Probing the acetylation code of histone H4
Probing the acetylation code of histone H4
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DOI：
10.1002/pmic.201200568
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发表时间：
2013-10
期刊：
影响因子：
3.4
通讯作者：
Diana Lang;M. Schümann;K. Gelato;W. Fischle;D. Schwarzer;E. Krause
中科院分区：
文献类型：
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作者：
Diana Lang;M. Schümann;K. Gelato;W. Fischle;D. Schwarzer;E. Krause
组蛋白修饰在基因组调控中起关键作用，赖氨酸乙酰化参与转录调控。在这里，我们报告了一项全蛋白质组的研究，研究了组蛋白H4的N-末端末端的乙酰化依赖的蛋白质-蛋白质相互作用。使用SILAC方法的基于多肽的定量亲和MS实验确定了H4尾巴在四个已知的乙酰化位点K5、K8、K12和K16单乙酰化、在K5/K12双乙酰化、在K8/12/16三乙酰化和完全四乙酰化的相互作用。一组29个蛋白质被发现富含在完全乙酰化的H4尾巴上，而单乙酰化和双乙酰化的尾巴几乎检测不到特定的结合蛋白。这些观察结果与早期的报道很好地一致，这些报道表明H4乙酰化状态以累积的方式建立其调节效应，而不是通过调节蛋白的位点特异性招募。
Histone modifications play crucial roles in genome regulation with lysine acetylation being implicated in transcriptional control. Here we report a proteome‐wide investigation of the acetylation‐dependent protein–protein interactions of the N‐terminal tail of histone H4. Quantitative peptide‐based affinity MS experiments using the SILAC approach determined the interactomes of H4 tails monoacetylated at the four known acetylation sites K5, K8, K12, and K16, bis‐acetylated at K5/K12, triple‐acetylated at K8/12/16 and fully tetra‐acetylated. A set of 29 proteins was found enriched on the fully acetylated H4 tail while specific binders of the mono and bis‐acetylated tails were barely detectable. These observations are in good agreement with earlier reports indicating that the H4 acetylation state establishes its regulatory effects in a cumulative manner rather than via site‐specific recruitment of regulatory proteins.