The Tudor Domain of the PHD Finger Protein 1 Is a Dual Reader of Lysine Trimethylation at Lysine 36 of Histone H3 and Lysine 27 of Histone Variant H3t
The Tudor Domain of the PHD Finger Protein 1 Is a Dual Reader of Lysine Trimethylation at Lysine 36 of Histone H3 and Lysine 27 of Histone Variant H3t
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DOI：
10.1016/j.jmb.2013.08.009
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发表时间：
2014-04-17
影响因子：
5.6
通讯作者：
Jeltsch, Albert
中科院分区：
文献类型：
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作者：
Kycia, Ina;Kudithipudi, Srikanth;Jeltsch, Albert
PHF1与Polycomb抑制复合体2结合，并被证明能刺激其h3k27 -三甲基化活性。我们研究了PHF1 Tudor结构域与修饰组蛋白肽的相互作用，发现它识别H3K36me3和H3tK27me3（在组蛋白变体H3t上），并且它使用相同的三甲基赖氨酸结合口袋与这两种肽相互作用。由于两种肽序列非常不同，这一结果表明阅读结构域可能具有双重特异性。全长PHF1在人HEK293细胞中的亚核定位研究表明，它与K27me3共定位，而不与K36me3共定位，这种共定位依赖于三甲基赖氨酸结合袋，表明。K27me3是PHF1 Tudor结构域的体内靶点。我们的数据表明，PHF1与人类染色质中的H3tK27me3结合，H3t在Polycomb调控中具有更普遍的作用。(C) 2013 Elsevier Ltd.版权所有。
PHF1 associates with the Polycomb repressive complex 2 and it was demonstrated to stimulate its H3K27-trimethylation activity. We studied the interaction of the PHF1 Tudor domain with modified histone peptides and found that it recognizes H3K36me3 and H3tK27me3 (on the histone variant H3t) and that it uses the same trimethyllysine binding pocket for the interaction with both peptides. Since both peptide sequences are very different, this result indicates that reading domains can have dual specificities. Sub-nuclear localization studies of full-length PHF1 in human HEK293 cells revealed that it co-localizes with K27me3, but not with K36me3, and that this co-localization depends on the trimethyllysine binding pocket indicating that. K27me3 is an in vivo target for the PHF1 Tudor domain. Our data suggest that PHF1 binds to H3tK27me3 in human chromatin, and H3t has a more general role in Polycomb regulation. (C) 2013 Elsevier Ltd. All rights reserved.