A structural perspective of CTD function.

Anton Meinhart, Tomislav Kamenski, Sabine Hoeppner, Sonja Baumli, Patrick Cramer

Journal: Genes & development 2005;19(12):1401-15

PMID: 15964991

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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.

Address: Department of Chemistry and Biochemistry, Gene Center, University of Munich (LMU), 81377 Munich, Germany.

DOI: 10.1101/gad.1318105

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MeSH Terms: Amino Acid Sequence, Binding Sites, Carrier Proteins, Models, Molecular, Molecular Sequence Data, Molecular Structure, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Protein Structure, Tertiary, RNA Polymerase II, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, mRNA Cleavage and Polyadenylation Factors