Meinhart Anton, Kamenski Tomislav, Hoeppner Sabine, Baumli Sonja, Cramer Patrick
Department of Chemistry and Biochemistry, Gene Center, University of Munich (LMU), 81377 Munich, Germany.
Genes Dev. 2005 Jun 15;19(12):1401-15. doi: 10.1101/gad.1318105.
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.
RNA聚合酶II（Pol II）的C末端结构域（CTD）通过与参与mRNA生物合成的蛋白质结合来整合核内事件。CTD结合蛋白识别特定的CTD磷酸化模式，由于CTD修饰酶的作用，这种模式在转录周期中会发生变化。目前，对CTD结合蛋白和修饰蛋白的结构与功能研究揭示了一些CTD功能的潜在机制。蛋白质通过接触磷酸化残基直接识别CTD磷酸化模式，或者不接触磷酸基团间接识别。CTD激酶和磷酸酶的催化机制已为人所知，但这些酶对CTD的特异性基础仍有待了解。
