title: Uracil-DNA glycosylase in the extreme thermophile Archaeoglobus fulgidus.
abstract: 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 degrees 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.
authors.affiliation: Departments of Radiology and Radiation Oncology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
authors.forename: M
authors.initials: M
authors.lastname: Sandigursky
authors.forename: W A
authors.initials: WA
authors.lastname: Franklin
mesh_terms: D000595:Amino Acid Sequence; D019611:Archaeoglobus fulgidus / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism; D045647:DNA Glycosylases; D017931:DNA Primers; D004260:DNA Repair / Q000235:genetics; D004795:Enzyme Stability; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D051981:Uracil-DNA Glycosidase
chemical_list: D017931:DNA Primers; D004247:DNA; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases; D051981:Uracil-DNA Glycosidase