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Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1
K. Kubicek, H. Cerna, P. Holub, J. Pasulka, D. Hrossova, F. Loehr, C. Hofr, S. Vanacova, R. Stefl,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 1987 to 6 months ago
Freely Accessible Science Journals
from 1987-03-01 to 6 months ago
PubMed Central
from 1997 to 6 months ago
Europe PubMed Central
from 1997 to 6 months ago
Open Access Digital Library
from 1987-03-01
Open Access Digital Library
from 1987-01-01
- MeSH
- Phosphorylation MeSH
- Models, Molecular MeSH
- RNA, Untranslated metabolism MeSH
- Proline metabolism MeSH
- RNA-Binding Proteins chemistry metabolism MeSH
- RNA Polymerase II metabolism MeSH
- Saccharomyces cerevisiae Proteins chemistry metabolism MeSH
- Saccharomyces cerevisiae cytology enzymology genetics metabolism MeSH
- Serine metabolism MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Cell Survival MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by Crossref.org
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