title: Protein complexes formed during the incision reaction catalyzed by the Escherichia coli UvrABC endonuclease.
abstract: An examination has been made into the nature of the nucleoprotein complexes formed during the incision reaction catalyzed by the Escherichia coli UvrABC endonuclease when acting on a pyrimidine dimer-containing fd RF-I DNA species. The complexes of proteins and DNA form in unique stages. The first stage of binding involves an ATP-stimulated interaction of the UvrA protein with duplex DNA containing pyrimidine dimer sites. The UvrB protein significantly stabilizes the UvrA-pyrimidine dimer containing DNA complex which, in turn, provides a foundation for the binding of UvrC to activate the UvrABC endonuclease. The binding of one molecule of UvrC to each UvrAB-damaged DNA complex is needed to catalyze incision in the vicinity of pyrimidine dimer sites. The UvrABC-DNA complex persists after the incision event suggesting that the lack of UvrABC turnover may be linked to other activities in the excision-repair pathway beyond the initial incision reaction.
mesh_terms: D004260:DNA Repair; D004269:DNA, Bacterial / Q000378:metabolism; D004706:Endodeoxyribonucleases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D029968:Escherichia coli Proteins; D009698:Nucleoproteins; D011485:Protein Binding; D011740:Pyrimidine Dimers / Q000378:metabolism*; D012834:Silver / Q000494:pharmacology
chemical_list: D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; D009698:Nucleoproteins; D011740:Pyrimidine Dimers; D012834:Silver; D004706:Endodeoxyribonucleases; C036385:endodeoxyribonuclease uvrABC