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Reference - PMID:10559981 - A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins.

Reference summary

PubMed ID
PMID:10559981
Title
A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins.
Authors
Edwards RJ, Bentley NJ, Carr AM
Citation
Nat Cell Biol 1999 Nov;1(7):393-8
Publication year
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.

Annotation

GO cellular component

GO:0070310 - ATR-ATRIP complex

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GO molecular function

GO:0005515 - protein binding

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Modification

MOD:00696 - phosphorylated residue

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Multi-locus phenotype

FYPO:0002096 - increased protein phosphorylation during cellular response to hydroxyurea

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FYPO:0003131 - normal protein phosphorylation during cellular response to ionizing radiation

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Single locus phenotype

FYPO:0004550 - abolished protein phosphorylation during cellular response to hydroxyurea

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FYPO:0002471 - abolished protein phosphorylation during cellular response to ionizing radiation

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FYPO:0002096 - increased protein phosphorylation during cellular response to hydroxyurea

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FYPO:0001038 - increased protein phosphorylation during vegetative growth

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FYPO:0001927 - normal cell cycle regulation during cellular response to ionizing radiation

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FYPO:0003131 - normal protein phosphorylation during cellular response to ionizing radiation

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FYPO:0000703 - normal protein-protein interaction

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FYPO:0000088 - sensitive to hydroxyurea

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FYPO:0000267 - sensitive to ionizing radiation during vegetative growth

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