Partial purification and properties of two histone acetyltransferases from the yeast, Saccharomyces cerevisiae

Abstract

Two histone acetyltransferases, A and B, have been extracted and partially purified from yeast cells. The purification scheme included ammonium sulfate precipitation, and chromatography on DEAE-Sepharose and Sephadex G-200. The basic properties of both enzymes closely correspond to those of acetyltransferase A and B found in higher eucaryotes. Yeast enzyme A elutes from DEAE-Sepharose prior to acetyltransferase B, and it is activated by low concentrations of DNA and strongly inhibited by p-chloromercuribenzoate (PCMB). Enzyme B is inhibited by DNA over the entire range of concentrations tested and it is less sensitive to PCMB than enzyme A. When assayed with yeast whole histones, enzyme B shows a marked specificity toward histone H4, although H3 and H2B are also accepted as substrates. Enzyme A preferentially catalyzes the acetylation of yeast H2B and H3, with the other two core histones being acetylated to a much lesser extent.