Abstract
Trimethylation of Lys36 in histone H3 (H3K36me3) coordinates events associated with the elongation phase of transcription and is also emerging as an important epigenetic regulator of cell growth and differentiation. We have identified the PWWP domain of bromo and plant homeodomain (PHD) finger–containing protein 1 (BRPF1) as a H3K36me3 binding module and have determined the structure of this domain in complex with an H3K36me3-derived peptide.
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Acknowledgements
The Göttgens laboratory is funded by the Leukaemia Research Fund, the Medical Research Council, Cancer Research UK and the Leukemia & Lymphoma Society of America. C.M.S. was the recipient of a European Molecular Biology Organization Fellowship (ALTF 562-2002).
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A.V. and M.D.A. performed the X-ray crystallography studies; A.V., M.D.A., S.M.V.F. and C.M.S. performed the NMR studies; A.V., N.B., B.K. and B.J.P.H. performed the ChIP analysis; M.B. and B.G. supervised the structural and functional aspects of the project, respectively; all authors discussed the results and commented on the manuscript.
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Supplementary Figures 1–6, Supplementary Table 1 and Supplementary Methods (PDF 2545 kb)
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Vezzoli, A., Bonadies, N., Allen, M. et al. Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1. Nat Struct Mol Biol 17, 617–619 (2010). https://doi.org/10.1038/nsmb.1797
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DOI: https://doi.org/10.1038/nsmb.1797
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