Structure and function of histone methylation binding proteins
Structure and function of histone methylation binding proteins
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DOI：
10.1139/o08-129
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发表时间：
2009-02-01
影响因子：
2.9
通讯作者：
Min, Jinrong
中科院分区：
文献类型：
--
作者：
Adams-Cioaba, Melanie A.;Min, Jinrong
染色质结构受染色质重塑因子、组蛋白交换、连接组蛋白关联和组蛋白修饰的调节。组蛋白的共价修饰是调节相关过程的重要因素。各种组蛋白修饰的实施和去除与 DNA 复制、修复、重组和转录以及 RNA 加工有关。近年来，组蛋白甲基化已成为调节染色质功能的关键修饰之一。然而，所涉及的机制很复杂并且尚不清楚。最近积累了大量关于 Tudor、植物同源域 (PHD) 和恶性脑肿瘤 (MBT) 蛋白家族的结构和生化信息。本综述总结了 PHD、Tudor 和 MBT 结构域在与目标组蛋白肽相互作用时所采用的结构和识别模式的当前知识。
Chromatin structure is regulated by chromatin remodeling factors, histone exchange, linker histone association, and histone modification. Covalent modification of histones is an important factor in the regulation of the associated processes. The implementation and removal of various histone modifications have been implicated in DNA replication, repair, recombination, and transcription, and in RNA processing. In recent years, histone methylation has emerged as one of the key modifications regulating chromatin function. However, the mechanisms involved are complex and not well understood. A large volume of structural and biochemical information has been recently amassed for the Tudor, plant homeodomain (PHD), and malignant brain tumor (MBT) protein families. This review summarizes current knowledge of the structures and modes of recognition employed by the PHD, Tudor, and MBT domains in their interactions with target histone peptides.