{"id":941,"date":"2026-06-12T16:51:31","date_gmt":"2026-06-12T07:51:31","guid":{"rendered":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/?post_type=information&#038;p=941"},"modified":"2026-06-12T16:51:31","modified_gmt":"2026-06-12T07:51:31","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%8cjournal-of-biological-chemistry%e8%aa%8c%e3%81%ab%e6%8e%b2","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%8cjournal-of-biological-chemistry%e8%aa%8c%e3%81%ab%e6%8e%b2","title":{"rendered":"\u80e1\u6843\u5742\u8a08\u753b\u7814\u7a76\u4ee3\u8868\u306b\u3088\u308b\u6210\u679c\u304cJournal of Biological Chemistry\u8a8c\u306b\u63b2\u8f09\u3055\u308c\u307e\u3057\u305f!"},"content":{"rendered":"\n<p class=\"wp-block-paragraph\"><strong>Structural basis of RNA polymerase II transcription on the histone H3-H4 octasome<\/strong><\/p>\n\n\n\n<p class=\"wp-block-paragraph\">Ching-Hao Ho, Kaho Nozawa, Mai Nishimura, Masahiro Oi, Tomoya Kujirai, Mitsuo Ogasawara, Hiroshi Ehara, Shun-ichi Sekine, Yoshimasa Takizawa, Hitoshi Kurumizaka<\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong>Abstract<\/strong><br>The histone H3-H4 octasome is a nucleosome-like particle in which two DNA gyres are wrapped around each histone (H3-H4)2 tetramer disk, forming a clamshell-like configuration. In the present study, we performed in vitro RNA polymerase II (RNAPII) transcription assays with the H3-H4 octasome and found that RNAPII transcribed the H3-H4 octasome more efficiently than the nucleosome. RNAPII paused at only one position, superhelical location (SHL(-4)) in the H3-H4 octasome, in contrast to pausing at the SHL(-5), SHL(-2), and SHL(-1) positions in the nucleosome. Cryo-EM analysis revealed that two (H3-H4)2 tetramer disks are retained when the RNAPII paused at the SHL(-4) position of the H3-H4 octasome. However, when RNAPII reached the SHL(-0.5) position, five base pairs before the dyad position of the H3-H4 octasome, the proximal (H3-H4)2 tetramer was disassembled, but the distal (H3-H4)2 tetramer still remained on the DNA. Therefore, RNAPII efficiently transcribes the H3-H4 octasome by stepwise (H3-H4)2 tetramer disassembly.<\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><em>Journal of Biological Chemistry<\/em><\/strong>, 302, 111340. doi: 10.1016\/j.jbc.2026.111340. (2026)<br><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0021925826002103?via%3Dihub\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0021925826002103?via%3Dihub<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Structural basis of RNA polymerase II transcription on the histone H3-H4 octasom &#8230; <\/p>\n","protected":false},"featured_media":0,"menu_order":0,"template":"","format":"standard","meta":{"footnotes":""},"class_list":["post-941","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\/941","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\/941\/revisions"}],"predecessor-version":[{"id":942,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/941\/revisions\/942"}],"wp:attachment":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/media?parent=941"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}