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J. Biol. Chem., Vol. 277, Issue 46, 43809-43812, November 15, 2002
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From the Departments of Rad17, Rad1, Hus1, and Rad9 are key participants
in checkpoint signaling pathways that block cell cycle progression in
response to genotoxins. Biochemical and molecular modeling data predict that Rad9, Hus1, and Rad1 form a heterotrimeric complex, dubbed 9-1-1, which is loaded onto chromatin by a complex of Rad17 and the four small
replication factor C (RFC) subunits (Rad17-RFC) in response to DNA
damage. It is unclear what checkpoint proteins or checkpoint signaling
events regulate the association of the 9-1-1 complex with DNA. Here we
show that genotoxin-induced chromatin binding of 9-1-1 does not require
the Rad9-inducible phosphorylation site (Ser-272). Although we found
that Rad9 undergoes an additional phosphatidylinositol 3-kinase-related
kinase (PIKK)-dependent posttranslational modification, we
also show that genotoxin-triggered 9-1-1 chromatin binding does not
depend on the catalytic activity of the PIKKs ataxia
telangiectasia-mutated (ATM), ataxia telangiectasia and Rad3-related
(ATR), or DNA-PK. Additionally, 9-1-1 chromatin binding does not
require DNA replication, suggesting that the complex can be loaded onto
DNA in response to DNA structures other than stalled DNA replication
forks. Collectively, these studies demonstrate that 9-1-1 chromatin
binding is a proximal event in the checkpoint signaling cascade.
Biochemistry and Molecular
Biology and ¶ Molecular Pharmacology and Experimental
Therapeutics, Mayo Graduate School, and the Divisions of
§ Developmental Oncology Research and Radiation
Oncology, Mayo Clinic and Foundation, Rochester, Minnesota 55905
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