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首页> 外文期刊>Current Biology: CB >Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition
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Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition

机译：组合组蛋白修饰对抗体和效应蛋白识别的影响

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Increasing evidence suggests that histone posttranslational modifications (PTMs) function in a combinatorial fashion to regulate the diverse activities associated with chromatin. Yet how these patterns of histone PTMs influence the adapter proteins known to bind them is poorly understood. In addition, how histone-specific antibodies are influenced by these same patterns of PTMs is largely unknown. Here we examine the binding properties of histone-specific antibodies and histone-interacting proteins using peptide arrays containing a library of combinatorially modified histone peptides. We find that modification-specific antibodies are more promiscuous in their PTM recognition than expected and are highly influenced by neighboring PTMs. Furthermore, we find that the binding of histone-interaction domains from BPTF, CHD1, and RAG2 to H3 lysine 4 trimethylation is also influenced by combinatorial PTMs. These results provide further support for the histone code hypothesis and raise specific concerns with the quality of the currently available modification-specific histone antibodies. Highlights: Assessing recognition of posttranslational modifications (PTMs) using peptide arrays Neighboring PTMs modulate antibody recognition of histone modifications Identification of positive and negative influences on chromatin factor recognition
机译：越来越多的证据表明，组蛋白翻译后修饰（PTM）以组合方式起作用，以调节与染色质相关的各种活性。然而，对组蛋白PTM的这些模式如何影响已知的结合它们的衔接蛋白的了解却很少。此外，很大程度上未知组蛋白特异性抗体如何受这些相同的PTM模式影响。在这里，我们使用包含经组合修饰的组蛋白肽库的肽阵列，检查组蛋白特异性抗体和组蛋白相互作用蛋白的结合特性。我们发现修饰特异性抗体在PTM识别中比预期的更加混杂，并且受邻近PTM的影响很大。此外，我们发现从BPTF，CHD1和RAG2到H3赖氨酸4三甲基化的组蛋白相互作用域的结合也受到组合PTM的影响。这些结果为组蛋白密码假说提供了进一步的支持，并引起了对当前可用的修饰特异性组蛋白抗体质量的特殊关注。亮点：使用肽阵列评估翻译后修饰（PTM）的识别相邻的PTM调节组蛋白修饰的抗体识别鉴定对染色质因子识别的正向和负面影响

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