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Originally published In Press as doi:10.1074/jbc.M108618200 on January 18, 2002

J. Biol. Chem., Vol. 277, Issue 13, 11135-11142, March 29, 2002
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Human MutY Homolog, a DNA Glycosylase Involved in Base Excision Repair, Physically and Functionally Interacts with Mismatch Repair Proteins Human MutS Homolog 2/Human MutS Homolog 6*

Yesong GuDagger , Antony ParkerDagger , Teresa M. Wilson§, Haibo BaiDagger , Dau-Yin ChangDagger , and A-Lien LuDagger

From the Departments of Dagger  Biochemistry and Molecular Biology and § Radiation Oncology, University of Maryland, Baltimore, Maryland 21201

Adenines mismatched with guanines or 7,8-dihydro-8-oxo-deoxyguanines that arise through DNA replication errors can be repaired by either base excision repair or mismatch repair. The human MutY homolog (hMYH), a DNA glycosylase, removes adenines from these mismatches. Human MutS homologs, hMSH2/hMSH6 (hMutSalpha ), bind to the mismatches and initiate the repair on the daughter DNA strands. Human MYH is physically associated with hMSH2/hMSH6 via the hMSH6 subunit. The interaction of hMutSalpha and hMYH is not observed in several mismatch repair-defective cell lines. The hMutSalpha binding site is mapped to amino acid residues 232-254 of hMYH, a region conserved in the MutY family. Moreover, the binding and glycosylase activities of hMYH with an A/7,8-dihydro-8-oxo-deoxyguanine mismatch are enhanced by hMutSalpha . These results suggest that protein-protein interactions may be a means by which hMYH repair and mismatch repair cooperate in reducing replicative errors caused by oxidized bases.

* This work was supported by National Institutes of Health (NIH) Grants GM35132 and CA/ES78391 (to A-L. L.).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, University of Maryland, 108 N. Greene St., Baltimore, MD 21201. Tel.: 410-706-4356; Fax: 410-706-1787; E-mail: aluchang@umaryland.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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