title: Involvement of a cryptic ATPase activity of UvrB and its proteolysis product, UvrB* in DNA repair.
abstract: The incision of damaged DNA by the Escherichia coli UvrABC endonuclease requires ATP hydrolysis. Although the deduced sequence of the UvrB protein suggests a putative ATP binding site, no nucleoside triphosphatase activity is demonstrable with the purified UvrB protein. The UvrB protein is specifically proteolyzed in E. coli cell extracts to yield a 70 kD fragment, referred to as UvrB*, which has been purified and is shown to possess a single-strand DNA dependent ATPase activity. Substrate specificity and kinetic analyses of UvrB* catalyzed nucleotide hydrolysis indicate that the stimulation in DNA dependent ATPase activity following formation of the UvrAB complex results from the activation of the normally sequestered UvrB associated ATPase. Using nucleotide analogues, it can be shown that this activity is essential to the DNA incision reaction carried out by the UvrABC complex.
authors.affiliation: Department of Biochemistry, Johns Hopkins University, School of Hygiene and Public Health, Baltimore, MD 21205.
authors.forename: P R
authors.initials: PR
authors.lastname: Caron
authors.forename: L
authors.initials: L
authors.lastname: Grossman
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D004265:DNA Helicases; D004260:DNA Repair; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D005796:Genes; D005798:Genes, Bacterial; D007700:Kinetics; D010957:Plasmids
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C058093:UvrB protein, E coli; D000251:Adenosine Triphosphatases; D004265:DNA Helicases