A heterodimeric DNA polymerase: evidence that members of Euryarchaeota possess a distinct DNA polymerase

Proc Natl Acad Sci U S A. 1998 Nov 24;95(24):14250-5. doi: 10.1073/pnas.95.24.14250.


We describe here a DNA polymerase family highly conserved in Euryarchaeota, a subdomain of Archaea. The DNA polymerase is composed of two proteins, DP1 and DP2. Sequence analysis showed that considerable similarity exists between DP1 and the second subunit of eukaryotic DNA polymerase delta, a protein essential for the propagation of Eukarya, and that DP2 has conserved motifs found in proteins with nucleotide-polymerizing activity. These results, together with our previous biochemical analyses of one of the members, DNA polymerase II (DP1 + DP2) from Pyrococcus furiosus, implicate the DNA polymerases of this family in the DNA replication process of Euryarchaeota. The discovery of this DNA-polymerase family, aside from providing an opportunity to enhance our knowledge of the evolution of DNA polymerases, is a significant step toward the complete understanding of DNA replication across the three domains of life.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Conserved Sequence
  • DNA Polymerase III / chemistry
  • DNA Polymerase III / genetics
  • DNA-Directed DNA Polymerase / chemistry
  • DNA-Directed DNA Polymerase / genetics*
  • Dimerization
  • Euryarchaeota / classification
  • Euryarchaeota / enzymology*
  • Euryarchaeota / genetics*
  • Evolution, Molecular*
  • Humans
  • Macromolecular Substances
  • Molecular Sequence Data
  • Multigene Family
  • Phylogeny*
  • Pyrococcus / enzymology
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • Macromolecular Substances
  • DNA Polymerase III
  • DNA-Directed DNA Polymerase