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. Author manuscript; available in PMC: 2012 Sep 17.
Published in final edited form as: Mol Cell. 2011 Jan 7;41(1):46–55. doi: 10.1016/j.molcel.2010.12.008

Figure 4. The Acidic domain and NAP1L motif of APLF are critical for its DNA repair function.

Figure 4

A, Recruitment of wild-type YFP-APLF and YFP-APLF lacking the C-terminal acidic domain (APLFΔAcidic) to the sites of laser-induced DNA damage. B, Time course showing recruitment and disassociation of APLF and APLFΔAcidic from sites of laser-induced DNA damage. The relative fluorescence values as shown in the graph were calculated by normalising against background fluorescence intensity in the nucleus for the wildtype and mutant protein respectively. C, APLF shifts from the soluble to the chromatin-bound fraction after H2O2 treatment. Retention of APLF variants with mutations in acidic domain in the chromatin following DNA damage is severely prolonged as compared to wt APLF. D, FACS-based survival assays of U2OS cells stably transfected with control or APLF shRNAs and subjected to indicated doses of phleomycin. E, APLFΔAcidic and APLF mutated in the histone-binding NAP1L motif (W485A mutant) are unable to complement DNA repair deficiency of APLF− cells as judged by FACS based live-dead cell analysis. The error bars represent s.d. (n=3).