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Originally published In Press as doi:10.1074/jbc.M005782200 on July 6, 2000

J. Biol. Chem., Vol. 275, Issue 38, 29767-29771, September 22, 2000
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The Human Checkpoint Protein hRad17 Interacts with the PCNA-like Proteins hRad1, hHus1, and hRad9*

Matthew RauenDagger §, Matthew A. BurtelowDagger §, Vanessa M. DufaultDagger , and Larry M. KarnitzDagger ||**Dagger Dagger

From the Divisions of Dagger  Developmental Oncology Research and || Radiation Oncology and the Departments of ** Immunology and  Molecular Pharmacology, Mayo Clinic, Rochester, Minnesota 55902

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 protein 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, and 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.

* This work was supported by the Mayo Foundation and a Fraternal Order of Eagles grant.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work.

Dagger Dagger To whom correspondence should be addressed: Mayo Foundation, Oncology Research, Guggenheim 13, Rochester, MN 55905. Tel.: 507-284-3124; Fax: 507-284-3906; E-mail: karnitz.larry@mayo.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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