Phosphorylation of the C-terminal domain of RNA polymerase II plays central roles in the integrated events of eucaryotic gene expression

J Biochem. 2007 May;141(5):601-8. doi: 10.1093/jb/mvm090. Epub 2007 Apr 3.

Abstract

RNA polymerase II (Pol II) is the only polymerase to possess heptapeptide repeats in the C-terminal domain (CTD) of its large subunit. During transcription, CTD phopshorylation occurs and is maintained from initiation to termination. To date, among the three known CTD kinases possessing CDK-cyclin pairs, TFIIH is the only one that forms a preinitiation complex. The Mediator complex plays essential roles in transcription initiation and during the transition from initiation to elongation by transmitting signals from transcriptional activators to Pol II. P-TEFb specifically plays a role in transcription elongation. TFIIH and mediator phosphorylate serine 5 (Ser5) of the CTD heptapeptide repeat sequence, whereas P-TEFb phosphorylates serine 2 (Ser2). Recently, it has become clear that CTD phosphorylation is not only essential for transcription, but also as a platform for RNA processing and chromatin regulation. In this review, we discuss the central role of Pol II phosphorylation in these nuclear events.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Humans
  • Models, Biological
  • Models, Molecular
  • Nuclear Proteins / physiology
  • Nucleotidyltransferases / metabolism
  • Phosphorylation
  • Protein Conformation / drug effects
  • Protein Structure, Tertiary / physiology
  • RNA Polymerase II / metabolism*
  • RNA Precursors / metabolism
  • RNA Processing, Post-Transcriptional / physiology
  • RNA Splicing / physiology
  • Transcription, Genetic / physiology*
  • mRNA Guanylyltransferases

Substances

  • Adaptor Proteins, Signal Transducing
  • Nuclear Proteins
  • PCIF1 protein, human
  • RNA Precursors
  • Nucleotidyltransferases
  • RNA Polymerase II
  • mRNA Guanylyltransferases