1H, 13C, and 15N resonance assignments for the CTD-interacting domain of Nrd1 bound to Ser5-phosphorylated CTD of RNA polymerase II
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Down-Regulation MeSH
- Phosphorylation MeSH
- Isotopes chemistry MeSH
- Nuclear Magnetic Resonance, Biomolecular * MeSH
- Peptides chemistry metabolism MeSH
- RNA-Binding Proteins chemistry metabolism MeSH
- RNA Polymerase II chemistry metabolism MeSH
- Saccharomyces cerevisiae Proteins chemistry metabolism MeSH
- Serine chemistry metabolism MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Isotopes MeSH
- NRD1 protein, S cerevisiae MeSH Browser
- Peptides MeSH
- RNA-Binding Proteins MeSH
- RNA Polymerase II MeSH
- Saccharomyces cerevisiae Proteins MeSH
- Serine MeSH
In this article, we report the resonance assignment of CTD-interacting domain (CID) of pre-mRNA down-regulation (Nrd)1 bound to Ser5-phosphorylated CTD (pSer5) of RNA Polymerase II. The presented assignment of backbone and side-chain resonances of the Nrd1 CID proton, carbon and nitrogen nuclei will allow studies of the structure and interaction of CID with carboxy-terminal domain (CTD) of the RNA polymerase II.
References provided by Crossref.org
Molecular basis for coordinating transcription termination with noncoding RNA degradation
Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1
