Preparing your results

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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

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


  • Elsässer SJ
  • Huang H
  • Lewis PW
  • Chin JW
  • Allis CD
  • Patel DJ



Publication Data

November 22, 2012

Associated Grants

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

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