Expanded lysine acetylation specificity of Gcn5 in native complexes
Expanded lysine acetylation specificity of Gcn5 in native complexes
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DOI：
10.1074/jbc.274.9.5895
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发表时间：
1999-02-26
影响因子：
4.8
通讯作者：
Workman, JL
中科院分区：
文献类型：
--
作者：
Grant, PA;Eberharter, A;Workman, JL
Gcn 5是一种保守的组蛋白乙酰转移酶，在多种酵母转录调控复合物中起催化亚基的作用。Gcn 5乙酰化核小体组蛋白的能力相对于其对游离组蛋白的活性显著降低，其中它主要在赖氨酸14处修饰组蛋白H3。然而，Gcn 5在多亚基复合物中的结合增强了其核小体组蛋白乙酰转移酶活性。在这里，我们表明，协会GCN 5与其他蛋白质在两个天然酵母复合物，阿达和佐贺（Spt-Ada-GCN 5-乙酰转移酶），直接赋予GCN 5的能力乙酰化的一组扩大的赖氨酸H3。此外，Ada和佐贺具有重叠但不同的乙酰化模式，表明特定亚基的关联决定位点特异性。
The coactivator/adaptor protein Gcn5 is a conserved histone acetyltransferase, which functions as the catalytic subunit in multiple yeast transcriptional regulatory complexes. The ability of Gcn5 to acetylate nucleosomal histones is significantly reduced relative to its activity on free histones, where it predominantly modifies histone H3 at lysine 14. However, the association of Gcn5 in multisubunit complexes potentiates its nucleosomal histone acetyltransferase activity. Here, we show that the association of Gcn5 with other proteins in two native yeast complexes, Ada and SAGA (Spt-Ada-Gcn5-acetyltransferase), directly confers upon Gcn5 the ability to acetylate an expanded set of lysines on H3. Furthermore Ada and SAGA have overlapping, yet distinct, patterns of acetylation, suggesting that the association of specific subunits determines site specificity.