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

Author:  ["Rhian J. Edwards","Nicola J. Bentley","Antony M. Carr"]

Publication:  Nature Cell Biology

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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.

Cite this article

Edwards, R., Bentley, N. & Carr, A. A Rad3–Rad26 complex responds to DNA damage independently of other checkpoint proteins. Nat Cell Biol 1, 393–398 (1999). https://doi.org/10.1038/15623

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