1. The Taf14 YEATS domain is a reader of histone crotonylation.
- Author
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Andrews FH, Shinsky SA, Shanle EK, Bridgers JB, Gest A, Tsun IK, Krajewski K, Shi X, Strahl BD, and Kutateladze TG
- Subjects
- Histones chemistry, Lysine chemistry, Models, Molecular, Molecular Structure, Protein Domains, Epigenesis, Genetic, Histones metabolism, Lysine analogs & derivatives, Lysine metabolism, Protein Processing, Post-Translational, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins chemistry, Saccharomyces cerevisiae Proteins metabolism, Transcription Factor TFIID chemistry, Transcription Factor TFIID metabolism
- 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
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