Document Detail

Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.
MedLine Citation:
PMID:  23142979     Owner:  NLM     Status:  MEDLINE    
Mammalian histone H3.3 is a variant of the canonical H3.1 essential for genome reprogramming in fertilized eggs and maintenance of chromatin structure in neuronal cells. An H3.3-specific histone chaperone, DAXX, directs the deposition of H3.3 onto pericentric and telomeric heterochromatin. H3.3 differs from H3.1 by only five amino acids, yet DAXX can distinguish the two with high precision. By a combination of structural, biochemical and cell-based targeting analyses, we show that Ala87 and Gly90 are the principal determinants of human H3.3 specificity. DAXX uses a shallow hydrophobic pocket to accommodate the small hydrophobic Ala87 of H3.3, whereas a polar binding environment in DAXX prefers Gly90 in H3.3 over the hydrophobic Met90 in H3.1. An H3.3-H4 heterodimer is bound by the histone-binding domain of DAXX, which makes extensive contacts with both H3.3 and H4.
Chao-Pei Liu; Chaoyang Xiong; Mingzhu Wang; Zhouliang Yu; Na Yang; Ping Chen; Zhiguo Zhang; Guohong Li; Rui-Ming Xu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-11-11
Journal Detail:
Title:  Nature structural & molecular biology     Volume:  19     ISSN:  1545-9985     ISO Abbreviation:  Nat. Struct. Mol. Biol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-05     Completed Date:  2013-02-04     Revised Date:  2014-03-19    
Medline Journal Info:
Nlm Unique ID:  101186374     Medline TA:  Nat Struct Mol Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1287-92     Citation Subset:  IM    
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MeSH Terms
Adaptor Proteins, Signal Transducing / chemistry*
Histones / chemistry*
Models, Molecular
Molecular Chaperones / chemistry*
Nuclear Proteins / chemistry*
Grant Support
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/DAXX protein, human; 0/Histones; 0/Molecular Chaperones; 0/Nuclear Proteins

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