Ⅰ型组蛋白去乙酰化酶复合物结构生物学研究进展
Progress in the structures of class Ⅰ histone deacetylase complexes
王雁南 1王晓 1张贺桥1
作者信息
- 1. 上海科技大学 免疫化学研究所,上海 201210
- 折叠
摘要
Ⅰ型组蛋白去乙酰化酶复合物是从酵母到人所有真核生物中都保守的依赖于锌离子的组蛋白修饰酶.酿酒酵母Rpd3S和裂殖酵母来源同系物Clr6S包含多个亚基,可以被甲基化修饰的组蛋白H3第36位赖氨酸招募到相关核小体位点,随后对组蛋白H3和H4上的乙酰化修饰位点进行去除,以防止隐匿转录的发生.文章总结了近期关于Ⅰ型组蛋白去乙酰化酶复合物结构生物学及生化方面的研究进展,对Ⅰ型组蛋白去乙酰化酶复合物识别核小体底物并对其乙酰化位点进行特异性去除的分子机制进行了讨论.
Abstract
Type Ⅰ histone deacetylase complex(type Ⅰ HDAC complex),conserved from yeast to human,is a zinc-dependent histone modifying enzyme.Both Saccharomyces cerevisiae Rpd3S and Schizosaccharomyces pombe Clr6S,two homologous multiple-subunit complexes,are recruited by histone H3 methylation K36(H3K36me)to open reading frame and remove the acetyl groups from specific lysine residues at histones H3 and H4,thereby suppressing cryptic transcription.In this review,the recent cryo-EM work on type Ⅰ HDAC complexes is summarized,and the mechanisms of nucleosome recognition and subsequent deacetylation by type Ⅰ HDAC complex are discussed.
关键词
组蛋白去乙酰化酶/Clr6S/Rpd3S/核小体/冷冻电镜Key words
histone deacetylase/Clr6S/Rpd3S/nucleosome/cryo-EM引用本文复制引用
出版年
2024
NETL
NSTL
万方数据