A structural perspective of CTD function

Genes Dev. 2005 Jun 15;19(12):1401-15. doi: 10.1101/gad.1318105.

Abstract

The C-terminal domain (CTD) of RNA polymerase II (Pol II) integrates nuclear events by binding proteins involved in mRNA biogenesis. CTD-binding proteins recognize a specific CTD phosphorylation pattern, which changes during the transcription cycle, due to the action of CTD-modifying enzymes. Structural and functional studies of CTD-binding and -modifying proteins now reveal some of the mechanisms underlying CTD function. Proteins recognize CTD phosphorylation patterns either directly, by contacting phosphorylated residues, or indirectly, without contact to the phosphate. The catalytic mechanisms of CTD kinases and phosphatases are known, but the basis for CTD specificity of these enzymes remains to be understood.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Carrier Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Phosphoprotein Phosphatases / chemistry
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Protein Kinases / chemistry
  • Protein Kinases / metabolism
  • Protein Structure, Tertiary
  • RNA Polymerase II / chemistry*
  • RNA Polymerase II / genetics
  • RNA Polymerase II / metabolism
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • mRNA Cleavage and Polyadenylation Factors

Substances

  • Carrier Proteins
  • SSU72 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • mRNA Cleavage and Polyadenylation Factors
  • Protein Kinases
  • carboxy-terminal domain kinase
  • RNA Polymerase II
  • Phosphoprotein Phosphatases
  • carboxy-terminal domain phosphatase