Backbone assignment of the binary complex of the full length Sulfolobus solfataricus DNA polymerase IV and DNA

Biomol NMR Assign. 2017 Apr;11(1):39-43. doi: 10.1007/s12104-016-9717-4. Epub 2016 Oct 13.

Abstract

Sulfolobus solfataricus DNA polymerase IV (Dpo4), a model Y-family DNA polymerase, bypasses a wide range of DNA lesions in vitro and in vivo. In this paper, we report the backbone chemical shift assignments of the full length Dpo4 in its binary complex with a 14/14-mer DNA substrate. Upon DNA binding, several β-stranded regions in the isolated catalytic core and little finger/linker fragments of Dpo4 become more structured. This work serves as a foundation for our ongoing investigation of conformational dynamics of Dpo4 and future determination of the first solution structures of a DNA polymerase and its binary and ternary complexes.

Keywords: Backbone resonance assignments; DNA lesion bypass; Heteronuclear NMR; Y-family DNA polymerase.

MeSH terms

  • Amino Acid Sequence
  • DNA / metabolism*
  • DNA Polymerase beta / chemistry*
  • DNA Polymerase beta / metabolism*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Sulfolobus solfataricus / enzymology*

Substances

  • DNA
  • DNA Polymerase beta