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. Author manuscript; available in PMC: 2014 Jul 1.
Published in final edited form as: Nat Commun. 2014;5:2987. doi: 10.1038/ncomms3987

Fig. 2.

Fig. 2

The positively charged patches of MHF are essential for DNA binding. Overall (top-left inset, shown as electrostatic surface; blue: positive, red: negative) and detailed (ribbon representation) views of the MHF-DNA interface (tetramer 1 in MHF-DNA1). a, The critical top and shoulder residues (stick representation) for DNA binding are in blue, the positively charged arm (highlighted by ovals) residues are in light-blue sticks, and those residues that do not affect DNA binding are in cyan. b, Electrophoretic mobility shift analysis of MHF mutants with various DNA substrates (the schematics of the HJ DNA, Y-DNA and dsDNA are shown on the left with the radiolabeled terminus indicated by an asterisk). The substrates (30 nM) were incubated with increasing amounts of WT or mutant MHF (25, 50, 75 and 100 nM) and analyzed. NP - no protein added. c. The results were quantified and plotted in the bar graphs. Error bars were generated from the standard deviation in triplicate experiments.