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A structural perspective of CTD function

MPG-Autoren
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Meinhart,  Anton
mRNA Processing, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Meinhart, A., Kamenski, T., Hoeppner, S., Baumli, S., & Cramer, P. (2005). A structural perspective of CTD function. Genes and Development, 19(12), 1401-1415. doi:10.1101/gad.1318105.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-002A-C3FD-3
Zusammenfassung
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.