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DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition
Simon J Elsässer1, Hongda Huang, Peter W Lewis
1Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, New York 10065, USA.
Nature
|October 19, 2012
Summary
DAXX histone chaperone specifically recognizes histone variant H3.3. Structural and functional studies reveal how DAXX binds H3.3-H4 dimers, clarifying H3.3 recognition specificity.
Area of Science:
- Molecular Biology
- Structural Biology
- Epigenetics
Background:
- Histone chaperones are crucial for preventing inappropriate histone interactions during chromatin assembly.
- DAXX is a metazoan histone chaperone that specifically binds the histone variant H3.3.
- Understanding H3.3 recognition is key to elucidating chromatin dynamics.
Purpose of the Study:
- To determine the structural basis of histone H3.3 recognition by the DAXX chaperone.
- To elucidate the molecular mechanisms underlying DAXX-H3.3 specificity.
- To investigate the functional implications of DAXX-H3.3 interactions in vitro and in vivo.
Main Methods:
- X-ray crystallography of DAXX histone-binding domain complexed with H3.3-H4 dimer and mutants.
- In vitro binding assays.
- In vivo functional studies.
Main Results:
- DAXX wraps around the H3.3-H4 dimer, inducing structural changes in the histone fold.
- DAXX utilizes an extended alpha-helical conformation to disrupt key interaction sites.
- Specific residues in H3.3 (Gly90) and DAXX (Glu225) were identified as critical for recognition specificity.
Conclusions:
- The study provides atomic-level insights into H3.3 variant recognition by DAXX.
- DAXX acts as a specialized chaperone, preventing promiscuous H3.3 interactions.
- These findings advance our understanding of histone variant deposition and chromatin regulation.
