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Fig. 1. Rapid induction and TSA-hypersensitivity of histone H3 phosphorylated at S28. (A) Quiescent C3H 10T ${gamma}$ fibroblasts were treated with 50 ng/ml EGF (lanes 2-6), 25 ng/ml anisomycin (sAn) (lanes 7-11), 100 nM TPA (lanes 12-16) for the times indicated. Acid-soluble proteins were run on 15% SDS-PAGE and transferred to PVDF membrane for western blotting with anti-phosphoS28-H3 (panel i), anti-phosphoacetyl-H3 (panel ii) or anti-phosphoS10-H3occ (panel iii) antibodies, or Coomassie-stained (panel iv). (B) Quiescent C3H 10T ${gamma}$ fibroblasts were treated with TSA (500 ng/ml, 1 hour, lanes 4-6) or not (lanes 1-3) before stimulating them with TPA (30 minutes, 100 nM, lanes 2, 5), sAn (45 minutes, 25 ng/ml, lanes 3, 6) or not at all (con, lanes 1, 4). Acid-soluble proteins were run on 15% acid-urea gels and transferred to PVDF membrane for western blotting with anti-phosphoS28-H3 (panel i), anti-phosphoacetyl-H3 (panel ii), anti-phosphoS10-H3occ. (panel iii) or anti-phosphoS10-H3 (panel iv), or Coomassie-stained (panel v). Positions of differentially-modified H3 are indicated by bars (and numbered where space permits) according to increasing modification by comparison with Coomassie-stained gels or Ponceau-S-stained PVDF membrane. (C) Quiescent C3H 10T ${gamma}$ fibroblasts were treated with TSA (500 ng/ml, 1 hour, lanes 5-8) or not (lanes 1-4) before stimulating them with with EGF (30 minutes, 50 ng/ml, lanes 2, 5), TPA (30 minutes, 100 nM, lanes 3, 6), sAn (45 minutes, 25 ng/ml, lanes 4, 8), or not at all (lanes 1, 5). Acid-soluble proteins were separated by 15% SDS-PAGE and transferred to PVDF membrane for western blotting with anti-phosphoS28-H3 (panel i), anti-phosphoacetyl-H3 (panel ii), anti-phosphoS10occ. (panel iii) or anti-phosphoS10-H3 (panel iv), or Coomassie-stained (panel v).

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