1H, 13C, and 15N resonance assignments for the CTD-interacting domain of Nrd1 bound to Ser5-phosphorylated CTD of RNA polymerase II

Biomol NMR Assign. 2011 Oct;5(2):203-5. doi: 10.1007/s12104-011-9300-y. Epub 2011 Feb 26.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Down-Regulation
  • Isotopes / chemistry
  • Nuclear Magnetic Resonance, Biomolecular*
  • Peptides / chemistry
  • Peptides / metabolism
  • Phosphorylation
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA Polymerase II / chemistry*
  • RNA Polymerase II / metabolism
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Serine / chemistry
  • Serine / metabolism

Substances

  • Isotopes
  • NRD1 protein, S cerevisiae
  • Peptides
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae Proteins
  • Serine
  • RNA Polymerase II