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Novel inhibition of archaeal family-D DNA polymerase by uracil.

Abstract : Archaeal family-D DNA polymerase is inhibited by the presence of uracil in DNA template strands. When the enzyme encounters uracil, following three parameters change: DNA binding increases roughly 2-fold, the rate of polymerization slows by a factor of ≈ 5 and 3'-5' proof-reading exonuclease activity is stimulated by a factor of ≈ 2. Together these changes result in a significant decrease in polymerization activity and a reduction in net DNA synthesis. Pol D appears to interact with template strand uracil irrespective of its distance ahead of the replication fork. Polymerization does not stop at a defined location relative to uracil, rather a general decrease in DNA synthesis is observed. 'Trans' inhibition, the slowing of Pol D by uracil on a DNA strand not being replicated is also observed. It is proposed that Pol D is able to interact with uracil by looping out the single-stranded template, allowing simultaneous contact of both the base and the primer-template junction to give a polymerase-DNA complex with diminished extension ability.
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Tomas T Richardson, Louise Gilroy, Yoshizumi Ishino, Bernard A Connolly, Ghislaine Henneke. Novel inhibition of archaeal family-D DNA polymerase by uracil.. Nucleic Acids Research, 2013, 41 (7), pp.4207-18. ⟨10.1093/nar/gkt083⟩. ⟨hal-00834323⟩



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