Rad9 BRCT domain interaction with phosphorylated H2AX regulates the G1 checkpoint in budding yeast.

@article{Hammet2007Rad9BD,
  title={Rad9 BRCT domain interaction with phosphorylated H2AX regulates the G1 checkpoint in budding yeast.},
  author={Andrew Hammet and Christine P Magill and J{\"o}rg Heierhorst and Stephen P. Jackson},
  journal={EMBO reports},
  year={2007},
  volume={8 9},
  pages={851-7}
}
Phosphorylation of histone H2A or H2AX is an early and sensitive marker of DNA damage in eukaryotic cells, although mutation of the conserved damage-dependent phosphorylation site is well tolerated. Here, we show that H2A phosphorylation is required for cell-cycle arrest in response to DNA damage at the G1/S transition in budding yeast. Furthermore, we show that the tandem BRCT domain of Rad9 interacts directly with phosphorylated H2A in vitro and that a rad9 point mutation that abolishes this… CONTINUE READING