THAP Domain Containing Protein 7 (THAP7)

THAP7 bound to all histone H3 tail peptides tested, including peptides that were mono-, di-, tri-, or tetraacetylated, as well as peptides modified by phosphorylation or methylation. However, THAP7 only bound histone H4 peptides that were unmodified, mono-, or diacetylated, and not to H4 peptides that were tri- or tetraacetylated. THAP7 localized primarily to the nucleus in several cell lines, and it was found in the soluble nuclear fraction and chromatin fraction of disrupted 293T cells. In chromatin association assays, THAP7 bound less tightly to hyperacetylated chromatin than to hypoacetylated chromatin, and the C-terminal acidic domain was required for chromatin binding. Coimmunoprecipitation and pull-down assays showed that THAP7 interacted with HDAC3 and with NCOR in 293T cell nuclear lysates.