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Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
Open accessAbstract
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.
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Cited by
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Schwartzentruber, J., Korshunov, A., Liu, X.-Y., Jones, D. T. W., Pfaff, E., Jacob, K., Sturm, D., Fontebasso, A. M., Quang, D.-A. K., Tönjes, M., et al. (2012) · Nature · doi:10.1038/nature10833 · Cited by 2,631
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes
Clapier, C. R., Iwasa, J., Cairns, B. R., & Peterson, C. L. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.26 · Cited by 1,305
Altered Telomeres in Tumors with ATRX and DAXX Mutations
Heaphy, C. M., de Wilde, R. F., Jiao, Y., Klein, A. P., Edil, B. H., Shi, C., Bettegowda, C., Rodriguez, F. J., Eberhart, C. G., Hebbar, S., et al. (2011) · Science · doi:10.1126/science.1207313 · Cited by 1,083
Khuong-Quang, D.-A., Buczkowicz, P., Rakopoulos, P., Liu, X.-Y., Fontebasso, A. M., Bouffet, E., Bartels, U., Albrecht, S., Schwartzentruber, J., Letourneau, L., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0998-0 · Cited by 1,028
Metadata
- Authors
- Lewis, P. W., Elsaesser, S. J., Noh, K.-M., Stadler, S. C., & Allis, C. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-07-22
- Volume
- 107
- Issue
- 32
- Pages
- 14075-14080
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1966218941
- Cited by
- 821
- References
- 0
- FWCI
- 20.91
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. https://app.cochat.ai/papers/10.1073/pnas.1008850107
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- Lewis, P. W., Elsaesser, S. J., Noh, K.-M., Stadler, S. C., & Allis, C. D. (2010). Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1008850107
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