Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii

FEBS Lett. 2011 Feb 4;585(3):452-8. doi: 10.1016/j.febslet.2010.12.040. Epub 2010 Dec 28.

Abstract

Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. The N-terminal (1-300) domain structure of the large subunit was determined by X-ray crystallography, although ∼50 N-terminal residues were disordered. The determined structure consists of nine alpha helices and three beta strands. We also identified the DNA-binding ability of the domain by SPR measurement. The N-terminal (1-100) region plays crucial roles in the folding of the large subunit dimer by connecting the ∼50 N-terminal residues with their own catalytic region (792-1163).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Catalytic Domain
  • Crystallography, X-Ray
  • DNA / metabolism
  • DNA, Single-Stranded / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • DNA-Directed DNA Polymerase / chemistry*
  • DNA-Directed DNA Polymerase / genetics
  • DNA-Directed DNA Polymerase / metabolism
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Interaction Domains and Motifs*
  • Protein Multimerization
  • Protein Refolding
  • Protein Stability
  • Protein Subunits / chemistry*
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Pyrococcus horikoshii / enzymology*
  • Selenomethionine / chemistry
  • Selenomethionine / metabolism
  • Surface Plasmon Resonance

Substances

  • Archaeal Proteins
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Protein Subunits
  • DNA
  • Selenomethionine
  • DNA-Directed DNA Polymerase
  • PolD DNA Polymerase, Pyrococcus horikoshii

Associated data

  • PDB/3O59