Interactions of acetylated H3 and H4 tails with Importins. Pulldown assays of Impβ, Kapβ2, Imp4, Imp5, Imp7, Imp9, and Impα binding to immobilized biotin-tagged unacetylated and acetylated histone H3 tail and H4 tail peptides (SDS-PAGE/Coomassie) were performed. Densities of the gel bands from experiments performed in triplicate are plotted in histograms. t tests were performed to assess effects of acetylation (ns, p > 0.05; *, p ≤ 0.05; **, p ≤ 0.01; ***, p ≤ 0.001; ****, p ≤ 0.0001). A, pulldown binding assays of biotin-H3 tail (unacetylated) versus biotin-H3 tails acetylated at either Lys14 or Lys18. B, pulldown binding assays of biotin-H4 tail (unacetylated) versus biotin-H4 tail acetylated at both Lys5 and Lys12. Error bars represent S.D.