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Papers In Press, published online ahead of print April 20, 2000
Department of Radiology, Albert Einstein College of Medicine, Bronx, NY 10461
Corresponding Author: franklin{at}aecom.yu.edu
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 E. coli, eukaryotes, and DNA-containing viruses. The A. fulgidus UDG is extremely thermostable, maintaining full activity after heating for 1.5 hours at 95oC. 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 (AP) 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.
J. Biol. Chem, 10.1074/jbc.M001995200
Submitted on March 9, 2000
Revised on April 14, 2000
Accepted on April 19, 2000
Uracil-DNA Glycosylase in the Extreme Thermophile Archaeoglobus fulgidus
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