期刊
NATURE
卷 491, 期 7425, 页码 560-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature11608
关键词
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资金
- Center for Synchrotron Biosciences from the National Institute of Biomedical Imaging and Bioengineering (NIBIB) [P30-EB-009998]
- National Center for Research Resources of the NIH [1S10RR022321-01, 1S10RR027037-01]
- Abby Rockefeller Mauze Trust
- Maloris Foundation
- STARR Foundation
- Rockefeller University
- UK Medical Research Council (MRC) [U105181009, UD99999908]
- Boehringer Ingelheim Funds fellowship
- David Rockefeller Graduate Program
- MRC [MC_U105181009] Funding Source: UKRI
- Medical Research Council [MC_U105181009] Funding Source: researchfish
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 a-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.
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