The Taf14 YEATS domain is a reader of histone crotonylation
FH Andrews, SA Shinsky, EK Shanle… - Nature chemical …, 2016 - nature.com
Nature chemical biology, 2016•nature.com
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.
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.
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.
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