Akhtar A, Becker P B
Adolf Butenandt-Institut, Molekularbiologie, Ludwig-Maximilians-Universität, München, Germany.
EMBO Rep. 2001 Feb;2(2):113-8. doi: 10.1093/embo-reports/kve022.
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.
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。
