CEITEC-Central European Institute of Technology, Masaryk University, Brno, 62500, Czech Republic.
Genes Dev. 2012 Sep 1;26(17):1891-6. doi: 10.1101/gad.192781.112. Epub 2012 Aug 14.
Recruitment of appropriate RNA processing factors to the site of transcription is controlled by post-translational modifications of the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Here, we report the solution structure of the Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream pSer5-Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface diminish binding affinity and impair processing or degradation of noncoding RNAs. These findings underpin the interplay between covalent and noncovalent changes in the CTD structure that constitute the CTD code.
RNA 聚合酶 II(RNAP II)C 端结构域(CTD)的翻译后修饰控制着适当的 RNA 加工因子在转录部位的募集。在这里,我们报告了 Ser5 磷酸化(pSer5)CTD 与 Nrd1 结合的溶液结构。该结构揭示了 Nrd1 对 pSer5 的直接识别,这需要 CTD 中上游 pSer5-Pro6 肽基脯氨酰键的顺式构象。复合物界面处的突变会降低结合亲和力,并损害非编码 RNA 的加工或降解。这些发现为 CTD 结构中的共价和非共价变化之间的相互作用提供了基础,这种相互作用构成了 CTD 密码。