Data/hora: 01/06/2024 06:15:13

Provedor de dados: | 5
País: | France
Título: | Novel inhibition of archaeal family-D DNA polymerase by uracil
Autores: | Richardson, Tomas T.; Gilroy, Louise; Ishino, Yoshizumi; Connolly, Bernard A.; Henneke, Ghislaine.
Data: | 2013-04
Ano: | 2013
Resumo: | 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 similar to 5 and 3'-5' proof-reading exonuclease activity is stimulated by a factor of similar to 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.
Tipo: | Text
Idioma: | Inglês

Identificador:

http://archimer.ifremer.fr/doc/00138/24975/23070.pdf

DOI:10.1093/nar/gkt083

Editor: | Oxford Univ Press
Relação: | http://archimer.ifremer.fr/doc/00138/24975/
Formato: | application/pdf
Fonte: | Nucleic Acids Research (0305-1048) (Oxford Univ Press), 2013-04 , Vol. 41 , N. 7 , P. 4207-4218
Fonte: | The Author(s) 2013. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.