H4K20me is an epigenetic modification to the DNA packaging protein Histone H4. It is a mark that indicates the methylation at the 20th lysine residue of the histone H4 protein. This mark can be mono-, di-, or tri-methylated. It is critical for genome integrity including DNA damage repair, DNA replication and chromatin compaction.

H4K20me 是一种抑制性的组蛋白修饰，被 L3MBTL1 蛋白（histonemethyl-lysine binding protein）的 MBT（malignant brain tumor）结构域结合，导致染色质致密化。

2013年3月1日 · Intense research during the past few years has revealed histone H4 lysine 20 methylation (H4K20me) as critically important for the biological processes that ensure genome integrity, such as DNA damage repair, DNA replication and chromatin compaction.

2021年8月20日 · Here, we describe a divergent role for histone H4 lysine 20 mono-methylation (H4K20me1) and demonstrate that it directly facilitates chromatin openness and accessibility by disrupting chromatin...

2018年9月12日 · Our data suggest that a histone H4K20me-dependent chromatin compaction threshold imposes constraints and hence regulates the chromatin loading of ORC and the MCM2-7 complexes.

2016年3月1日 · We review the signaling pathways and functions associated with a single residue, H4K20, as a model chromatin and clinically important mark that regulates biological processes ranging from the DNA damage response and DNA replication to gene expression and silencing. The human genome consists of greater than 20,000 protein-coding genes (1).

2022年7月30日 · H4K20me是DNA包装蛋白组蛋白H4的一种表观遗传修饰。 它是一个表示在组蛋白H4蛋白的第20个赖氨酸残基上的单甲基化的标记。 这个标记可以被二甲基化和三甲基化。 它对基因组的完整性至关重要，包括DNA损伤修复、DNA复制和染色质的压实。

2022年2月7日 · In this review, we summarize the critical roles of histone lysine methylation, especially H4K20 methylation, and the relevant modulating enzymes in the DDR. Histone methylation has been recognized as being a PTM since 1964 (Murray, 1964).

2009年2月27日 · Methylation of histone H4 lysine 20 (H4K20me) is essential for recruiting checkpoint proteins 53BP1/Crb2 to DNA lesions and subsequent activation of a DNA-damage checkpoint. In fission yeast, Set9 (spKMT5) catalyzes mono-, di-, and trimethylation of H4K20. However, the mechanisms that regulate Set9 function are poorly understood.

揭示了TIRR抑制53BP1识别组蛋白修饰H4K20me2的结构基础和分子机制。 这项研究通过解析TIRR/53BP1 Tudor复合物的 1.76 Å 分辨率晶体结构，发现TIRR通过其N端区域以及L8 loop结合53BP1 Tudor，诱导Tudor结构域上用于阅读H4K20me2 分子标记 的芳香笼结构发生构象改变，抑制3BP1 Tudor对H4K20me2的识别能力。 本研究还通过生物化学、生物物理、细胞生物学等多种方法验证了在TIRR/53BP1相互作用中关键的氨基酸残基。 图三 TIRR与53BP1 Tudor的复合 …