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Fig. 6 | BMC Microbiology

Fig. 6

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. 6

Effect of nucleotide cofactors on nuclease activity of HpMutS2 and mutants. Plots showing time dependent depletion of substrate DNA (a, b, c) Single-stranded DNA and d, e, f Holliday junction. DNA substrates (1 nM) were incubated with HpMutS2 and mutants (150 nM) at 37 °C. Reactions aliquots were removed at 0, 15, 30, 60, 90, and 120 min. The reactions were stopped using (50 mM EDTA + formamide dye) and the products were electrophoresed on urea-PAGE (15 %). The percentage reduction in substrate was calculated by considering DNA without protein as 100 %. Error bars represent standard deviation from two or more different experiments. (g, panel 1–6) Time dependent cleavage of Holliday junction by HpMutS2 and mutants. Reactions were performed as described in (A-F). Reactions aliquots were removed at 0, 15, 30, 60, 90, and 120 min

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BMC Microbiology

ISSN: 1471-2180

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