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J Biol Chem, Vol. 275, Issue 12, 8448-8455, March 24, 2000

The C-terminal Domain of MutY Glycosylase Determines the 7,8-Dihydro-8-oxo-guanine Specificity and Is Crucial for Mutation Avoidance*

Xianghong Li, Patrick M. Wright, and A-Lien LuDagger

From the Department of Biochemistry and Molecular Biology, University of Maryland at Baltimore, Baltimore, Maryland 21201

Escherichia coli MutY is an adenine DNA glycosylase active on DNA substrates containing A/G, A/8-oxoG, or A/C mismatches and also has a weak guanine glycosylase activity on G/8-oxoG-containing DNA. The N-terminal domain of MutY, residues 1-226, has been shown to retain catalytic activity. Substrate binding, glycosylase, and Schiff base intermediate formation activities of the truncated and intact MutY were compared. MutY has high binding affinity with 8-oxoG when mispaired with A, G, T, C, or inosine. The truncated protein has more than 18-fold lower affinities for binding various 8-oxoG-containing mismatches when compared with intact MutY. MutY catalytic activity toward A/8-oxoG-containing DNA is much faster than that on A/G-containing DNA whereas deletion of the C-terminal domain reduces its catalytic preference for A/8-oxoG-DNA over A/G-DNA. MutY exerts more inhibition on the catalytic activity of MutM (Fpg) protein than does truncated MutY. The tight binding of MutY with GO mispaired with T, G, and apurinic/apyrimidinic sites may be involved in the regulation of MutM activity. An E. coli mutY strain that produces an N-terminal 249-residue truncated MutY confers a mutator phenotype. These findings strongly suggest that the C-terminal domain of MutY determines the 8-oxoG specificity and is crucial for mutation avoidance by oxidative damage.

* This work was supported by United States Public Health Service Grant GM 35132 from the NIGMS, National Institute of Health.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.

Dagger To whom correspondence should be addressed. Tel.: 410-706-4356; Fax: 410-706-1787; E-mail: aluchang@umaryland.edu.

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