The tumor suppressor inhibitor of growth 4 (ING4) regulates chromatin structure by recruiting the histone acetyl transferase complex HBO1 to sites with histone H3 trimethylated at K4. ING4 dimerizes through its N-terminal domain and recognizes H3K4me3 by the C-terminal plant homeodomain (PHD). The central region of ING4 is disordered and contains the nuclear localization signal. Here, utilizing electrophoresis and nuclear magnetic resonance, we show that ING4 binds double-stranded DNA through its central region with micromolar affinity. Our findings suggest that the cooperativity arising from the presence of two DNA-binding regions in the ING4 dimer, as well as two H3K4me3-binding PHD fingers, may strengthen nucleosome binding and HBO1 complex recruitment.
Keywords: DNA binding; chromatin remodeling; electrophoretic mobility shift assay; inhibitor of growth 4; nuclear magnetic resonance; tumor suppressor.
© 2016 Federation of European Biochemical Societies.