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首页> 外文期刊>Molecular and Cellular Biology >An Oligomerized 53BP1 Tudor Domain Suffices for Recognition of DNA Double-Strand Breaks
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An Oligomerized 53BP1 Tudor Domain Suffices for Recognition of DNA Double-Strand Breaks

机译：寡聚的53BP1 Tudor域足以识别DNA双链断裂。

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摘要

53BP1, the vertebrate ortholog of the budding yeast Rad9 and fission yeast Crb2/Rhp9 checkpoint proteins, is recruited rapidly to sites of DNA double-strand breaks (DSBs). A tandem tudor domain in human 53BP1 that recognizes methylated residues in the histone core is necessary, but not sufficient, for efficient recruitment. By analysis of deletion mutants, we identify here additional elements in 53BP1 that facilitate recognition of DNA DSBs. The first element corresponds to an independently folding oligomerization domain. Replacement of this domain with heterologous tetramerization domains preserves the ability of 53BP1 to recognize DNA DSBs. A second element is only about 15 amino acids long and appears to be a C-terminal extension of the tudor domain, rather than an independently functioning domain. Recruitment of 53BP1 to sites of DNA DSBs is facilitated by histone H2AX phosphorylation and ubiquitination. However, none of the 53BP1 domains/elements important for recruitment are known to bind phosphopeptides or ubiquitin, suggesting that histone phosphorylation and ubiquitination regulate 53BP1 recruitment to sites of DNA DSBs indirectly.
机译：53BP1是发芽酵母Rad9和裂变酵母Crb2 / Rhp9检查点蛋白的脊椎动物直系同源物，可迅速募集到DNA双链断裂（DSB）的位点。识别组蛋白核心中甲基化残基的人5​​3BP1中的串联Tudor域对于有效募集是必要的，但还不够。通过删除突变体的分析，我们在这里确定了53BP1中有助于识别DNA DSB的其他元素。第一元素对应于独立折叠的低聚结构域。用异源四聚化结构域替换该结构域保留了53BP1识别DNA DSB的能力。第二个元素只有大约15个氨基酸长，似乎是tudor结构域的C端延伸，而不是独立起作用的结构域。组蛋白H2AX磷酸化和泛素化促进了53BP1向DNA DSBs位点的募集。然而，已知对募集重要的53BP1结构域/元件均未结合磷酸肽或泛素，这表明组蛋白磷酸化和泛素化间接调节53BP1募集至DNA DSB的位点。

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