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A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins
R J Edwards1, N J Bentley, A M Carr
1MRC Cell Mutation Unit, Sussex University, Falmer BN1 9RR, UK.
Nature Cell Biology
|November 24, 1999
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.