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

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F12%3A00057508" target="_blank" >RIV/00216224:14740/12:00057508 - isvavai.cz</a>
Result on the web
<a href="http://www.ncbi.nlm.nih.gov/pubmed/22892239" target="_blank" >http://www.ncbi.nlm.nih.gov/pubmed/22892239</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1101/gad.192781.112" target="_blank" >10.1101/gad.192781.112</a>

Result language
angličtina
Original language name
Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1
Original language 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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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