1. The Taf14 YEATS domain is a reader of histone crotonylation
- Author
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Ian K. Tsun, Xiaobing Shi, Forest H. Andrews, Erin K. Shanle, Brian D. Strahl, Krzysztof Krajewski, Stephen A. Shinsky, Joseph B. Bridgers, Tatiana G. Kutateladze, and Anneliese Gest
- Subjects
0301 basic medicine ,Models, Molecular ,Saccharomyces cerevisiae Proteins ,PTM ,Protein domain ,Taf14 ,Computational biology ,histone ,Saccharomyces cerevisiae ,Biology ,Article ,Epigenesis, Genetic ,Histones ,03 medical and health sciences ,Protein Domains ,Transcription (biology) ,Histone code ,Epigenetics ,Molecular Biology ,Molecular Structure ,Lysine ,crotonylated lysine ,YEATS domain ,Cell Biology ,Molecular biology ,030104 developmental biology ,Histone ,Transcription Factor TFIID ,Posttranslational modification ,biology.protein ,chromatin ,Protein Processing, Post-Translational - Abstract
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 π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.
- Published
- 2016