Fiche publication
Date publication
février 2024
Journal
Cells
Auteurs
Membres identifiés du Cancéropôle Est :
Dr BRONNER Christian
,
Dr HAMICHE Ali
Tous les auteurs :
Ignatyeva M, Patel AKM, Ibrahim A, Albiheyri RS, Zari AT, Bahieldin A, Bronner C, Sabir JSM, Hamiche A
Lien Pubmed
Résumé
HIRIP3 is a mammalian protein homologous to the yeast H2A.Z deposition chaperone Chz1. However, the structural basis underlying Chz's binding preference for H2A.Z over H2A, as well as the mechanism through which Chz1 modulates histone deposition or replacement, remains enigmatic. In this study, we aimed to characterize the function of HIRIP3 and to identify its interacting partners in HeLa cells. Our findings reveal that HIRIP3 is specifically associated in vivo with H2A-H2B dimers and CK2 kinase. While bacterially expressed HIRIP3 exhibited a similar binding affinity towards H2A and H2A.Z, the associated CK2 kinase showed a notable preference for H2A phosphorylation at serine 1. The recombinant HIRIP3 physically interacted with the H2A αC helix through an extended CHZ domain and played a crucial role in depositing the canonical core histones onto naked DNA. Our results demonstrate that mammalian HIRIP3 acts as an H2A histone chaperone, assisting in its selective phosphorylation by Ck2 kinase at serine 1 and facilitating its deposition onto chromatin.
Mots clés
CK2 kinase, H2A, HIRIP3, histone chaperone
Référence
Cells. 2024 02 1;13(3):
