The structural basis of the kinetic mechanism of a gap-filling X-family DNA polymerase that binds Mg(2+)-dNTP before binding to DNA.

@article{Nakane2012TheSB,
  title={The structural basis of the kinetic mechanism of a gap-filling X-family DNA polymerase that binds Mg(2+)-dNTP before binding to DNA.},
  author={Shuhei Nakane and Hirohito Ishikawa and Noriko Nakagawa and Seiki Kuramitsu and Ryoji Masui},
  journal={Journal of molecular biology},
  year={2012},
  volume={417 3},
  pages={179-96}
}
DNA with single-nucleotide (1-nt) gaps can arise during various DNA processing events. These lesions are repaired by X-family DNA polymerases (PolXs) with high gap-filling activity. Some PolXs can bind productively to dNTPs in the absence of DNA and fill these 1-nt gaps. Although PolXs have a crucial role in efficient gap filling, currently, little is known of the kinetic and structural details of their productive dNTP binding. Here, we show that Thermus thermophilus HB8 PolX (ttPolX) had… CONTINUE READING