Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response.
Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response.
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DOI：
10.1101/gad.269977.115
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发表时间：
2015-09-01
影响因子：
10.5
通讯作者：
Strahl BD
中科院分区：
文献类型：
--
作者：
Shanle EK;Andrews FH;Meriesh H;McDaniel SL;Dronamraju R;DiFiore JV;Jha D;Wozniak GG;Bridgers JB;Kerschner JL;Krajewski K;Martín GM;Morrison AJ;Kutateladze TG;Strahl BD
Shanle等人表明Taf14的YEATS结构域是组蛋白H3 Lys9乙酰化（H3K9ac）的选择性阅读器。乙酰化的Lys9被夹在由F62和W81形成的芳香笼中。细胞中这种结合的破坏会损害基因转录和DNA损伤反应。在许多染色质相关蛋白中发现的YEATS结构域最近被证明具有结合组蛋白赖氨酸乙酰化的能力。在这里，我们表明，YEATS结构域的Taf14，在酵母中的关键转录和染色质修饰复合物的成员，是一个选择性的组蛋白H3赖氨酸9乙酰化（H3K9ac）的读者。结构分析表明，乙酰化的赖氨酸9被夹在由F62和W81形成的芳香笼中。细胞中这种结合的破坏会损害基因转录和DNA损伤反应。我们的研究结果为YEATS结构域蛋白家族建立了一个高度保守的乙酰赖氨酸阅读器功能，并强调了这种相互作用对Taf14的重要性。
Shanle et al. show that the YEATS domain of Taf14 is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcription and the DNA damage response. The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Structural analysis reveals that acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcription and the DNA damage response. Our findings establish a highly conserved acetyllysine reader function for the YEATS domain protein family and highlight the significance of this interaction for Taf14.