The Taf14 YEATS domain is a reader of histone crotonylation

• Published in: Nature chemical biology Vol. 12; no. 6; pp. 396 - 398
• Main Authors: Andrews, Forest H, Shinsky, Stephen A, Shanle, Erin K, Bridgers, Joseph B, Gest, Anneliese, Tsun, Ian K, Krajewski, Krzysztof, Shi, Xiaobing, Strahl, Brian D, Kutateladze, Tatiana G
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.06.2016; Nature Publishing Group
• Subjects: 631/535/1266; 631/535/878; 631/92/458; 631/92/612/100/2285; Biochemical Engineering; Biochemistry; Bioorganic Chemistry; brief-communication; Cell Biology; Chemistry; Chemistry/Food Science; Crystallography; Epigenesis, Genetic; Epigenetics; Histones - chemistry; Histones - metabolism; Lysine - analogs & derivatives; Lysine - chemistry; Lysine - metabolism; Models, Molecular; Molecular Structure; Protein Domains; Protein Processing, Post-Translational; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Spectrum analysis; Transcription Factor TFIID - chemistry; Transcription Factor TFIID - metabolism; Transcription factors
• ISSN: 1552-4450; 1552-4469; 1552-4469
• DOI: 10.1038/nchembio.2065

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. 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.