The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.
The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.
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MOF复合物中的环手指蛋白MSL2是H2B K34的E3泛素连接酶，与H3 K4和K79甲基化串扰。
DOI：
10.1016/j.molcel.2011.05.015
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发表时间：
2011-07-08
期刊：
影响因子：
16
通讯作者：
Dou Y
中科院分区：
文献类型：
--
作者：
Wu L;Zee BM;Wang Y;Garcia BA;Dou Y
我们证明MOF-MSL复合体中的无名指蛋白MSL2是一种组蛋白泛素E3连接酶。MSL2和MSL1具有强大的组蛋白泛素化活性，主要靶向核小体H2B的赖氨酸34位点（H2B K34ub），这是H2B尾部保守碱性斑块内的一个位点。MSL1/2介导的H2B K34ub在体外和细胞内通过跨尾串扰直接调控H3 K4和K79的甲基化。MSL1/2的活性对于HOXA9和MEIS1位点的转录激活很重要，并且这种活性在果蝇剂量补偿复合体中具有进化保守性，这一事实强调了MSL1/2介导的组蛋白H2B泛素化的重要性。总之，这些结果表明MOF- msl复合物通过MOF和MSL2亚基具有两种不同的染色质修饰活性（即H4 K16乙酰化和H2B K34泛素化）。他们还揭示了染色质修饰酶的复杂网络如何在基因激活中协调起作用。
We demonstrate that RING finger protein MSL2 in the MOF-MSL complex is a histone ubiquitin E3 ligase. MSL2, together with MSL1, has robust histone ubiquitylation activity that mainly targets nucleosomal H2B on lysine 34 (H2B K34ub), a site within a conserved basic patch on H2B tail. H2B K34ub by MSL1/2 directly regulates H3 K4 and K79 methylation through trans-tail crosstalk both in vitro and in cells. The significance of MSL1/2 mediated histone H2B ubiquitylation is underscored by facts that MSL1/2 activity is important for transcription activation at HOXA9 and MEIS1 loci and that this activity is evolutionarily conserved in the Drosophila dosage compensation complex. Altogether, these results establish that the MOF-MSL complex possesses two distinct chromatin-modifying activities (i.e. H4 K16 acetylation and H2B K34 ubiquitylation) through MOF and MSL2 subunits. They also shed new lights on how intricate network of chromatin modifying enzymes functions coordinately in gene activation.
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