Informace o publikaci

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

Autoři

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

Druh Článek v odborném periodiku
Časopis / Zdroj Genes & Development
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://www.ncbi.nlm.nih.gov/pubmed/22892239
Doi http://dx.doi.org/10.1101/gad.192781.112
Obor Biofyzika
Klíčová slova RNA polymerase II; CTD code; phosphorylation; proline isomerization; RNA processing and degradation; NMR spectroscopy; structure
Přiložené soubory
Popis 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.
Související projekty: