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A more recent version of this article appeared on February 16, 2001
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Papers In Press, published online ahead of print November 22, 2000
J. Biol. Chem, 10.1074/jbc.M008463200
Submitted on September 15, 2000
Revised on November 13, 2000
Accepted on November 21, 2000

Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long-patch DNA base excision repair

Antony Parker, Yesong Gu, William Mahoney, Suk-Hee Lee, Keshav K Singh, and A-Lien Lu

Biochemistry and Molecular Biology, University of Maryland, Baltimore, MD 21201

Corresponding Author: aluchang{at}umaryland.edu

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-oxo-deoxyguanines. 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 b and d were not detected. 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 exclusively 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.


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