Tudor, MBT and chromo domains gauge the degree of lysine methylation
Tudor, MBT and chromo domains gauge the degree of lysine methylation
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DOI：
10.1038/sj.embor.7400625
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发表时间：
2006-04-01
期刊：
影响因子：
7.7
通讯作者：
Bedford, MT
中科院分区：
文献类型：
--
作者：
Kim, J;Daniel, J;Bedford, MT
组蛋白的翻译后修饰调节许多细胞过程，包括转录、复制和DNA修复。翻译后修饰的大量组合是可能的。这种密码被称为组蛋白密码。许多酶奠定了这一代码已被确定。然而，到目前为止，很少有编码阅读蛋白被鉴定出来。在这里，我们描述了一种用于识别甲基特异性相互作用蛋白质的蛋白质阵列方法。我们发现，不仅染色体结构域，而且tudor和MBT结构域结合到组蛋白H3和H4的氨基末端尾部的甲基化肽。使用肽下拉，表面等离子体共振和远蛋白质印迹法证实了蛋白质结构域微阵列上观察到的结合特异性。因此，我们的研究揭示了都铎和MBT域作为新的类甲基赖氨酸结合蛋白模块，也表明，蛋白质结构域微阵列是强大的工具，用于识别新的结构域类型，识别组蛋白修饰。
The post-translational modification of histones regulates many cellular processes, including transcription, replication and DNA repair. A large number of combinations of post-translational modifications are possible. This cipher is referred to as the histone code. Many of the enzymes that lay down this code have been identified. However, so far, few code-reading proteins have been identified. Here, we describe a protein-array approach for identifying methyl-specific interacting proteins. We found that not only chromo domains but also tudor and MBT domains bind to methylated peptides from the amino-terminal tails of histones H3 and H4. Binding specificity observed on the protein-domain microarray was corroborated using peptide pull-downs, surface plasma resonance and far western blotting. Thus, our studies expose tudor and MBT domains as new classes of methyl-lysinebinding protein modules, and also demonstrates that proteindomain microarrays are powerful tools for the identification of new domain types that recognize histone modifications.