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

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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.