Psy2 and Pph3 form a phosphatase complex required for Rad53 dephosphorylation and replication fork restart during recovery from DNA damage
B.M. O’Neill, S.J. Szyjka, E.T. Lis, A.O. Bailey, J.R. Yates III, O.M. Aparicio, F.E. Romesberg, Proc. Natl. Acad. Sci. USA (2007) 104:9290-9295.
We present genetic and biochemical evidence that the type 2A-like protein phosphatase Pph3 forms a complex with Psy2 (Pph3–Psy2) that binds and dephosphorylates activated Rad53 during treatment with, and recovery from, methylmethane sulfonate-mediated DNA damage. Our findings suggest that Rad53 regulates replication fork restart and initiation of late firing origins independently and that regulation of these processes is mediated by specific Rad53 phosphatases order of magnitude relative to mispairing.