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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 3. — TFIIH complex into XPD fibroblasts. (A) The diagram represents the 760-aa XPD protein with the 7 (I–VI) helicase motifs. Amino acid changes resulting from mutations found in the XPD/R683W patients who are compound heterozygotes are depicted. (B) Western blot analyses of TFIIH subunits (XPB, XPD, p62, p52, and cdk7) in increasing amounts of whole-cell extracts isolated from fibroblasts of FB789, XP34BE, XP29BE, AS550, and AS552 patients. * indicate nonspecific bands. β-Tubulin (β tub) was used as an internal control. The results are representative of three independent experiments. Diagram represents the ratio between each TFIIH subunit and β tub (arbitrary units). (C) Western blotting analysis of Ab-XPB ChIP (IP XPB) samples from chromatin extracts isolated from HD2 cells transfected with expression vectors encoding either Flag-XPD/WT (∼80 kD), /Q452X (∼53 kD), /199insPP (∼28 kD), or /I455del (∼80 kD). The immunoprecipitated fractions were resolved on SDS-PAGE followed by immunoblotting using antibodies raised against XPB, p62, p44, cyclin H and the Flag-tag. In vitro synthesized Flag-XPD mutated proteins (IVT Flag XPD, lanes 1 to 4) and highly purified TFIIH from HeLa cells (lane 5) were used as references. Arrows indicate the different forms of XPD. * indicate nonspecific bands. The results are representative of three independent experiments.