The UvrABC endonuclease system of Escherichia coli--a view from Baltimore.
Nucleotide excision is initiated by the UvrABC endonuclease system in which the initial DNA interaction is with UvrA which was dimerized in the presence of ATP. Nucleoprotein formation most likely takes place on undamaged regions of DNA by (UvrA)2 which has been dimerized in the presence of ATP. Topological unwinding of DNA, driven by ATP binding, is increased by the presence of UvrB to approximately a single helical turn. The Uvr(A)2B complex translocates to a damaged site by the combined Uvr(A)2B helicase in which the driving force is provided by the UvrB-associated ATPase. The dual incision reaction is initiated by the binding of the UvrC protein to the Uvr(A)2B-nucleoprotein complex. The proteins in this post-incision nucleoprotein complex do not turn over and require the presence of the UvrD protein and DNA polymerase I under polymerizing conditions. The final integrity of the DNA strands is restored with polynucleotide ligase.
Grossman
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Department of Biochemistry, Johns Hopkins University, School of Hygiene and Public Health, Baltimore, MD 21205.
Yeung
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D000251:Adenosine Triphosphatases / Q000502:physiology; D000595:Amino Acid Sequence; D004249:DNA Damage; D004265:DNA Helicases; D004260:DNA Repair / Q000502:physiology; D004706:Endodeoxyribonucleases / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008954:Models, Biological; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
D029968:Escherichia coli Proteins; D004706:Endodeoxyribonucleases; C036385:endodeoxyribonuclease uvrABC; D000251:Adenosine Triphosphatases; C506746:UvrD protein, E coli; D004265:DNA Helicases