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Hogrel, Gaelle; Lu, Yang; Alexandre, Nicolas; Bossé, Audrey; Dulermo, Remi; Ishino, Sonoko; Ishino, Yoshizumi; Flament, Didier. |
Among the three domains of life, the process of homologous recombination (HR) plays a central role in the repair of double-strand DNA breaks and the restart of stalled replication forks. Curiously, main protein actors involved in the HR process appear to be essential for hyperthermophilic Archaea raising interesting questions about the role of HR in replication and repair strategies of those Archaea living in extreme conditions. One key actor of this process is the recombinase RadA, which allows the homologous strand search and provides a DNA substrate required for following DNA synthesis and restoring genetic information. DNA polymerase operation after the strand exchange step is unclear in Archaea. Working with Pyrococcus abyssi proteins, here we show... |
Tipo: Text |
Palavras-chave: Homologous recombination; Archaea; DNA polymerase; Recombinase; DNA repair. |
Ano: 2020 |
URL: https://archimer.ifremer.fr/doc/00641/75274/75539.pdf |
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Richardson, Tomas T.; Gilroy, Louise; Ishino, Yoshizumi; Connolly, Bernard A.; Henneke, Ghislaine. |
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... |
Tipo: Text |
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Ano: 2013 |
URL: http://archimer.ifremer.fr/doc/00138/24975/23070.pdf |
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