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DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition

Author

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  • Simon J. Elsässer

    (Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University
    MRC Laboratory of Molecular Biology)

  • Hongda Huang

    (Structural Biology Program, Memorial Sloan-Kettering Cancer Center)

  • Peter W. Lewis

    (Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University)

  • Jason W. Chin

    (MRC Laboratory of Molecular Biology)

  • C. David Allis

    (Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University)

  • Dinshaw J. Patel

    (Structural Biology Program, Memorial Sloan-Kettering Cancer Center)

Abstract

Histone chaperones represent a structurally and functionally diverse family of histone-binding proteins that prevent promiscuous interactions of histones before their assembly into chromatin. DAXX is a metazoan histone chaperone specific to the evolutionarily conserved histone variant H3.3. Here we report the crystal structures of the DAXX histone-binding domain with a histone H3.3–H4 dimer, including mutants within DAXX and H3.3, together with in vitro and in vivo functional studies that elucidate the principles underlying H3.3 recognition specificity. Occupying 40% of the histone surface-accessible area, DAXX wraps around the H3.3–H4 dimer, with complex formation accompanied by structural transitions in the H3.3–H4 histone fold. DAXX uses an extended α-helical conformation to compete with major inter-histone, DNA and ASF1 interaction sites. Our structural studies identify recognition elements that read out H3.3-specific residues, and functional studies address the contributions of Gly 90 in H3.3 and Glu 225 in DAXX to chaperone-mediated H3.3 variant recognition specificity.

Suggested Citation

  • Simon J. Elsässer & Hongda Huang & Peter W. Lewis & Jason W. Chin & C. David Allis & Dinshaw J. Patel, 2012. "DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition," Nature, Nature, vol. 491(7425), pages 560-565, November.
    • Handle: RePEc:nat:nature:v:491:y:2012:i:7425:d:10.1038_nature11608
    DOI: 10.1038/nature11608
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    Cited by:

    1. Iqbal Mahmud & Guimei Tian & Jia Wang & Tarun E. Hutchinson & Brandon J. Kim & Nikee Awasthee & Seth Hale & Chengcheng Meng & Allison Moore & Liming Zhao & Jessica E. Lewis & Aaron Waddell & Shangtao , 2023. "DAXX drives de novo lipogenesis and contributes to tumorigenesis," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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