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

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

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)

The HIRA histone chaperone complex is involved in the deposition of the histone variant H3.3. Here the authors, by using biochemical and crystallographic approaches, report the homotrimerization of the HIRA subunit which is critical for the functiona

Externí odkaz: https://doaj.org/article/71022acda3b54be6ad946c83a4006f44

Rap1‐mediated nucleosome displacement can regulate gene expression in senescent cells without impacting the pace of senescence

Autor: Ronen Marmorstein, Shufei Song, William Svitko, Elliot Dean, F. Brad Johnson, M. Daniel Ricketts, Javier V Perez, David C. Schultz

Publikováno v: Aging Cell

Cell senescence is accompanied, and in part mediated, by changes in chromatin, including histone losses, but underlying mechanisms are not well understood. We reported previously that during yeast cell senescence driven by telomere shortening, the te

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b517c6cfaa1d728a98b4d52b80289c8
http://europepmc.org/articles/PMC6974733

L'activité fonctionnelle du complexe d'histone chaperon H3.3 HIRA nécessite la trimérisation de la sous-unité HIRA

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

Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2018, 9 (1), pp.3103 article number. ⟨10.1038/s41467-018-05581-y⟩
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Nature Communications, Nature Publishing Group, 2018, 9, ⟨10.1038/s41467-018-05581-y⟩

The HIRA histone chaperone complex deposits the histone variant H3.3 onto chromatin in a DNA synthesis-independent manner. It comprises three identified subunits, HIRA, UBN1 and CABIN1, however the functional oligomerization state of the complex has

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::020f05546bb40ecbc23c22e3828e2551
https://pubmed.ncbi.nlm.nih.gov/30082790

The scaffolding protein JADE1 physically links the acetyltransferase subunit HBO1 with its histone H3-H4 substrate

Autor: Ben E. Black, Jacques Côté, Ronen Marmorstein, Catherine Lachance, M. Daniel Ricketts, Cheryl E. McCullough, Morgan Gerace, Joseph Han

Publikováno v: The Journal of biological chemistry. 293(12)

The human enzyme histone acetyltransferase binding to ORC1 (HBO1) regulates DNA replication, cell proliferation, and development. HBO1 is part of a multiprotein histone acetyltransferase (HAT) complex that also contains inhibitor of growth family mem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5eabd134aed5123fcd7bf500e33f6db2
https://pubmed.ncbi.nlm.nih.gov/29382722

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

Autor: Peter D. Adams, Ronen Marmorstein, Brian Frederick, Henry Hoff, David C. Schultz, Yong Tang, Taranjit Singh Rai, Maria Grazia Vizioli, M. Daniel Ricketts

Publikováno v: Nature Communications

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 me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92f2116925aef9b56e11912a19ee25a3
https://eprints.gla.ac.uk/109536/1/109536.pdf