Figure 1: A TAF2–8–10 complex exists in the cytoplasm. | Nature Communications

Figure 1: A TAF2–8–10 complex exists in the cytoplasm.

From: Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules

Figure 1

(a) Purified, polyclonal anti-TAF2 antibodies specifically recognize recombinant and endogenous TAF2. Recombinant (rec.) purified TAF2 (10 ng, lane 1) and immunopurified TFIID (300 and 150 ng; lanes 2, 3) were loaded on an 8% SDS–PAGE, blotted and analysed by western blot assay. Protein size markers are indicated. (b) Abundances of individual proteins co-immunoprecipitated from nuclear or cytoplasmic HeLa cell extracts (grey or black bars, respectively) using purified polyclonal anti-TAF2 antibodies were compared in units of normalized spectral abundance factors (NSAFs). Each column is the average of two independent experiments and error bars represent range of the data. (c) Domain organization of TAF2, TAF8 and TAF10 in a schematic view. Grey rectangles indicate predicted, unstructured regions. The NLS of TAF8 is shown as a black bar. Numbers indicate first and last amino acids in each protein. (d) Immunofluorescence microscopy of HeLa cells. Nuclei are visualized by 4′,6-diamidino-2-phenylindole (DAPI) staining (blue). TAF2 is displayed in green and TAF8 in red. The bottom panel shows images of control cells, which were treated with secondary antibodies only. Scale bar, 10 μm. (e) Immunofluorescence microscopy of HeLa cells as in d, but displaying TAF2 (green) and TAF10 (red).

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