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首页> 外文期刊>Molecular and Cellular Biology >Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes
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Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes

机译：组蛋白H3K27三甲基化抑制H3结合和SET1样H3K4甲基转移酶复合物的功能

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摘要

Trimethylated histone H3 lysine 4 (H3K4) and H3K27 generally mark transcriptionally active and repressive chromatins, respectively. In most cell types, these two modifications are mutually exclusive, and this segregation is crucial for the regulation of gene expression. However, how this anticorrelation is achieved has not been fully understood. Here, we show that removal of the H3K27 trimethyl mark facilitates recruitment of SET1-like H3K4 methyltransferase complexes to their target genes by eliciting a novel interaction between histone H3 and two common subunits, WDR5 and RBBP5, of SET1-like complexes. Consistent with this result, H3K27 trimethylation destabilizes interactions of H3 with SET1-like complexes and antagonizes their ability to carry out H3K4 trimethylation of peptide (H3 residues 1 to 36), histone octamer, and mononucleosome substrates. Altogether, our studies reveal that H3K27 trimethylation of histone H3 represses a previously unrecognized interaction between H3 and SET1-like complexes. This provides an important mechanism that directs the anticorrelation between H3K4 and H3K27 trimethylation.
机译：三甲基化的组蛋白H3赖氨酸4（H3K4）和H3K27通常分别标记转录活性和抑制性染色质。在大多数细胞类型中，这两个修饰是互斥的，并且这种分离对于调节基因表达至关重要。然而，如何获得这种反相关性还没有被完全理解。在这里，我们显示，通过引发组蛋白H3与SET1样复合物的两个常见亚基WDR5和RBBP5之间的新型相互作用，H3K27三甲基标记的去除促进了SET1样H3K4甲基转移酶复合物向其靶标基因的募集。与此结果一致，H3K27三甲基化会破坏H3与SET1样复合物的相互作用，并拮抗其进行肽（H3残基1至36），组蛋白八聚体和单核小体底物的H3K4三甲基化的能力。总的来说，我们的研究表明，组蛋白H3的H3K27三甲基化抑制了H3和SET1样复合物之间以前无法识别的相互作用。这提供了指导H3K4和H3K27三甲基化之间反相关的重要机制。

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