doi: 10.1038/15623.
A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins
Affiliations
- PMID: 10559981
- DOI: 10.1038/15623
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A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins
Nat Cell Biol.
1999 Nov.
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.
Comment in
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Sensor-less checkpoint activation?Nat Cell Biol. 1999 Nov;1(7):E177-9. doi: 10.1038/15614. Nat Cell Biol. 1999. PMID: 10559997 No abstract available.
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