Fig. 6.

Phosphorylation of histone H3 at Ser10 is involved in LMP1 induction of Fra-1 and c-Jun in CNE1 cells. (a) The expressions of H3 WT and H3 S10A mutant in stably transfected CNE1 cells were detected with an anti-His antibody against His-histone H3 by Western blotting. Histone H2A was used as loading control. (b) CNE1 cells stably expressing mock, H3 WT or mutant H3 S10A were transfected with pcDNA3.0 or pcDNA3.0-LMP1. At 36 hours after transfection, the firefly luciferase activity was measured and normalized against Renilla luciferase activity respectively. *P < 0.01; **P < 0.005, compared with mock/LMP1 cells. (c) The effect of overexpressing histone H3 WT or H3 S10A mutant on Fra-1 or c-Jun protein levels induced by LMP1 was examined by Western blotting. β-actin was used as loading control. Corresponding signaling intensities of Fra-1 or c-Jun were densitometrically determined and normalized to β-actin in each lane and is given below in each data