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首页> 外文期刊>Epigenetics & Chromatin >Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions
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Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions

机译：染色体和Tudor域的组蛋白肽微阵列筛选定义了新的组蛋白赖氨酸甲基化相互作用

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Background Histone posttranslational modifications (PTMs) function to regulate chromatin structure and function in part through the recruitment of effector proteins that harbor specialized “reader” domains. Despite efforts to elucidate reader domain–PTM interactions, the influence of neighboring PTMs and the target specificity of many reader domains is still unclear. The aim of this study was to use a high-throughput histone peptide microarray platform to interrogate 83 known and putative histone reader domains from the chromo and Tudor domain families to identify their interactions and characterize the influence of neighboring PTMs on these interactions. Results Nearly a quarter of the chromo and Tudor domains screened showed interactions with histone PTMs by peptide microarray, revealing known and several novel methyllysine interactions. Specifically, we found that the CBX/HP1 chromodomains that recognize H3K9me also recognize H3K23me2/3—a poorly understood histone PTM. We also observed that, in addition to their interaction with H3K4me3, Tudor domains of the Spindlin family also recognized H4K20me3—a previously uncharacterized interaction. Several Tudor domains also showed novel interactions with H3K4me as well. Conclusions These results provide an important resource for the epigenetics and chromatin community on the interactions of many human chromo and Tudor domains. They also provide the basis for additional studies into the functional significance of the novel interactions that were discovered.
机译：背景组蛋白翻译后修饰（PTM）的功能是调节染色质的结构和功能，部分是通过募集具有特殊“阅读器”结构域的效应蛋白来实现的。尽管努力阐明阅读器域与PTM的相互作用，但尚不清楚邻近PTM的影响和许多阅读器域的靶标特异性。这项研究的目的是使用高通量组蛋白肽微阵列平台，对来自染色体和Tudor域家族的83个已知和推定的组蛋白阅读器域进行询问，以鉴定它们的相互作用并表征相邻PTM对这些相互作用的影响。结果筛选的近四分之一的色度和Tudor域显示通过肽微阵列与组蛋白PTM相互作用，揭示了已知的和几种新颖的甲基赖氨酸相互作用。具体来说，我们发现识别H3K9me的CBX / HP1色域也识别H3K23me2 / 3，这是一个不太了解的组蛋白PTM。我们还观察到，除了与H3K4me3相互作用之外，Spindlin家族的Tudor域还识别H4K20me3，这是以前未知的相互作用。几个Tudor域也显示出与H3K4me的新颖相互作用。结论这些结果为表观遗传学和染色质群落在许多人类染色体和Tudor域之间的相互作用提供了重要资源。它们还为进一步研究发现的新型相互作用的功能意义提供了基础。

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