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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Genetics

Background:

  • The DNA damage checkpoint is regulated by phosphatidylinositol 3-kinase-related kinases (PIKKs), including ATM and ATR.
  • ATR forms a complex with ATRIP, which in budding yeast are Mec1 and Ddc2, respectively.
  • ATRIP/Ddc2 recruits ATR/Mec1 to DNA damage sites and interacts with replication protein A-bound single-stranded DNA (RPA-ssDNA).

Purpose of the Study:

  • To elucidate the mechanism of Ddc2-dependent Mec1 activation.
  • To characterize the role of the ddc2-S4 mutation in DNA damage response.
  • To investigate the contribution of Ddc2 to Mec1 activation independently of canonical activators.

Main Methods:

  • Characterization of the ddc2-S4 mutation in vivo.
  • In vitro kinase assays using purified Mec1-Ddc2 complex, RPA, and single-stranded DNA (ssDNA).
  • Analysis of checkpoint mediator phosphorylation (Rad9 and Mrc1) in wild-type and mutant cells.

Main Results:

  • Ddc2 promotes Mec1 activation independently of Ddc1/Dpb11/Dna2 in vivo and via ssDNA recognition in vitro.
  • The ddc2-S4 mutation impairs damage-induced phosphorylation of Rad9 and Mrc1, with a more severe defect in S-phase checkpoint signaling.
  • ssDNA stimulates Mec1-Ddc2 kinase activity, and RPA enhances this stimulation; the ddc2-S4 mutant shows reduced stimulation by RPA-ssDNA.

Conclusions:

  • Ddc2 plays a dual role in DNA damage response: recruiting Mec1 and directly stimulating its kinase activity.
  • Ddc2-mediated Mec1 activation occurs at RPA-ssDNA tracts and is crucial for efficient checkpoint signaling, particularly during S-phase.
  • The findings support a model where Ddc2 acts as a critical activator of Mec1 kinase at DNA damage sites.