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Papers In Press, published online ahead of print July 6, 2000
Oncology, Mayo Clinic, Rochester, MN 55905
Corresponding Author: karnitz.larry{at}mayo.edu
DNA damage activates cell cycle checkpoints that prevent progression through the cell cycle. In yeast, the DNA damage checkpoint response is regulated by a series of genes that have mammalian homologs, including Rad1, Rad9, Hus1, and Rad17. On the basis of sequence homology, yeast and human Rad1, Rad9, and Hus1 homologs are predicted to structurally resemble the sliding clamp PCNA. Likewise, Rad17 homologs have extensive homology with replication factor C (RFC) subunits (p36, p37, p38, p40, p140), which form a clamp loader for PCNA. These observations predict that Rad1, Hus1, and Rad9 might interact with Rad17 as a clamp-clamp loader pair during the DNA damage response. In this report we demonstrate that endogenous human Rad17 (hRad17) interacts with the PCNA-related checkpoint proteins hRad1, hRad9, and hHus1. Mutational analysis of hRad1 and hRad17 demonstrates that this interaction has properties similar to the interaction between RFC and PCNA, a well-characterized clamp-clamp loader pair. Moreover, we show that DNA damage affects the association of hRad17 with the clamp-like checkpoint proteins. Collectively, these data provide the first experimental evidence that hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9 in manner similar to the interaction between RFC and PCNA.
J. Biol. Chem, 10.1074/jbc.M005782200
Submitted on June 30, 2000
Accepted on July 6, 2000
The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9
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