Research Paper Volume 4, Issue 11 pp 790—802
The helicase and ATPase activities of RECQL4 are compromised by mutations reported in three human patients
Figure 5. Strand annealing activity is not correspondingly reduced. Amalgamated gel from representative experiments showing annealing activity of WT and mutants at 0, 2.5, 5, 10 and 20 nM protein, as well as double- and single-stranded controls. (B) Annealing data compiled from triplicate experiments. At 2.5 and 5 nM protein, WT shows significantly higher activity than F637S, but at higher concentrations this difference is not seen. ‡ denote p < 0.05 between WT and F697L. Error bars represent standard error of mean from three experiments.