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

Dominique Ray-Gallet, M. Daniel Ricketts, Yukari Sato, Kushol Gupta, Ekaterina Boyarchuk, Toshiya Senda, Ronen Marmorstein and Geneviève Almouzni ()
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Dominique Ray-Gallet: Equipe Labellisée Ligue contre le Cancer
M. Daniel Ricketts: Perelman School of Medicine at the University of Pennsylvania
Yukari Sato: High Energy Accelerator Research Organization (KEK), 1-1 Oho
Kushol Gupta: Perelman School of Medicine at the University of Pennsylvania
Ekaterina Boyarchuk: Equipe Labellisée Ligue contre le Cancer
Toshiya Senda: High Energy Accelerator Research Organization (KEK), 1-1 Oho
Ronen Marmorstein: Perelman School of Medicine at the University of Pennsylvania
Geneviève Almouzni: Equipe Labellisée Ligue contre le Cancer

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-05581-y

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