Characterization and PCR Application of Family B DNA Polymerases from .

DNA polymerases from the hyperthermophilic Archaea have attracted considerable attention as PCR enzymes due to their high thermal stability and proofreading 3' → 5' exonuclease activity. This study is the first to report data concerning the purification and biochemical characteristics of the Tst DNA polymerase from . Both the wild type Tst(wt) DNA polymerase and its chimeric form containing the P36H substitution-which reduces the enzyme's affinity for the U-containing template and dUTP-and the DNA-binding domain Sso7d from were obtained and analyzed.