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. 2014 Jan 6;204(1):129–146. doi: 10.1083/jcb.201305084

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© 2014 Zambrano et al.

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Figure 9. — PKRAA and ATM activation is required for T3-dependent NRF1 induction and oxidative DNA damage. (A) Western blot of NRF1 in TP53KO MEFs treated with T3 for 3 h after transfection with control or NRF1 siRNAs 48 h before. (B) Percentage of nuclei with γ-H2AFX/TP53BP1 foci in these cells. (C) Phosphorylated and total PRKAA evaluated by Western blotting in TP53KO and ATMKO MEFs incubated with T3 for times ranging between 0 and 60 min. Densitometries (P-PRKAA/PRKAA) in arbitrary units (a.u.) are shown on the right. (D) NRF1 levels in TP53KO and wild-type MEFs preincubated for 2 h with 20 µM compound C before treatment with T3 for 3 h. Wt, wild type. (E) NRF1 in TP53KO cells preincubated with 10 µM KU-55993. TUBA1A was used as a loading control. inh., inhibitor. (F) TP53BP1/8-OH-dG immunofluorescences in cells treated as in D and E. Bars, 10 µm. (G) Quantification of TP53BP1/8-OH-dG foci in the same groups (P < 0.0001, n = 3). (H) Cells were infected with adenovirus expressing a dominant-negative (dn) PRKAA. After 24 h, cells were treated with T3 for 3 h, and the levels of NRF1, P-PRKAA, and total PRKAA were analyzed by Western blotting. Mock-infected cells were used as controls. (I) Percentages of nuclei bearing γ-H2AFX/TP53BP1 foci in cells expressing dominant-negative PRKAA. Results are presented as means ± SD. **, P < 0.01; ***, P < 0.001.