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. 2009 Dec 21;206(13):3031–3046. doi: 10.1084/jem.20091892

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© 2009 Ueda et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jem.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 5. — DNA Repair Activities of the rIIHs. (A) Equivalent increasing amounts of rIIHs (adjusted according to Western blotting) were added to an incision/excision assay using recombinant NER factors. The area of the gel containing the excision products is shown (the complete gel is shown in Fig. S1 A). The excised oligonucleotides signals were quantified and plotted in arbitrary units (au). The results are representative of three independent experiments. (B) Helicase activity of the WT and mutated forms of XPD. Equivalent increasing amounts of the various immunoprecipitated rIIH were tested for their 5′–3′ XPD helicase activity. The density of radiolabeled oligo displaced by the XPD helicase activity was measured and plotted in arbitrary units (au). The results are representative of three independent experiments. The complete gel is shown in Fig. S1 B. (C) Equal amounts of immunoprecipitated XPD were tested in an ATPase assay for 120 min. Nonhydrolyzed ATP as well as Pi are indicated. The ATP hydrolysis was quantified and plotted in arbitrary units (au). The results are representative of three independent experiments.