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XB-ART-53300
Nat Commun July 10, 2015; 6 7711.
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Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex.

Ricketts MD , Frederick B , Hoff H , Tang Y , Schultz DC , Singh Rai T , Grazia Vizioli M , Adams PD , Marmorstein R .


Abstract
Histone chaperones bind specific histones to mediate their storage, eviction or deposition from/or into chromatin. The HIRA histone chaperone complex, composed of HIRA, ubinuclein-1 (UBN1) and CABIN1, cooperates with the histone chaperone ASF1a to mediate H3.3-specific binding and chromatin deposition. Here we demonstrate that the conserved UBN1 Hpc2-related domain (HRD) is a novel H3.3-specific-binding domain. Biochemical and biophysical studies show the UBN1-HRD preferentially binds H3.3/H4 over H3.1/H4. X-ray crystallographic and mutational studies reveal that conserved residues within the UBN1-HRD and H3.3 G90 as key determinants of UBN1-H3.3-binding specificity. Comparison of the structure with the unrelated H3.3-specific chaperone DAXX reveals nearly identical points of contact between the chaperone and histone in the proximity of H3.3 G90, although the mechanism for H3.3 G90 recognition appears to be distinct. This study points to UBN1 as the determinant of H3.3-specific binding and deposition by the HIRA complex.

PubMed ID: 26159857
PMC ID: PMC4510971
Article link: Nat Commun
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: asf1a cabin1 daxx hira ubn1


Article Images: [+] show captions
References [+] :
Adam, Transcription recovery after DNA damage requires chromatin priming by the H3.3 histone chaperone HIRA. 2013, Pubmed