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. 2010 May;17(5):617-9.
doi: 10.1038/nsmb.1797. Epub 2010 Apr 18.

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

Alessandro Vezzoli  1 , Nicolas Bonadies, Mark D Allen, Stefan M V Freund, Clara M Santiveri, Brynn T Kvinlaug, Brian J P Huntly, Berthold Göttgens, Mark Bycroft
Affiliations

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

Alessandro Vezzoli et al. Nat Struct Mol Biol. 2010 May.

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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