酵母组蛋白乙酰转移酶的亚细胞定位和核小体特异性

Subcellular localization and nucleosome specificity of yeast histone acetyltransferases.

作者信息

López-Rodas G, Tordera V, Sánchez del Pino M M, Franco L

机构信息

Department of Biochemistry and Molecular Biology, University of Valencia, Burjassot, Spain.

出版信息

Biochemistry. 1991 Apr 16;30(15):3728-32. doi: 10.1021/bi00229a020.

DOI:10.1021/bi00229a020

PMID:2015228

Abstract

We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate both H3 and H4 in nucleosomes. The fourth enzyme, which is located in the cytoplasm, does not accept nucleosomes as substrate, and it represents a canonical type B, H4-specific histone acetyltransferase. Finally, histone deacetylase activity is preferentially found in the nucleus.

摘要

我们之前报道过[洛佩斯 - 罗达斯等人（1989年），《生物化学杂志》264卷，19028 - 19033页]，酿酒酵母含有四种组蛋白乙酰转移酶，可通过离子交换色谱法分离，并研究了它们对酵母游离组蛋白的特异性。在本论文中，我们表明其中三种酶是核内的A型组蛋白乙酰转移酶，它们能够使与核小体结合的组蛋白乙酰化。它们在组蛋白特异性方面存在差异。酶A1可使鸡核小体中的H2A乙酰化，尽管它对酵母游离H2B具有特异性；组蛋白乙酰转移酶A2对H3具有高度特异性，而组蛋白乙酰转移酶A3制剂可使核小体中的H3和H4都乙酰化。第四种酶位于细胞质中，不将核小体作为底物，它代表一种典型的B型、H4特异性组蛋白乙酰转移酶。最后，组蛋白脱乙酰酶活性优先在细胞核中被发现。