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

Author:

Bauche Cécile1,Laval Jacques1

Affiliation:

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

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference45 articles.

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5. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein;Boiteux S.;EMBO J.,1987

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