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Originally published In Press as doi:10.1074/jbc.M008463200 on November 22, 2000

J. Biol. Chem., Vol. 276, Issue 8, 5547-5555, February 23, 2001
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Human Homolog of the MutY Repair Protein (hMYH) Physically Interacts with Proteins Involved in Long Patch DNA Base Excision Repair*

Antony ParkerDagger , Yesong GuDagger , William MahoneyDagger §, Suk-Hee Lee, Keshav K. Singh||, and A-Lien LuDagger **

From the Dagger  Department of Biochemistry and Molecular Biology and § Combined Ph.D. Program in Biochemistry, the University of Maryland, Baltimore, Maryland 21201, the  Department of Biochemistry and Molecular Biology, Indiana University Cancer Center and Walther Oncology Center, Indiana University School of Medicine, Indianapolis, Indiana 46202, and the || Radiation Research Program, The Johns Hopkins Oncology Center, Baltimore, Maryland 21231

The human MutY homolog (hMYH) is a DNA glycosylase involved in the removal of adenines or 2-hydroxyadenines misincorporated with template guanines or 7,8-dihydro-8-oxodeoxyguanines. hMYH is associated in vivo with apurinic/apyrimidinic endonuclease (APE1), proliferating cell nuclear antigen (PCNA), and replication protein A (RPA) in HeLa nuclear extracts as shown by immunoprecipitation and Western blotting. However, binding of hMYH to DNA polymerases beta  and delta  was not detected. By using constructs containing different portions of hMYH fused to glutathione S-transferase, we have demonstrated that the APE1-binding site is at a region around amino acid residue 300, that the PCNA binding activity is located at the C terminus, and that RPA binds to the N terminus of hMYH. A peptide consisting of residues 505-527 of hMYH that contains a conserved PCNA-binding motif binds PCNA, and subsequent amino acid substitution identified Phe-518 and Phe-519 as essential residues required for PCNA binding. RPA binds to a peptide that consists of residues 6-32 of hMYH and contains a conserved RPA-binding motif. The PCNA- and RPA-binding sites of hMYH are further confirmed by peptide and antibody titration. These results suggest that hMYH repair is a long patch base excision repair pathway.

* This work was supported by National Institutes of Health Grants GM35132, CA/ES78391 (to A-L. L.), GM52358 (to S.-H. L.), and Grant ES09714 and American Heart Association Grant 9930223N (to K. K. S).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.

** To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, the University of Maryland, 108 N. Greene St., Baltimore, MD 21201. Tel.: 410-706-4356; Fax: 410-706-1787; E-mail: aluchang@umaryland.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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