The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition
The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition
复制标题
DOI：
10.1093/embo-reports/kve022
复制
发表时间：
2001-02-01
期刊：
影响因子：
7.7
通讯作者：
Becker, PB
中科院分区：
文献类型：
--
作者：
Akhtar, A;Becker, PB
MOF对组蛋白H4的定点乙酰化是建立果蝇高活性雄性X染色体的关键。MOF属于组蛋白乙酰转移酶(HATS)的MYST家族，其特征是在其HAT结构域附近有一个不寻常的C2HC型锌指。这些稀有的锌指的功能尚不清楚。我们发现，除了已建立的催化结构域外，该结构域对HAT活性也是必不可少的。MOF用它的锌指接触核小体的球状部分以及组蛋白H4N末端的尾部底物。然而，保持锌指结构不变的点突变会取消它与核小体的相互作用。我们的数据证明了C2HC型手指在核小体结合和HAT活性中的新角色。
Site-specific acetylation of histone H4 by MOF is central to establishing the hyperactive male X chromosome in Drosophila. MOF belongs to the MYST family of histone acetyltransferases (HATs) characterized by an unusual C2HC-type zinc finger close to their HAT domains. The function of these rare zinc fingers is unknown. We found that this domain is essential for HAT activity, in addition to the established catalytic domain. MOF uses its zinc finger to contact the globular part of the nucleosome as well as the histone H4 N-terminal tail substrate. Point mutations that leave the zinc-finger structure intact nevertheless abolish its interaction with the nucleosome. Our data document a novel role of the C2HC-type finger in nucleosome binding and HAT activity.