A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins

Nat Cell Biol. 1999 Nov;1(7):393-8. doi: 10.1038/15623.

Abstract

The conserved PIK-related kinase Rad3 is required for all DNA-integrity-checkpoint responses in fission yeast. Here we report a stable association between Rad3 and Rad26 in soluble protein extracts. Rad26 shows Rad3-dependent phosphorylation after DNA damage. Unlike phosphorylation of Hus1, Crb2/Rhp9, Cds1 and Chk1, phosphorylation of Rad26 does not require other known checkpoint proteins. Rad26 phosphorylation is the first biochemical marker of Rad3 function, indicating that Rad3-related checkpoint kinases may have a direct role in DNA-damage recognition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism*
  • Blotting, Western
  • Cell Cycle Proteins / physiology*
  • DNA Damage*
  • DNA Helicases / genetics
  • DNA Helicases / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gamma Rays
  • Hydroxyurea / pharmacology
  • Macromolecular Substances
  • Models, Biological
  • Phosphorylation
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces / cytology*
  • Schizosaccharomyces / drug effects
  • Schizosaccharomyces / genetics
  • Schizosaccharomyces / radiation effects
  • Schizosaccharomyces pombe Proteins*
  • Ultraviolet Rays

Substances

  • Cell Cycle Proteins
  • Enzyme Inhibitors
  • Fungal Proteins
  • Macromolecular Substances
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • rad26 protein, S pombe
  • Adenosine Triphosphatases
  • Rad3 protein, S cerevisiae
  • DNA Helicases
  • Hydroxyurea