Backbone assignment of the little finger domain of a Y-family DNA polymerase

Biomol NMR Assign. 2011 Oct;5(2):195-8. doi: 10.1007/s12104-011-9298-1. Epub 2011 Feb 20.


Sulfolobus solfataricus DNA polymerase IV (Dpo4), a prototype Y-family DNA polymerase, contains a unique little finger domain besides a catalytic core. Here, we report the chemical shift assignments for the backbone nitrogens, α and β carbons, and amide protons of the little finger domain of Dpo4. This work and our published backbone assignment for the catalytic core provide the basis for investigating the conformational dynamics of Dpo4 during catalysis using solution NMR spectroscopy.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Archaeal Proteins / chemistry*
  • Carbon Isotopes / chemistry
  • DNA Polymerase beta / chemistry*
  • Molecular Sequence Data
  • Nitrogen Isotopes / chemistry
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sulfolobus solfataricus / enzymology*


  • Archaeal Proteins
  • Carbon Isotopes
  • Nitrogen Isotopes
  • DNA Polymerase beta