previously shown to be a component of M-phase-promoting factor and M-phase-specific histone H1 kinase. This observation suggests a role for the cdc2 protein kinase in transcriptional regulation.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • CDC2 Protein Kinase
  • Cell Cycle
  • Gene Expression Regulation
  • Humans
  • Mice
  • Molecular Sequence Data
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Kinases / genetics
  • Protein Kinases / isolation & purification
  • Protein Kinases / metabolism*
  • RNA Polymerase II / metabolism*
  • Species Specificity
  • Transcription, Genetic


  • Phosphoproteins
  • Protein Kinases
  • carboxy-terminal domain kinase
  • CDC2 Protein Kinase
  • RNA Polymerase II