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- W2017978995 abstract "The nicking of damaged DNA during the nucleotide excision repair reaction in E. coli, is the result of a multi-step process involving three enzymes, UvrA, UvrB and UvrC. The UvrB protein is loaded on the site of the damage by UvrA, forming a stable UvrB–DNA complex. This complex is recognized by UvrC and in the resulting UvrBC–DNA complex dual incision takes place, first on the 3′-side and next on the 5′-side of the damaged nucleotide. A domain in the C-terminal part of UvrB has been identified to be essential for formation of the specific UvrBC–DNA complex that induces the 3′-incision [1]. The N-terminal half of UvrC contains a region that is homologous to this C-terminal domain of UvrB. Using site-directed mutagenesis of a conserved phenylalanine in the homologous regions of UvrB and UvrC two mutants were constructed, UvrB(F652L) and UvrC(F223L). Both proteins were tested in vitro using a DNA substrate with a defined cisplatin lesion. The protein–DNA and protein–protein interactions were studied using bandshift assays and DNAse I footprinting. We show that both domains are important for the binding of UvrC to the UvrB–DNA complex." @default.
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- W2017978995 date "1997-12-01" @default.
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- W2017978995 title "Function of the homologous regions of the Escherichia coli DNA excision repair proteins UvrB and UvrC in stabilization of the UvrBC–DNA complex and in 3′-incision" @default.
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- W2017978995 doi "https://doi.org/10.1016/s0921-8777(97)00042-6" @default.
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