Stimulation of the UvrABC enzyme-catalyzed repair reactions by the UvrD protein (DNA helicase II).
An in vitro assay system was constructed using highly purified preparations of UvrA, UvrB, UvrC, UvrD proteins and DNA polymerase I, the objective being to analyse the role of UvrD protein in excision repair of UV-induced DNA damage. UvrABC enzyme-initiated repair synthesis was greatly enhanced by the addition of UvrD protein to the reaction mixture. Further analysis revealed that UvrD protein stimulated introduction of strand breaks in irradiated DNA by UvrABC enzyme but had no effect on the DNA polymerase I reaction. Thus, the site of action of UvrD protein is probably at the incision-excision step and not in later steps in excision repair.
Kumura
K
K
Sekiguchi
M
M
Steinum
A L
AL
Seeberg
E
E
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D004265:DNA Helicases; D004256:DNA Polymerase I / Q000378:metabolism; D004260:DNA Repair; D004269:DNA, Bacterial / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D013997:Time Factors
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; D004256:DNA Polymerase I; D000251:Adenosine Triphosphatases; C506746:UvrD protein, E coli; D004265:DNA Helicases