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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Acknowledgements
We thank L. Aponte-Collazo for help with experiments and M. Bedford, K. Chua, D. Stillman, and J. Tyler for kindly providing some original DNA constructs of YEATS and bromodomains, as well as the yeast strains and extracts. This work was supported by NIH grants R01 GM106416 and GM100907 to T.G.K. and GM110058 to B.D.S. and by CPRIT RP160237 to X.S. F.H.A. is supported by the NIH grant T32AA007464, E.K.S. is supported by the NIH grant K12-GM000678, S.A.S. is supported by a UNC Lineberger Cancer Center Postdoctoral Fellowship Award, and A.G. is supported by the CPRIT Research Training grant RP140106.
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F.H.A., S.A.S., E.K.S., J.B.B., A.G., I.K.T., and K.K. performed experiments and, together with X.S., B.D.S., and T.G.K., analyzed the data. F.H.A., S.A.S., B.D.S., and T.G.K. wrote the manuscript with input from all authors.
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Andrews, F., Shinsky, S., Shanle, E. et al. The Taf14 YEATS domain is a reader of histone crotonylation. Nat Chem Biol 12, 396–398 (2016). https://doi.org/10.1038/nchembio.2065
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DOI: https://doi.org/10.1038/nchembio.2065
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