1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1

Biomol NMR Assign. 2016 Apr;10(1):31-4. doi: 10.1007/s12104-015-9631-1. Epub 2015 Aug 19.

Abstract

Chromatin remodelling proteins are an essential family of eukaryotic proteins. They harness the energy from ATP hydrolysis and apply it to alter chromatin structure in order to regulate all aspects of genome biology. Chromodomain helicase DNA-binding protein 1 (CHD1) is one such remodelling protein that has specialised nucleosome organising abilities and is conserved across eukaryotes. CHD1 possesses a pair of tandem chromodomains that directly precede the core catalytic Snf2 helicase-like domain, and a C-terminal SANT-SLIDE DNA-binding domain. We have identified an additional conserved domain in the C-terminal region of CHD1. Here, we report the backbone and side chain resonance assignments for this domain from human CHD1 at pH 6.5 and 25 °C (BMRB No. 25638).

Keywords: C-terminal domain; CHD1; Chromatin remodelling; Nucleosomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Isotopes
  • DNA Helicases / chemistry*
  • DNA-Binding Proteins / chemistry*
  • Humans
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Domains
  • Protein Structure, Secondary
  • Tritium

Substances

  • Carbon Isotopes
  • DNA-Binding Proteins
  • Nitrogen Isotopes
  • Tritium
  • DNA Helicases
  • CHD1 protein, human