title: 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.
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D002645:Chickens; D002729:Chloromercuribenzoates / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D004247:DNA / Q000494:pharmacology; D004912:Erythrocytes / Q000378:metabolism; D051548:Histone Acetyltransferases; D006657:Histones / Q000378:metabolism; D066298:In Vitro Techniques; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D002729:Chloromercuribenzoates; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D012710:Serum Albumin, Bovine; D004247:DNA; D000123:Acetyltransferases; D051548:Histone Acetyltransferases