Chromatin condensation and recruitment of PHD finger proteins to histone H3K4me3 are mutually exclusive.
Chromatin condensation and recruitment of PHD finger proteins to histone H3K4me3 are mutually exclusive.
复制标题
DOI：
10.1093/nar/gkw193
复制
发表时间：
2016-07-27
影响因子：
14.9
通讯作者：
Kutateladze TG
中科院分区：
文献类型：
--
作者：
Gatchalian J;Gallardo CM;Shinsky SA;Ospina RR;Liendo AM;Krajewski K;Klein BJ;Andrews FH;Strahl BD;M van Wely KH;Kutateladze TG
组蛋白翻译后修饰及其产生的特定组合介导了广泛的核事件。然而，识别这些组合的机制基础尚未阐明。在这里，我们的特点之间的串扰H3 T3和H3 T6磷酸化，发生在有丝分裂，和H3 K4 me 3，一个标记与活跃的转录。我们详细介绍了H3 T3 ph/K4 me 3/T6 ph开关介导H3 K4 me 3结合蛋白活性的分子机制，包括那些含有植物同源结构域（PHD）和双Tudor阅读器结构域的蛋白。我们的结果来自核磁共振化学位移扰动分析，正交结合试验和细胞荧光显微镜研究揭示了一个强的组蛋白H3 T3/T6磷酸化和保留的PHD指蛋白在染色质有丝分裂过程中的反相关性。总之，我们的研究结果揭示了细胞分裂过程中H3 K4 me 3特异性读者染色质参与的机械规则。
Histone post-translational modifications, and specific combinations they create, mediate a wide range of nuclear events. However, the mechanistic bases for recognition of these combinations have not been elucidated. Here, we characterize crosstalk between H3T3 and H3T6 phosphorylation, occurring in mitosis, and H3K4me3, a mark associated with active transcription. We detail the molecular mechanisms by which H3T3ph/K4me3/T6ph switches mediate activities of H3K4me3-binding proteins, including those containing plant homeodomain (PHD) and double Tudor reader domains. Our results derived from nuclear magnetic resonance chemical shift perturbation analysis, orthogonal binding assays and cell fluorescence microscopy studies reveal a strong anti-correlation between histone H3T3/T6 phosphorylation and retention of PHD finger proteins in chromatin during mitosis. Together, our findings uncover the mechanistic rules of chromatin engagement for H3K4me3-specific readers during cell division.