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Originally published In Press as doi:10.1074/jbc.M001995200 on April 20, 2000

J. Biol. Chem., Vol. 275, Issue 25, 19146-19149, June 23, 2000
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Uracil-DNA Glycosylase in the Extreme Thermophile Archaeoglobus fulgidus*

Margarita Sandigursky and William A. FranklinDagger

From the Departments of Radiology and Radiation Oncology, Albert Einstein College of Medicine, Bronx, New York 10461

Uracil-DNA glycosylase (UDG) is an essential enzyme for maintaining genomic integrity. Here we describe a UDG from the extreme thermophile Archaeoglobus fulgidus. The enzyme is a member of a new class of enzymes found in prokaryotes that is distinct from the UDG enzyme found in Escherichia coli, eukaryotes, and DNA-containing viruses. The A. fulgidus UDG is extremely thermostable, maintaining full activity after heating for 1.5 h at 95 °C. The protein is capable of removing uracil from double-stranded DNA containing either a U/A or U/G base pair as well as from single-stranded DNA. This enzyme is product-inhibited by both uracil and apurinic/apyrimidinic sites. The A. fulgidus UDG has a high degree of similarity at the primary amino acid sequence level to the enzyme found in Thermotoga maritima, a thermophilic eubacteria, and suggests a conserved mechanism of UDG-initiated base excision repair in archaea and thermophilic eubacteria.

* This work was supported by NCI Grant CA52025 from the National Institutes 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: Depts. of Radiology and Radiation Oncology, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Tel.: 718-430-2239; Fax: 718-430- 4039; E-mail: frankin@aecom.yu.edu.

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