{"id":943,"date":"2026-06-12T16:52:11","date_gmt":"2026-06-12T07:52:11","guid":{"rendered":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/?post_type=information&#038;p=943"},"modified":"2026-06-12T16:52:11","modified_gmt":"2026-06-12T07:52:11","slug":"%e8%83%a1%e6%a1%83%e5%9d%82%e8%a8%88%e7%94%bb%e7%a0%94%e7%a9%b6%e4%bb%a3%e8%a1%a8%e3%81%ab%e3%82%88%e3%82%8b%e6%88%90%e6%9e%9c%e3%81%8ccommunications-biology%e8%aa%8c%e3%81%ab%e6%8e%b2%e8%bc%89","status":"publish","type":"information","link":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/archives\/information\/%e8%83%a1%e6%a1%83%e5%9d%82%e8%a8%88%e7%94%bb%e7%a0%94%e7%a9%b6%e4%bb%a3%e8%a1%a8%e3%81%ab%e3%82%88%e3%82%8b%e6%88%90%e6%9e%9c%e3%81%8ccommunications-biology%e8%aa%8c%e3%81%ab%e6%8e%b2%e8%bc%89","title":{"rendered":"\u80e1\u6843\u5742\u8a08\u753b\u7814\u7a76\u4ee3\u8868\u306b\u3088\u308b\u6210\u679c\u304cCommunications Biology\u8a8c\u306b\u63b2\u8f09\u3055\u308c\u307e\u3057\u305f!"},"content":{"rendered":"\n<p class=\"wp-block-paragraph\"><strong>Linker histone H1 represses H3 tail acetylation induced by H4 tail acetylation and alters its dynamics<\/strong><\/p>\n\n\n\n<p class=\"wp-block-paragraph\">Ayako Furukawa, Kenta Echigoya, Samuel Blazquez, Masatoshi Wakamori, Hideaki Ohtomo, Yasuo Tsunaka, Takashi Umehara, Tsuyoshi Terakawa, Yoshimasa Takizawa, Hitoshi Kurumizaka, Yoshifumi Nishimura<\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong>Abstract<\/strong><br>The nucleosome is the fundamental chromatin unit, containing two copies of histones H2A, H2B, H3, and H4 wrapped by ~146 bp of core DNA plus linker DNA; addition of linker histone H1 forms a chromatosome. Tetra-acetylation of the H4 N-terminal tail (H4-4Kac) enhances H3 N-tail acetylation by altering their mutual dynamics, but how H1 influences these dynamics remains unclear. Using cryo-electron microscopy and coarse-grained molecular dynamics simulations, we show that H4-4Kac and unmodified chromatosomes share essentially identical core histone\u2013DNA structures and similar H3 N-tail dynamics. However, nuclear magnetic resonance spectroscopy reveals that in the H4-4Kac chromatosome, the H3 N-tail adopts a dynamically robust DNA-contact state distinct from that in the unmodified chromatosome, resulting in markedly reduced H3 N-tail acetylation. These findings suggest that linker histone H1 suppresses the progression of euchromatin formation.<\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><em>Communications Biology<\/em><\/strong>, 9, 496. doi: 10.1038\/s42003-026-09926-y. (2026)<br><a href=\"https:\/\/www.nature.com\/articles\/s42003-026-09926-y\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/www.nature.com\/articles\/s42003-026-09926-y<\/a><\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Linker histone H1 represses H3 tail acetylation induced by H4 tail acetylation a &#8230; <\/p>\n","protected":false},"featured_media":0,"menu_order":0,"template":"","format":"standard","meta":{"footnotes":""},"class_list":["post-943","information","type-information","status-publish","format-standard","hentry"],"_links":{"self":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/943","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information"}],"about":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/types\/information"}],"version-history":[{"count":1,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/943\/revisions"}],"predecessor-version":[{"id":944,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/943\/revisions\/944"}],"wp:attachment":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/media?parent=943"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}