Suppr超能文献

组蛋白H4乙酰转移酶MOF利用一个C2HC型锌指结构进行底物识别。

The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition.

作者信息

Akhtar A, Becker P B

机构信息

Adolf Butenandt-Institut, Molekularbiologie, Ludwig-Maximilians-Universität, München, Germany.

出版信息

EMBO Rep. 2001 Feb;2(2):113-8. doi: 10.1093/embo-reports/kve022.

Abstract

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.

摘要

MOF介导的组蛋白H4位点特异性乙酰化对于在果蝇中建立超活性雄性X染色体至关重要。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。这些罕见锌指的功能尚不清楚。我们发现,除了已确定的催化结构域外,该结构域对于HAT活性也是必不可少的。MOF利用其锌指与核小体的球状部分以及组蛋白H4 N端尾部底物接触。那些使锌指结构保持完整的点突变却消除了它与核小体的相互作用。我们的数据证明了C2HC型锌指在核小体结合和HAT活性中的新作用。

相似文献

引用本文的文献

5
Structure and function of histone acetyltransferase MOF.组蛋白乙酰转移酶MOF的结构与功能。
AIMS Biophys. 2015;2(4):555-569. doi: 10.3934/biophy.2015.4.555. Epub 2015 Oct 19.
8

本文引用的文献

6
The language of covalent histone modifications.共价组蛋白修饰的语言
Nature. 2000 Jan 6;403(6765):41-5. doi: 10.1038/47412.
7
The many HATs of transcription coactivators.转录共激活因子的多种功能
Trends Biochem Sci. 2000 Jan;25(1):15-9. doi: 10.1016/s0968-0004(99)01516-9.

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验