Tails of intrigue: phosphorylation of RNA polymerase II mediates histone methylation

Cell. 2003 May 16;113(4):429-32. doi: 10.1016/s0092-8674(03)00360-x.

Abstract

Histone lysine methylation plays a key role in the organization of chromatin structure and the regulation of gene expression. Recent studies demonstrated that the yeast Set1 and Set2 histone methyltransferases are recruited to mRNA coding regions by the PAF transcription elongation complex in a manner dependent upon the phosphorylation state of the carboxy-terminal domain of RNA polymerase II. These studies define an unexpected link between transcription elongation and histone methylation.

Publication types

  • Review

MeSH terms

  • Animals
  • Chromatin / genetics
  • Chromatin / metabolism*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Eukaryotic Cells / enzymology*
  • Gene Expression Regulation, Enzymologic / genetics*
  • Genes, Regulator / genetics
  • Histone-Lysine N-Methyltransferase
  • Histones / genetics
  • Histones / metabolism*
  • Humans
  • Methylation
  • Phosphorylation
  • RNA Polymerase II / genetics
  • RNA Polymerase II / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • Chromatin
  • DNA-Binding Proteins
  • Histones
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Histone-Lysine N-Methyltransferase
  • SET1 protein, S cerevisiae
  • RNA Polymerase II