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Nat Cell Biol. 1999 Nov;1(7):393-8.

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

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1
MRC Cell Mutation Unit, Sussex University, Falmer BN1 9RR, UK.

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.

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PMID:
10559981
DOI:
10.1038/15623
[Indexed for MEDLINE]

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