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Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
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Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
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Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
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Journal Article
Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
2010
Overview
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 α-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 ATRX–Daxx complex is bound to telomeric chromatin, and that both components of this complex are required for H3.3 deposition at telomeres in murine embryonic stem cells (ESCs). These data demonstrate that Daxx functions as an H3.3-specific chaperone and facilitates the deposition of H3.3 at heterochromatin loci in the context of the ATRX–Daxx complex.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Animals
/ Carrier Proteins - metabolism
/ Carrier Proteins - physiology
/ Cells
/ Chromatin Assembly and Disassembly
/ DNA
/ Histone Chaperones - metabolism
/ Histones
/ Intracellular Signaling Peptides and Proteins - metabolism
/ Intracellular Signaling Peptides and Proteins - physiology
/ loci
/ Metazoa
/ Mice
/ Nuclear Proteins - metabolism
/ Nuclear Proteins - physiology
/ Proteins
/ Telomere
