| Literature DB >> 15964991 |
Anton Meinhart1, Tomislav Kamenski, Sabine Hoeppner, Sonja Baumli, Patrick Cramer.
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.Entities:
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Year: 2005 PMID: 15964991 DOI: 10.1101/gad.1318105
Source DB: PubMed Journal: Genes Dev ISSN: 0890-9369 Impact factor: 11.361