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Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit

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Listed:
  • Dominique Ray-Gallet

    (Equipe Labellisée Ligue contre le Cancer
    Institut Curie, CNRS, UMR3664)

  • M. Daniel Ricketts

    (Perelman School of Medicine at the University of Pennsylvania)

  • Yukari Sato

    (High Energy Accelerator Research Organization (KEK), 1-1 Oho
    Tohoku University)

  • Kushol Gupta

    (Perelman School of Medicine at the University of Pennsylvania)

  • Ekaterina Boyarchuk

    (Equipe Labellisée Ligue contre le Cancer
    Institut Curie, CNRS, UMR3664)

  • Toshiya Senda

    (High Energy Accelerator Research Organization (KEK), 1-1 Oho
    The Graduate University for Advanced Studies (Soken-dai))

  • Ronen Marmorstein

    (Perelman School of Medicine at the University of Pennsylvania)

  • Geneviève Almouzni

    (Equipe Labellisée Ligue contre le Cancer
    Institut Curie, CNRS, UMR3664)

Abstract

The HIRA histone chaperone complex deposits the histone variant H3.3 onto chromatin in a DNA synthesis-independent manner. It comprises three identified subunits, HIRA, UBN1 and CABIN1, however the functional oligomerization state of the complex has not been investigated. Here we use biochemical and crystallographic analysis to show that the HIRA subunit forms a stable homotrimer that binds two subunits of CABIN1 in vitro. A HIRA mutant that is defective in homotrimer formation interacts less efficiently with CABIN1, is not enriched at DNA damage sites upon UV irradiation and cannot rescue new H3.3 deposition in HIRA knockout cells. The structural homology with the homotrimeric replisome component Ctf4/AND-1 enables the drawing of parallels and discussion of the functional importance of the homotrimerization state of the HIRA subunit.

Suggested Citation

  • Dominique Ray-Gallet & M. Daniel Ricketts & Yukari Sato & Kushol Gupta & Ekaterina Boyarchuk & Toshiya Senda & Ronen Marmorstein & Geneviève Almouzni, 2018. "Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit," Nature Communications, Nature, vol. 9(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05581-y
    DOI: 10.1038/s41467-018-05581-y
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