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- W2000405188 abstract "Escherichia coli UvrD protein is a superfamily 1 DNA helicase which plays a crucial role in nucleotide excision repair and methyl-directed mismatch repair. There is a general consensus that the enzyme unwinds a duplex DNA from a 3′ end single-stranded DNA (ssDNA) tail, a gap or a nick. However, conflicting models for the unwinding mechanism have been proposed. Concerning its stoichiometry, some biochemical studies have suggested that the enzyme has optimal activity as an oligomeric form. However, a structural study has indicated that the enzyme functions as a monomer deduced from structural analysis of UvrD-DNA complexes. To address this issue, we attempted to unravel the number of UvrD molecules bound to DNA in the presence and absence of nucleotide by single-molecule fluorescence microscopy. We performed single-molecule visualization of a Cy5-labeled Cys-Ala mutant (Cy5-UvrDC640A), in which Cys52 was labeled with high specificity, bound to 18-bp duplex DNA having a 12, 20 or 40-nt ssDNA tail under several Cy5-UvrDC640A concentrations (0.5, 1.0 and 2.0 nM). We analyzed the number of Cy5 photobleaching steps to quantify the number of UvrD molecules bound to the DNA in the absence and presence of an ATP analog, ATPγS. All the distributions of the number agreed well with the predicted distributions which support the model that UvrD protein is bound to the DNA as an oligomeric form. In the presence of ATP, inefficient DNA unwinding in the absence of free Cy5-UvrDC640A in solution and higher fluorescence intensity of Cy5-UvrDC640A compared to that non-specifically attached on the surface were observed. These results indicate that an oligomer of UvrD is the active form of the helicase." @default.
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- W2000405188 date "2010-01-01" @default.
- W2000405188 modified "2023-10-01" @default.
- W2000405188 title "Single-Molecule Visualization of the Oligomeric form of Escherichia Coli UvrD Helicase In Vitro" @default.
- W2000405188 doi "https://doi.org/10.1016/j.bpj.2009.12.1461" @default.
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