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Nucleic Acids Research, 1994, Vol. 22, No. 18 3760-3764
© 1994

ENZYMOLOGY

Formamidopyrimidine DNA glycosylase in the yeast Saccharomyces cerevisiae

Regina de Oliveira, Patricia Auffret van der Kemp, Dominique Thomas1, Albert Geiger2, Peter Nehls2 and Serge Boiteux*

Groupe ‘Réparation des lésions radio et chimioinduites’, URA147 CNRS, Institut Gustave Roussy 94800 Villejuif 1Centre de Génétique Moléculaire du CNRS 91178 Gif-sur-Yvette, France 2Institute of Cell Biology, West-German Cancer Center Essen Virchowstrasse 173, D-45147 Essen, Germany

*To whom correspondence should be addressed

Received May 13, 1994. Revised July 28, 1994. Accepted July 28, 1994.

A DNA glycosylase that excises 2,6-diamino-4-hydroxy- 5N-methylformamidopyrimidine (Fapy) from double stranded DNA has been purified 28,570-fold from the yeast Saccharomyces cerevisiae. Gel filtration chromatography shows that yeast Fapy DNA glycosylase has a molecular weight of about 40 kDa. The Fapy DNA glycosylase is active in the presence of EDTA, but is completely inhibited by 0.2 M KCI. Yeast Fapy DNA glycosylase does not excise N7-methylguanine, N3- methyladenine or uracil. A repair enzyme for 7,8-dihydro- 8-oxoguanine (8-OxoG) co-purifies with the Fapy DNA glycosylase. This repair activity causes strand cleavage at the site of 8-OxoG in DNA duplexes. The highest rate of incision of the 8-OxoG-containing strand was observed for duplexes where 8-OxoG was opposite guanine. The mode of incision at 8-OxoG was not established yet. The results however suggest that the Fapy- and 8-OxoG-repair activities are associated with a single protein.


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