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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
Uracil-DNA Glycosylase in the Extreme Thermophile
Archaeoglobus fulgidus*
Margarita
Sandigursky and
William A.
Franklin
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.
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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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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