A sensitive and flexible assay for determining histone deacetylase 1 (HDAC1) activity

Abstract

Histones acetylation and deacetylation constitute part of the so-called “histone code” and work in concert with other posttranslational modifications to determine the activity of genes. Deacetylation of histone is carried out by a class of enzymes, known as histone deacetylases (HDACs). The action of HDAC is countered by histone acetyltransferases. Although histone is the best characterized substrate of HDACs, increasing evidence also indicates that non-histone proteins are equally important subtract of HDACs. Since HDACs play an important role in normal physiological and pathophysiological conditions, a sensitive and flexible deacetylation assay that can reliably detect HDAC activity and identify potential novel targets of HDACs is critical.