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 3. All mutants have decreased helicase activity. (A) Amalgamated gel from representative experiments showing helicase activity of WT and mutants at 0, 12.5, 25, 50 and 100 nM protein, as well as a single-stranded control. (B) Unwinding data compiled from triplicate experiments. The P466L and F697L mutants show significantly reduced helicase activity compared to wild-type (38% and 28% of WT respectively at 100 nM protein), while F637S has no detectable activity. *, †, and ‡ denote p < 0.05 between WT and P466L, F637S and F697L, respectively. Error bars represent standard error of mean from three experiments.