The Taf14 YEATS domain is a reader of histone crotonylation

Forest H Andrews,Stephen A Shinsky,Erin K Shanle,Joseph B Bridgers,Anneliese Gest,Ian K Tsun,Krzysztof Krajewski,Xiaobing Shi,Brian D Strahl,Tatiana G Kutateladze

NATURE CHEMICAL BIOLOGY（2016）

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摘要

Crotonylated lysine residues within histones are linked to transcriptional activation in a process involving histone mark ‘reader’ proteins. Crystallographic analysis of the YEATS domain of the Taf14 protein reveals a mode of crotonylated histone mark recognition via a π-sandwich motif.

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关键词

NMR spectroscopy,Histone post-translational modifications,X-ray crystallography,Post-translational modifications

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