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Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1

Nature Structural & Molecular Biology volume 17, pages 617–619 (2010)Cite this article

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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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Figure 1: Interactions of the PWWP domain of BRPF1 with an H3K36me3 peptide.
Figure 2: Localization of H3K36me3 and Brpf1 on Hox genes.
Figure 3: Structure of the BRPF1 PWWP domain in complex with an H3K36me3 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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Authors and Affiliations

  1. MRC Centre for Protein Engineering, Cambridge, UK

    Alessandro Vezzoli, Mark D Allen, Clara M Santiveri & Mark Bycroft

  2. Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK

    Nicolas Bonadies, Brynn T Kvinlaug, Brian J P Huntly & Berthold Göttgens

  3. Medical Research Council Laboratory of Molecular Biology, Cambridge, UK

    Stefan M V Freund

Authors
  1. Alessandro Vezzoli
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  2. Nicolas Bonadies
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  3. Mark D Allen
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  4. Stefan M V Freund
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  5. Clara M Santiveri
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  6. Brynn T Kvinlaug
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  7. Brian J P Huntly
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  8. Berthold Göttgens
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  9. Mark Bycroft
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Contributions

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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Correspondence to Mark Bycroft.

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The authors declare no competing financial interests.

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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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