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Journal articles
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.
Cited literature [39 references]
https://hal.univ-brest.fr/hal-00834323
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Submitted on : Friday, June 14, 2013 - 4:44:53 PM
Last modification on : Monday, October 11, 2021 - 2:22:07 PM
Long-term archiving on: : Sunday, September 15, 2013 - 4:12:09 AM
Contributor : Adminhal Univbrestbu Connect in order to contact the contributor
Submitted on : Friday, June 14, 2013 - 4:44:53 PM
Last modification on : Monday, October 11, 2021 - 2:22:07 PM
Long-term archiving on: : Sunday, September 15, 2013 - 4:12:09 AM
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Nucl._Acids_Res.-2013-Richards...
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