Zhang Y, Sun Z W, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D
Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School Piscataway, New Jersey 08854, USA.
Mol Cell. 1998 Jun;1(7):1021-31. doi: 10.1016/s1097-2765(00)80102-1.
Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Recently, histone acetylation and deacetylation were found to be catalyzed by structurally distinct, multisubunit complexes that mediate, respectively, activation and repression of transcription. Here, we identify SAP30 as a novel component of the human histone deacetylase complex that includes Sin3, the histone deacetylases HDAC1 and HDAC2, histone binding proteins RbAp46 and RbAp48, as well as other polypeptides. Moreover, we describe a SAP30 homolog in yeast that is functionally related to Sin3 and the histone deacetylase Rpd3. The human SAP30 complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones due to the inability of the histone binding proteins RbAp46 and RbAp48 to gain access to nucleosomal histones. These results define SAP30 as a component of a histone deacetylase complex conserved among eukaryotic organisms.
组蛋白乙酰化在真核基因表达调控中起关键作用。最近发现，组蛋白乙酰化和去乙酰化分别由结构不同的多亚基复合物催化，这些复合物分别介导转录的激活和抑制。在此，我们鉴定出SAP30是人类组蛋白去乙酰化酶复合物的一个新组分，该复合物包括Sin3、组蛋白去乙酰化酶HDAC1和HDAC2、组蛋白结合蛋白RbAp46和RbAp48以及其他多肽。此外，我们描述了酵母中与Sin3和组蛋白去乙酰化酶Rpd3功能相关的SAP30同源物。人类SAP30复合物在使核心组蛋白八聚体去乙酰化方面具有活性，但在使核小体组蛋白去乙酰化方面无活性，这是由于组蛋白结合蛋白RbAp46和RbAp48无法接触到核小体组蛋白。这些结果确定了SAP30是真核生物中保守的组蛋白去乙酰化酶复合物的一个组分。
