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- W2891374857 abstract "The proper pausing of replication forks at barriers on chromosomes is important for genome integrity. However, the detailed mechanism underlying this process has not been well elucidated. Here, we successfully reconstituted fork-pausing reactions from purified yeast proteins on templates that had binding sites for the LacI, LexA, and/or Fob1 proteins; the forks paused specifically at the protein-bound sites. Moreover, although the replicative helicase Cdc45–Mcm2–7–GINS (CMG) complex alone unwound the protein-bound templates, the unwinding of the LacI-bound site was impeded by the presence of a main leading strand DNA polymerase: polymerase ε (Polε). This suggests that Polε modulates CMG to pause at these sites." @default.
- W2891374857 created "2018-09-27" @default.
- W2891374857 creator A5011799677 @default.
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- W2891374857 creator A5047498931 @default.
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- W2891374857 date "2018-09-19" @default.
- W2891374857 modified "2023-10-16" @default.
- W2891374857 title "DNA polymerase ε-dependent modulation of the pausing property of the CMG helicase at the barrier" @default.
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- W2891374857 doi "https://doi.org/10.1101/gad.317073.118" @default.
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