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Effector proteins for methylated histones: an expanding family.

机译：甲基化组蛋白的效应蛋白：一个扩展的家族。

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Methylation of histone lysine residues in eukaryotic chromatin has been an exciting area of research ever since the first histone methyltransferase enzyme, Suv39h, was found to methylate lysine 9 of histone H3 in 2000. Only a year later, the HP1 chromodomain polypeptide was identified as a recognition module for this histone modification. Similar to bromodomain-containing proteins that recognize histone acetylation sites and subsequently stabilize large complexes to chromatin, effector proteins can also be recruited and stabilized by histone methylation. Although histone acetylation generally correlates with active transcription, histone methylation is associated with both the activation and silencing of transcription, depending on which lysine residue is modified. The list of proteins that may in fact directly associate with specific methylated histone lysines is expanding. Since the finding of HP1, many additional proteins have been shown to bind methylated histone residues. For instance, Polycomb, Chd1, 53BP1, and Crb2/Rad9 proteins all associate with methylated chromatin in a unique manner governed by their respective recognition motifs. Here we highlight recent data on the recognition specificity and biological significance of proteins that associate with methylated histone lysines.
机译：自从2000年发现第一个组蛋白甲基转移酶Suv39h使组蛋白H3的赖氨酸9甲基化以来，真核染色质中组蛋白赖氨酸残基的甲基化一直是令人兴奋的研究领域。仅一年后，HP1染色体结构域多肽被鉴定为用于组蛋白修饰的识别模块。与识别组蛋白乙酰化位点并随后稳定大分子复合物至染色质的含溴结构域蛋白相似，效应蛋白也可以通过组蛋白甲基化来募集并稳定化。尽管组蛋白乙酰化通常与活性转录相关，但组蛋白甲基化与转录的激活和沉默都相关，这取决于赖氨酸残基被修饰的程度。实际上可能与特定的甲基化组蛋白赖氨酸直接缔合的蛋白质的清单正在扩大。自发现HP1以来，已显示许多其他蛋白质可结合甲基化的组蛋白残基。例如，Polycomb，Chd1、53BP1和Crb2 / Rad9蛋白均以独特的方式与甲基化染色质相关联，并受其各自的识别基序支配。在这里，我们重点介绍与甲基化组蛋白赖氨酸相关的蛋白质的识别特异性和生物学意义的最新数据。

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