Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases

FEBS Lett. 2010 Aug 4;584(15):3370-5. doi: 10.1016/j.febslet.2010.06.026. Epub 2010 Jun 23.


Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. We analyzed the structure of the N-terminal 200 amino-acid regulatory region of the small subunit by NMR and revealed that the N-terminal approximately 70 amino-acid region is folded. The structure consists of a four-alpha-helix bundle including a short parallel beta-sheet, which is similar to the N-terminal regions of the B subunits of human DNA polymerases alpha and epsilon, establishing evolutionary relationships among these archaeal and eukaryotic polymerases. We observed monomer-dimer equilibrium of this domain, which may be related to holoenzyme architecture and/or functional regulation.

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Amino Acid Sequence
  • DNA-Directed DNA Polymerase / chemistry*
  • Eukaryota / enzymology*
  • Evolution, Molecular*
  • Humans
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Subunits / chemistry*
  • Pyrococcus horikoshii / enzymology*
  • Solutions
  • Ultracentrifugation


  • Protein Subunits
  • Solutions
  • DNA-Directed DNA Polymerase
  • Adenosine Triphosphatases