Insights into newly discovered marks and readers of epigenetic information
August 18th, 2016 by Forest H Andrews
Nature Chemical Biology 12, 662 (2016). doi:10.1038/nchembio.2149
Authors: Forest H Andrews, Brian D Strahl & Tatiana G Kutateladze
The Taf14 YEATS domain is a reader of histone crotonylation
April 18th, 2016 by Forest H Andrews
Nature Chemical Biology 12, 396 (2016). doi:10.1038/nchembio.2065
Authors: 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
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.