Multiplicity of histone deacetylase from calf thymus

Abstract

Histone is modified enzymatically with acetyl, methyl and phosphoryl groups, and enzymes catalyzing these reactions may play an important role in the regulation of gene expression [ 11. Recently, the multiplicity and organ specificity of histone acetylase were reported [2]. These features of the enzyme may be compatible with the proposed role of histone acetylation in the complex process of gene regulation. Histone deacetylase was demonstrated first in an extract of calf thymus [3,4] and subsequently in extracts of various animal and plant tissues [5,6]. The enzyme from calf thymus acts on the specific e-N-acetyllysyl residues in arginine-rich histone fractions, f2al and f3 [7]. However, the enzyme has not yet been purified and the question as to whether the deacetylation of histone is achieved by multiple enzymes, as is the case with histone acetylation, remains to be solved. We report here the partial purification of histone deacetylase from calf thymus. During the purification, we obtained the results which suggested the multiplicity of the enzyme.