GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode,ACS Chemical Biology

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GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode
ACS Chemical Biology ( IF 3.5 ) Pub Date : 2018-08-02 00:00:00 , DOI: 10.1021/acschembio.8b00674
Hyo Je Cho ₁ , Hao Li _{1,

2} , Brian M. Linhares ₁ , EunGi Kim ₁ , Juliano Ndoj ₁ , Hongzhi Miao ₁ , Jolanta Grembecka _{1,

2} , Tomasz Cierpicki _{1,

2}

Affiliation

GAS41 is a chromatin-associated protein that belongs to the YEATS family and is involved in the recognition of acetyl-lysine in histone proteins. A unique feature of GAS41 is the presence of a C-terminal coiled-coil domain, which is responsible for protein dimerization. Here, we characterized the specificity of the GAS41 YEATS domain and found that it preferentially binds to acetylated H3K18 and H3K27 peptides. Interestingly, we found that full-length, dimeric GAS41 binds to diacetylated H3 peptides with an enhanced affinity when compared to those for monoacetylated peptides, through a bivalent binding mode. We determined the crystal structure of the GAS41 YEATS domain with H3K23acK27ac to visualize the molecular basis of diacetylated histone binding. Our results suggest a unique binding mode in which full-length GAS41 is a reader of diacetylated histones.

中文翻译：

GAS41通过二价结合模式识别二乙酰化组蛋白H3

GAS41是一种染色质相关蛋白，属于YEATS家族，参与组蛋白中乙酰赖氨酸的识别。GAS41的独特功能是存在一个C末端卷曲螺旋结构域，该结构域负责蛋白质二聚化。在这里，我们表征了GAS41 YEATS域的特异性，并发现它优先结合乙酰化的H3K18和H3K27肽。有趣的是，我们发现全长二聚体GAS41通过二价结合模式与单乙酰化肽相比，以增强的亲和力与二乙酰化H3肽结合。我们确定了具有H3K23acK27ac的GAS41 YEATS域的晶体结构，以可视化二乙酰化组蛋白结合的分子基础。

更新日期：2018-08-02

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