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Journal of Bacteriology, January 1999, p. 262-269, Vol. 181, No. 1
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Repair of Oxidized Bases in the Extremely Radiation-Resistant Bacterium Deinococcus radiodurans

Cécile Bauche and Jacques Laval*

Groupe "Réparation des Lésions Radio-et Chimio-Induites," UMR 1772 CNRS, Institut Gustave Roussy, 94805 Villejuif Cedex, France

Received 2 July 1998/Accepted 9 October 1998

Deinococcus radiodurans is able to resist and survive extreme DNA damage induced by ionizing radiation and many other DNA-damaging agents. It is believed that it possesses highly efficient DNA repair mechanisms. To characterize the repair pathway of oxidized purines in this bacteria, we have purified, from crude extracts, proteins that recognize these oxidized bases. We report here that D. radiodurans possesses two proteins excising the oxidized purines (formamidopyrimidine and 8-oxoguanine) by a DNA glycosylase-a purinic/apyrimidine lyase mechanism. Moreover, one of those proteins is endowed with a thymine glycol DNA glycosylase activity. One of these proteins could be the homolog of the Escherichia coli Fpg enzyme, which confirms the existence of a base excision repair system in this bacteria.

* Corresponding author. Mailing address: Groupe "Réparation des Lésions Radio-et Chimio-Induites," UMR 1772 CNRS, Institut Gustave Roussy, 94805 Villejuif Cedex, France. Phone: 33 1 42114824. Fax: 33 1 42114454. E-mail: jlaval{at}igr.fr.

Journal of Bacteriology, January 1999, p. 262-269, Vol. 181, No. 1
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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