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

Nature | Nov 22, 2012

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.

Pubmed ID: 23075851 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Amino Acid Sequence | Binding, Competitive | Cell Cycle Proteins | Crystallography, X-Ray | DNA | Histone Chaperones | Histones | Humans | Models, Molecular | Molecular Sequence Data | Nuclear Proteins | Nucleosomes | Protein Conformation | Protein Multimerization | Substrate Specificity | Water

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Associated grants

  • Agency: Medical Research Council, Id: MC_U105181009
  • Agency: PHS HHS, Id: U105181009
  • Agency: Medical Research Council, Id: P30 CA008748
  • Agency: NCI NIH HHS, Id: UD99999908
  • Agency: PHS HHS, Id: S10 RR027037
  • Agency: NCRR NIH HHS, Id: S10 RR022321
  • Agency: NCRR NIH HHS, Id: 1S10RR027037-01
  • Agency: NCRR NIH HHS, Id: P30 EB009998
  • Agency: NIBIB NIH HHS, Id: 1S10RR022321-01
  • Agency: NCRR NIH HHS, Id: P30-EB-009998
  • Agency: NIBIB NIH HHS, Id:

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