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Fig. 5 | BMC Microbiology

Fig. 5

From: Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function

Fig. 5

Effect of nucleotide cofactors on DNA binding activity of HpMutS2 and mutants. Electrophoretic mobility shift assays were performed by incubating radiolabeled DNA substrates (0.16 nM) with increasing concentrations of proteins as described in Methods section. Nucleotides (1 mM) were added separately to the reaction mixtures. After incubation of 30 min on ice, the reaction mixtures were electrophoresed on native PAGE (8 %) at 4 °C. (a, panel 1–6) Interaction of HpMutS2 and mutants with single-stranded DNA. b-g Plots of percentage of bound DNA substrate (ssDNA and Holliday junction) versus protein concentration. The percentage binding was calculated by measuring the depletion in substrate DNA considering DNA without protein as 100 %. Error bars represent standard deviation from two or more different experiments. Schematic representation of DNA substrates used are shown at the left side of figures

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