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首页> 外文期刊>Journal of Molecular Biology >The dimeric structure and the bivalent recognition of H3K4me3 by the tumor suppressor ING4 suggests a mechanism for enhanced targeting of the HBO1 complex to chromatin.
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The dimeric structure and the bivalent recognition of H3K4me3 by the tumor suppressor ING4 suggests a mechanism for enhanced targeting of the HBO1 complex to chromatin.

机译：抑癌药ING4对H3K4me3的二聚体结构和二价识别表明了将HBO1复合物靶向染色质的增强机制。

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摘要

The INhibitor of Growth (ING) family of tumor suppressors regulates the transcriptional state of chromatin by recruiting remodeling complexes to sites with histone H3 trimethylated at position K4 (H3K4me3). This modification is recognized by the plant homeodomain (PHD) present at the C-terminus in the five members of the ING family. ING4 facilitates histone H3 acetylation by the HBO1 complex. Here, we show that ING4 forms homodimers through its N-terminal domain, which folds independently into an elongated coiled-coil structure. The central region of ING4, which contains the nuclear localization sequence, is disordered and flexible and does not directly interact with p53, or does it with very low affinity, in contrast to previous findings. The NMR analysis of the full-length protein reveals that the two PHD fingers of the dimer are chemically equivalent and independent of the rest of the molecule. The detailed NMR analysis of the full-length dimeric protein binding to histone H3K4me3 shows essentially the same binding site and affinity as the isolated PHD finger. Therefore, the ING4 dimer has two identical and independent binding sites for H3K4me3 tails, which, in the context of the chromatin, could belong to the same or to different nucleosomes. These results show that ING4 is a bivalent reader of the chromatin H3K4me3 modification and suggest a mechanism for enhanced targeting of the HBO1 complex to specific chromatin sites. This mechanism could be common to other ING-containing remodeling complexes.
机译：通过将重塑复合物募集到在位置K4（H3K4me3）具有三甲基化的组蛋白H3的位点，肿瘤抑制物的生长抑制剂（ING）家族可调节染色质的转录状态。 ING家族五个成员的C末端存在的植物同源域（PHD）可以识别这种修饰。 ING4通过HBO1复合物促进组蛋白H3乙酰化。在这里，我们显示ING4通过其N末端结构域形成同型二聚体，该结构独立折叠成细长的卷曲螺旋结构。与以前的发现相反，ING4的中央区域含有核定位序列，是无序且有弹性的，不直接与p53相互作用，或以非常低的亲和力与之相互作用。全长蛋白质的NMR分析表明，二聚体的两个PHD指在化学上是等价的，并且与分子的其余部分无关。全长二聚体蛋白与组蛋白H3K4me3结合的详细NMR分析显示出与分离的PHD手指基本相同的结合位点和亲和力。因此，ING4二聚体具有两个相同且独立的H3K4me3尾部结合位点，在染色质的背景下，它们可能属于相同或不同的核小体。这些结果表明，ING4是染色质H3K4me3修饰的二价阅读器，并提出了将HBO1复合物靶向特定染色质位点的增强机制。此机制可能是其他包含ING的重塑复合体所共有的。

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