Journal
NATURE CHEMICAL BIOLOGY
Volume 12, Issue 6, Pages 396-U33Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.2065
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Funding
- NIH [R01 GM106416, GM100907, GM110058, T32AA007464, K12-GM000678]
- CPRIT [RP160237]
- UNC Lineberger Cancer Center Postdoctoral Fellowship Award
- CPRIT Research Training grant [RP140106]
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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 pi-pi-pi-stacking mechanism and that other YEATS domains have crotonyllysine-binding activity.
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