Publication details

Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1

Authors

KUBÍČEK Karel ČERNÁ Hana HOLUB Peter PASULKA Josef HROŠŠOVÁ Dominika LOEHR Frank HOFR Ctirad VAŇÁČOVÁ Štěpánka ŠTEFL Richard

Year of publication 2012
Type Article in Periodical
Magazine / Source Genes & Development
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.ncbi.nlm.nih.gov/pubmed/22892239
Doi http://dx.doi.org/10.1101/gad.192781.112
Field Biophysics
Keywords RNA polymerase II; CTD code; phosphorylation; proline isomerization; RNA processing and degradation; NMR spectroscopy; structure
Attached files
Description 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.
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