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Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibility

Author

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  • Catherine A. Musselman

    (University of Colorado School of Medicine
    Present address: Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242, USA)

  • Matthew D. Gibson

    (Ohio State University)

  • Erik W. Hartwick

    (Program in Structural Biology and Biochemistry, University of Colorado School of Medicine)

  • Justin A. North

    (Ohio State University)

  • Jovylyn Gatchalian

    (University of Colorado School of Medicine)

  • Michael G. Poirier

    (Ohio State University)

  • Tatiana G. Kutateladze

    (University of Colorado School of Medicine
    Program in Structural Biology and Biochemistry, University of Colorado School of Medicine)

Abstract

The Tudor domain of human PHF1 recognizes trimethylated lysine 36 of histone H3 (H3K36me3). This interaction modulates the methyltransferase activity of the PRC2 complex and has a role in retention of PHF1 at DNA damage sites. We have previously determined the structural basis for the association of Tudor with a methylated histone peptide. Here we detail the molecular mechanism of binding of the Tudor domain to the H3KC36me3-nucleosome core particle (H3KC36me3-NCP). Using a combination of TROSY NMR and FRET, we show that Tudor concomitantly interacts with H3K36me3 and DNA. Binding of the PHF1 Tudor domain to the H3KC36me3-NCP stabilizes the nucleosome in a conformation in which the nucleosomal DNA is more accessible to DNA-binding regulatory proteins. Our data provide a mechanistic explanation for the consequence of reading of the active mark H3K36me3 by the PHF1 Tudor domain.

Suggested Citation

  • Catherine A. Musselman & Matthew D. Gibson & Erik W. Hartwick & Justin A. North & Jovylyn Gatchalian & Michael G. Poirier & Tatiana G. Kutateladze, 2013. "Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibility," Nature Communications, Nature, vol. 4(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3969
    DOI: 10.1038/ncomms3969
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    Cited by:

    1. Dustin C. Becht & Brianna J. Klein & Akinori Kanai & Suk Min Jang & Khan L. Cox & Bing-Rui Zhou & Sabrina K. Phanor & Yi Zhang & Ruo-Wen Chen & Christopher C. Ebmeier & Catherine Lachance & Maxime Gal, 2023. "MORF and MOZ acetyltransferases target unmethylated CpG islands through the winged helix domain," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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