Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1

Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1
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DOI：
10.1038/nsmb.1797
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发表时间：
2010-05
期刊：
Nature Structural &Molecular Biology
影响因子：
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通讯作者：
A. Vezzoli;N. Bonadies;M. Allen;S. Freund;C. Santiveri;B. Kvinlaug;B. Huntly;B. Göttgens;M. Bycro
A. Vezzoli;N. Bonadies;M. Allen;S. Freund;C. Santiveri;B. Kvinlaug;B. Huntly;B. Göttgens;M. Bycro
中科院分区：
其他
文献类型：
--
作者：
A. Vezzoli;N. Bonadies;M. Allen;S. Freund;C. Santiveri;B. Kvinlaug;B. Huntly;B. Göttgens;M. Bycro

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组蛋白 H3 (H3K36me3) 中 Lys36 的三甲基化协调与转录延伸期相关的事件，并且也正在成为细胞生长和分化的重要表观遗传调节因子。我们已将溴和植物同源结构域 (PHD) 指状蛋白 1 (BRPF1) 的 PWWP 结构域鉴定为 H3K36me3 结合模块，并确定了该结构域与 H3K36me3 衍生肽复合物的结构。
Trimethylation of Lys36 in histone H3 (H3K36me3) coordinates events associated with the elongation phase of transcription and is also emerging as an important epigenetic regulator of cell growth and differentiation. We have identified the PWWP domain of bromo and plant homeodomain (PHD) finger–containing protein 1 (BRPF1) as a H3K36me3 binding module and have determined the structure of this domain in complex with an H3K36me3-derived peptide.