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Originally published In Press as doi:10.1074/jbc.M001071200 on April 20, 2000

J. Biol. Chem., Vol. 275, Issue 26, 20077-20083, June 30, 2000
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A Novel 3-Methyladenine DNA Glycosylase from Helicobacter pylori Defines a New Class within the Endonuclease III Family of Base Excision Repair Glycosylases*

Eyleen J. O'RourkeDagger §, Catherine Chevalier||**, Serge BoiteuxDagger , Agnès Labigne||, Luis Ielpi§Dagger Dagger , and J. Pablo RadicellaDagger §§

From the Dagger   Département de Radiobiologie et Radiopathologie, Commissariat à l'Energie Atomique, UMR217 CEA/CNRS, BP6, 92265 Fontenay-aux-Roses, France, the § Instituto de Investigaciones Bioquímicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales-UBA and the Consejo Nacional de Investigaciones Cientifícas y Técnicas, 1405 Buenos Aires, Argentina, and the || Unité de Pathogénie Bactérienne des Muqueuses, Institut Pasteur, 75724 Paris, France

The cloning, purification, and characterization of MagIII, a 3-methyladenine DNA glycosylase from Helicobacter pylori, is presented in this paper. Sequence analysis of the genome of this pathogen failed to identify open reading frames potentially coding for proteins with a 3-methyladenine DNA glycosylase activity. The putative product of the HP602 open reading frame, reported as an endonuclease III, shares extensive amino acid sequence homology with some bacterial members of this family and has the canonic active site helix-hairpin-helix-GPD motif. Surprisingly, this predicted H. pylori endonuclease III encodes a 25,220-Da protein able to release 3-methyladenine, but not oxidized bases, from modified DNA. MagIII has no abasic site lyase activity and displays the substrate specificity of the 3-methyladenine-DNA glycosylase type I of Escherichia coli (Tag) because it is not able to recognize 7-methylguanine or hypoxanthine as substrates. The expression of the magIII open reading frame in null 3-methyladenine glycosylase E. coli (tag alkA) restores to this mutant partial resistance to alkylating agents. MagIII-deficient H. pylori cells show an alkylation-sensitive phenotype. H. pylori wild type cells exposed to alkylating agents present an adaptive response by inducing the expression of magIII. MagIII is thus a novel bacterial member of the endonuclease III family, which displays biochemical properties not described for any of the members of this group until now.

* This work was supported in France by the Commissariat à l'Energie Atomique, CNRS, and Electricite de France and in Argentina by a fellowship from Fundación Antorchas (to E. J. O.), grants from the Laboratorios Bagó SA, and Argentine Federal Government Grant ANPCT PICT97-00419) (to L. I.).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.

Recipient of a doctoral fellowship from the University of Buenos Aires (Fondo Para el Mejoramiento de la Calidad Universitaria).

** Member of Unité INSERM U389.

Dagger Dagger Research Career Investigator of the Consejo Nacional de Investigaciones Cientifícas y Técnicas.

§§ To whom correspondence should be addressed. Tel.: 33-1-46-54-88-57; Fax: 33-1-46-54-88-59; E-mail: jpradicella@cea.fr.

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