Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex

M Daniel Ricketts, Brian Frederick, Henry Hoff, Yong Tang, David C. Schultz, Taranjit Singh Rai, Maria Grazia Vizioli, Peter D. Adams and Ronen Marmorstein ()
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M Daniel Ricketts: Perelman School of Medicine, University of Pennsylvania
Brian Frederick: The Wistar Institute
Henry Hoff: The Wistar Institute
Yong Tang: The Wistar Institute
David C. Schultz: The Wistar Institute
Taranjit Singh Rai: Institute of Cancer Sciences, CR-UK Beatson Labs, University of Glasgow
Maria Grazia Vizioli: Institute of Cancer Sciences, CR-UK Beatson Labs, University of Glasgow
Peter D. Adams: Institute of Cancer Sciences, CR-UK Beatson Labs, University of Glasgow
Ronen Marmorstein: Perelman School of Medicine, University of Pennsylvania

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8711

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