Research Paper Volume 4, Issue 6 pp 417—429
DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities
Figure 4. WRN RQC mutants are not able to resolve different structures of DNA substrates. DNA unwinding activity on (A) Holliday junction (HJ) like substrate, (B) G-quadruplex (G4) substrate, (C) D-loop substrate and (D) bubble substrate. 1, 2, 5 nM WRN wild type (lane 2 to 4) or WRN mutants (lane 5 to 7, R993A; lane 8 to 10, F1037A; lane 11 to 13, R993A/F1037A) were incubated with either HJ, G4 or bubble substrate. 5, 10, 20 nM WRN wild type or WRN mutants were incubated with D-loop substrate. Reactions were performed as described in Experimental Procedures. Δ indicates heat-denatured substrate control. (E), (F), (G), (H) Quantitative analysis corresponding to (A), (B), (C), (D), respectively. Experiments were repeated at least three times, error bars represent ± SD.