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 6. WRN RQC mutants are folded properly.
(A) WRN mutants are able to stimulate DNA unwinding activity of wild type WRN by forming hetero oligomeric structure. 2 nM of either native or heat-denatured WRN wild type (2d, heat denatured form) was mixed with 4 nM of either native or heat-denatured WRN mutant (4d, heat denatured form), and incubated with 0.5 nM forked duplex substrate at 37 °C for 20 min. Reaction products were separated on 8% polyacrylamide gel. Δ indicates heat-denatured substrate control. (B) Quantitative analysis of (A). Experiments were repeated at least three times, error bars represent ± SD.