A structural perspective of CTD function

  1. Anton Meinhart1,
  2. Tomislav Kamenski,
  3. Sabine Hoeppner,
  4. Sonja Baumli, and
  5. Patrick Cramer2
  1. Gene Center, University of Munich (LMU), Department of Chemistry and Biochemistry, 81377 Munich, Germany

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.

Keywords

Footnotes

  • Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1318105.

  • 1

    1 Present address: Max-Planck-Institute for Medical Research, Department of Biomolecular Mechanisms, Jahnstrasse 29, 69126 Heidelberg, Germany.

  • 2

    2 Corresponding author. E-MAIL cramer{at}LMB.uni-muenchen.de; FAX 49-89-2180-76999.

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