The Taf14 YEATS domain is a reader of histone crotonylation

被引：190

作者：

Andrews, Forest H. ^{[1
]}

Shinsky, Stephen A. ^{[2
]}

Shanle, Erin K. ^{[2
]}

Bridgers, Joseph B. ^{[2
]}

Gest, Anneliese ^{[3
]}

Tsun, Ian K. ^{[2
]}

Krajewski, Krzysztof ^{[2
]}

Shi, Xiaobing ^{[3
]}

Strahl, Brian D. ^{[2
]}

Kutateladze, Tatiana G. ^{[1
]}

机构：

[1] Univ Colorado, Sch Med, Dept Pharmacol, Aurora, CO USA

[2] Univ N Carolina, Sch Med, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA

[3] Univ Texas MD Anderson Canc Ctr, Dept Epigenet & Mol Carcinogenesis, Houston, TX 77030 USA

来源：

NATURE CHEMICAL BIOLOGY | 2016年 / 12卷 / 06期

关键词：

TRANSCRIPTION; COMPLEX; ASSOCIATION; INTERACTS; PROTEINS; BINDING; DIRECTS; INO80; LINKS;

D O I：

10.1038/nchembio.2065

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The discovery of new histone modifications is unfolding at startling rates; however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation, an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique pi-pi-pi-stacking mechanism and that other YEATS domains have crotonyllysine-binding activity.

引用

页码：396 / U33

页数：4

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