Phosphorylation of the C-terminal domain of RNA polymerase II by the extracellular-signal-regulated protein kinase ERK2

Rhea-Beth Markowitz, April S. Hermann, Daniel F. Taylor, Li Yan He, Spencer Anthony-Cahill, Natalie G. Ahn, William S. Dynan

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Rat ERK2, an extracellular-signal-regulated protein kinase family member, phosphorylates RNA polymerase II in vitro. Phosphorylation occurs within the heptapeptide repeats of the C-terminal domain of the largest subunit, in a region important for regulation of transcriptional activity. Analysis of deletion mutants and synthetic peptides showed that ERK2 phosphorylation occurrs at multiple serine residues throughout the C-terminal domain, with no marked preference for consensus repeats versus naturally occurring variants. Our results are consistent with the idea that protein kinases in the extracellular-signal-regulated protein kinase family regulate transcription by direct phosphorylation of RNA polymerase II, but do not support a model where particular portions of the C-terminal domain are special targets of ERK phosphorylation.

Original languageEnglish (US)
Pages (from-to)1051-1057
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume207
Issue number3
DOIs
StatePublished - Feb 27 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Phosphorylation of the C-terminal domain of RNA polymerase II by the extracellular-signal-regulated protein kinase ERK2'. Together they form a unique fingerprint.

  • Cite this