Histone deacetylase 2 isoforms and association with chromatin

摘要

Histone deacetylase 2 (HDAC2) is one of the histone-modifying enzymes that regulates gene expression by remodeling chromatin structure. Along with HDAC1, it is found in the Sin3 and NuRD multiprotein complexes, which are recruited to promoters by DNA binding proteins. In this study, we show that HDAC2 in human breast cancer cells is mostly aot phosphorylated. However, a minor population of HDAC2, preferentially cross-linked to DNA by cisplatin and formaldehyde, is mono-, di-, or tri-phosphorylated. Moreover, the formation of Sin3 and NuRD complexes, as well as their recruitment to promoters by factors such as p53, Rb, YY1, p50, p65, Spl, and Sp3, are dependent on HDAC2 phosphorylation.