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, Ronen Marmorstein

Research output: Contribution to journalArticle

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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.

Original languageEnglish
Pages (from-to)7711
JournalNature Communications
Volume6
DOIs
Publication statusPublished - 2015

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Histone Chaperones
Histones
chromatin
determinants
Chromatin
proximity
X-Rays
X rays
x rays

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Daniel Ricketts, M., Frederick, B., Hoff, H., Tang, Y., Schultz, D. C., Singh Rai, T., ... Marmorstein, R. (2015). Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex. Nature Communications, 6, 7711. https://doi.org/10.1038/ncomms8711
Daniel Ricketts, M ; Frederick, Brian ; Hoff, Henry ; Tang, Yong ; Schultz, David C ; Singh Rai, Taranjit ; Grazia Vizioli, Maria ; Adams, Peter D ; Marmorstein, Ronen. / Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex. In: Nature Communications. 2015 ; Vol. 6. pp. 7711.
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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.",
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Daniel Ricketts, M, Frederick, B, Hoff, H, Tang, Y, Schultz, DC, Singh Rai, T, Grazia Vizioli, M, Adams, PD & Marmorstein, R 2015, 'Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex', Nature Communications, vol. 6, pp. 7711. https://doi.org/10.1038/ncomms8711

Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex. / Daniel Ricketts, M; Frederick, Brian; Hoff, Henry; Tang, Yong; Schultz, David C; Singh Rai, Taranjit; Grazia Vizioli, Maria; Adams, Peter D; Marmorstein, Ronen.

In: Nature Communications, Vol. 6, 2015, p. 7711.

Research output: Contribution to journalArticle

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AU - Daniel Ricketts, M

AU - Frederick, Brian

AU - Hoff, Henry

AU - Tang, Yong

AU - Schultz, David C

AU - Singh Rai, Taranjit

AU - Grazia Vizioli, Maria

AU - Adams, Peter D

AU - Marmorstein, Ronen

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AB - 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.

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Daniel Ricketts M, Frederick B, Hoff H, Tang Y, Schultz DC, Singh Rai T et al. Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex. Nature Communications. 2015;6:7711. https://doi.org/10.1038/ncomms8711