4.5 Article

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

Journal

NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 17, Issue 5, Pages 617-619

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1797

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Funding

  1. Leukaemia Research Fund
  2. Medical Research Council
  3. Cancer Research UK
  4. Leukemia & Lymphoma Society of America
  5. European Molecular Biology Organization Fellowship [ALTF 562-2002]
  6. MRC [MC_U105459896, G0800784, G116/187] Funding Source: UKRI
  7. Medical Research Council [G0800784B, G116/187, G0800784, MC_U105459896] Funding Source: researchfish
  8. National Centre for the Replacement, Refinement and Reduction of Animals in Research (NC3Rs) [G0900729/1] Funding Source: researchfish

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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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