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The Taf14 YEATS domain is a reader of histone crotonylation.

Nature chemical biology (2016-04-19)
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
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Glutathione-S-Transferase (GST) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
Sigma-Aldrich
Anti-acetyl-Histone H3 (Lys9) Antibody, serum, Upstate®