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            <title xml:lang="en">Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit</title>
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                <title xml:lang="en">Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit</title>
                <title xml:lang="fr">L'activité fonctionnelle du complexe d'histone chaperon H3.3 HIRA nécessite la trimérisation de la sous-unité HIRA</title>
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                    <forename type="first">Dominique</forename>
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                <term xml:lang="en">Nucleosomes</term>
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              <p>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.</p>
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              <p>Le complexe d'histones chaperon HIRA dépose le variant d'histone H3.3 sur la chromatine de manière indépendante de la synthèse d'ADN. Il comprend trois sous-unités identifiées, HIRA, UBN1 et CABIN1, mais l'état d'oligomérisation fonctionnelle du complexe n'a pas été étudié. Nous utilisons ici l'analyse biochimique et cristallographique pour montrer que la sous-unité HIRA forme un homotrimère stable qui lie deux sous-unités de CABIN1 in vitro. Un mutant ARHI qui est défectueux dans la formation de l'homotrimère interagit moins efficacement avec CABIN1, n'est pas enrichi sur les sites d'endommagement de l'ADN lors de l'irradiation UV et ne peut pas sauver un nouveau dépôt de H3.3 dans les cellules knock-out ARHI. L'homologie structurelle avec le composant réplisomique homotrimérique Ctf4/ AND-1 permet d'établir des parallèles et de discuter de l'importance fonctionnelle de l'état d'homotrimérisation de la sous-unité HIRA.</p>
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