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

Simon J. Elsässer, Hongda Huang, Peter W. Lewis, Jason W. Chin, C. David Allis () and Dinshaw J. Patel ()
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Simon J. Elsässer: Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University
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

Nature, 2012, vol. 491, issue 7425, 560-565

Abstract: 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.

Date: 2012
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DOI: 10.1038/nature11608

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