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Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex

Author

Listed:
  • M Daniel Ricketts

    (Perelman School of Medicine, University of Pennsylvania
    Graduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania)

  • Brian Frederick

    (The Wistar Institute)

  • Henry Hoff

    (The Wistar Institute)

  • Yong Tang

    (The Wistar Institute)

  • David C. Schultz

    (The Wistar Institute)

  • Taranjit Singh Rai

    (Institute of Cancer Sciences, CR-UK Beatson Labs, University of Glasgow
    Institute of Biomedical and Environmental Health Research, University of West of Scotland)

  • Maria Grazia Vizioli

    (Institute of Cancer Sciences, CR-UK Beatson Labs, University of Glasgow)

  • Peter D. Adams

    (Institute of Cancer Sciences, CR-UK Beatson Labs, University of Glasgow)

  • Ronen Marmorstein

    (Perelman School of Medicine, University of Pennsylvania
    Graduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania
    Abramson Family Cancer Research Institute, University of Pennsylvania)

Abstract

Histone chaperones bind specific histones to mediate their storage, eviction or deposition from/or into chromatin. The HIRA histone chaperone complex, composed of HIRA, ubinuclein-1 (UBN1) and CABIN1, cooperates with the histone chaperone ASF1a to mediate H3.3-specific binding and chromatin deposition. Here we demonstrate that the conserved UBN1 Hpc2-related domain (HRD) is a novel H3.3-specific-binding domain. Biochemical and biophysical studies show the UBN1-HRD preferentially binds H3.3/H4 over H3.1/H4. X-ray crystallographic and mutational studies reveal that conserved residues within the UBN1-HRD and H3.3 G90 as key determinants of UBN1–H3.3-binding specificity. Comparison of the structure with the unrelated H3.3-specific chaperone DAXX reveals nearly identical points of contact between the chaperone and histone in the proximity of H3.3 G90, although the mechanism for H3.3 G90 recognition appears to be distinct. This study points to UBN1 as the determinant of H3.3-specific binding and deposition by the HIRA complex.

Suggested Citation

  • M Daniel Ricketts & Brian Frederick & Henry Hoff & Yong Tang & David C. Schultz & Taranjit Singh Rai & Maria Grazia Vizioli & Peter D. Adams & Ronen Marmorstein, 2015. "Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex," Nature Communications, Nature, vol. 6(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8711
    DOI: 10.1038/ncomms8711
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