Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit-Reference-Cited by-同舟云学术

Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit

Published:2018-08-06 Issue:1 Volume:9 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Ray-Gallet Dominique,Ricketts M. Daniel,Sato Yukari^ORCID,Gupta Kushol,Boyarchuk Ekaterina^ORCID,Senda Toshiya,Marmorstein Ronen^ORCID,Almouzni Geneviève

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-05581-y.pdf

Reference49 articles.

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2. Gurard-Levin, Z. A., Quivy, J. P. & Almouzni, G. Histone chaperones: assisting histone traffic and nucleosome dynamics. Annu. Rev. Biochem. 83, 487–517 (2014).

3. Tagami, H., Ray-Gallet, D., Almouzni, G. & Nakatani, Y. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell 116, 51–61 (2004).

4. Ray-Gallet, D. et al. HIRA is critical for a nucleosome assembly pathway independent of DNA synthesis. Mol. Cell 9, 1091–1100 (2002).

5. Ray-Gallet, D. et al. Dynamics of histone H3 deposition in vivo reveal a nucleosome gap-filling mechanism for H3.3 to maintain chromatin integrity. Mol. Cell 44, 928–941 (2011).

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