articleProceedings of the National Academy of SciencesJul 22, 2010Closed access

Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres

Rockefeller University

PubMed
Indexed incrossrefpubmed

Abstract

The histone variant H3.3 is implicated in the formation and maintenance of specialized chromatin structure in metazoan cells. H3.3-containing nucleosomes are assembled in a replication-independent manner by means of dedicated chaperone proteins. We previously identified the death domain associated protein (Daxx) and the alpha-thalassemia X-linked mental retardation protein (ATRX) as H3.3-associated proteins. Here, we report that the highly conserved N terminus of Daxx interacts directly with variant-specific residues in the H3.3 core. Recombinant Daxx assembles H3.3/H4 tetramers on DNA templates, and the ATRX-Daxx complex catalyzes the deposition and remodeling of H3.3-containing nucleosomes. We find that the…

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808
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Authors

5

Topics & keywords

Keywords
  • Death-associated protein 6
  • ATRX
  • Biology
  • Nucleosome
  • Histone
  • Telomere
  • Chromatin
  • Cell biology
UN Sustainable Development Goals
  • Good health and well-being
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