The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3

The histone variant H3.3 marks active chromatin by replacing the conventional histone H3.1. In this study, we investigate the detailed mechanism of H3.3 replication-independent deposition. We found that the death domain-associated protein DAXX and the chromatin remodeling factor ATRX (alpha-thalassemia/mental retardation syndrome protein) are specifically associated with the H3.3 deposition machinery. Bacterially expressed DAXX has a marked binding preference for H3.3 and assists the deposition of (H3.3-H4)(2) tetramers on naked DNA, thus showing that DAXX is a H3.3 histone chaperone. In DAXX-depleted cells, a fraction of H3.3 was found associated with the replication-dependent machinery of deposition,…

• AP
  Association pour la Recherche sur le Cancer
• AN
  Agence Nationale de la Recherche
• IN
  Institut National de la Santé et de la Recherche Médicale
• LC
  Ligue Contre le Cancer
• CN
  Centre National de la Recherche Scientifique
• IN
  Institut National Du Cancer