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An Archaeal B‐family DNA Polymerase Exists as a Trimer with Additional Annealing and Terminal Transferase Activities

The primary DNA replication polymerase from Sulfolobus solfataricus (Dpo1) has been shown previously to provide the necessary polymerization speed and exonuclease activity to replicate the genome accurately. We find that this polymerase is able to cooperatively associate with itself to promote trimer formation. We have determined that these are specific polymerase‐polymerase interactions around DNA. This trimeric complex has unique thermodynamic binding parameters due to changes in the coupled equilibria of the various polymerase/DNA complexes. Interestingly, this unusual trimeric DNA polymerase complex has an increased kinetic rate of synthesis, extremely long processivity, increased DNA annealing activity and robust terminal transferase activity. Although the monomeric polymerase is fully functional, the trimeric polymerase affords additional activities that result in efficient activities at high temperatures in DNA replication or repair. Taken together, these results suggest the presence of a dynamic trimeric DNA polymerase complex that is able to process DNA substrates more efficiently than the monomeric form. This trimeric polymerase complex is implicated in the maintenance of the archaeal genome through coupled activities in DNA replication and repair.