{"id":440,"date":"2025-02-22T09:07:56","date_gmt":"2025-02-22T00:07:56","guid":{"rendered":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/?post_type=information&#038;p=440"},"modified":"2025-02-22T09:14:23","modified_gmt":"2025-02-22T00:14:23","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%80%81%e5%be%8c%e8%97%a4%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","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%80%81%e5%be%8c%e8%97%a4%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","title":{"rendered":"\u80e1\u6843\u5742\u8a08\u753b\u7814\u7a76\u4ee3\u8868\u3001\u5f8c\u85e4\u8a08\u753b\u7814\u7a76\u4ee3\u8868\u3001\u6728\u6751\u8a08\u753b\u7814\u7a76\u4ee3\u8868\u306b\u3088\u308b\u6210\u679c\u304cNature Structural &amp; Molecular Biology \u8a8c\u306b\u63b2\u8f09\u3055\u308c\u307e\u3057\u305f!"},"content":{"rendered":"\n<p><strong>Structural insights into how DEK nucleosome binding facilitates H3K27 trimethylation in chromatin<\/strong><\/p>\n\n\n\n<p>Tomoya Kujirai, Kenta Echigoya, Yusuke Kishi, Mai Saeki, Tomoko Ito, Junko Kato, Lumi Negishi, Hiroshi Kimura, Hiroshi Masumoto, Yoshimasa Takizawa, Yukiko Gotoh &amp; Hitoshi Kurumizaka<\/p>\n\n\n\n<p><strong>Abstract<\/strong><br>Structural diversity of the nucleosome affects chromatin conformations and regulates eukaryotic genome functions. Here we identify DEK, whose function is unknown, as a nucleosome-binding protein. In embryonic neural progenitor cells, DEK colocalizes with H3 K27 trimethylation (H3K27me3), the facultative heterochromatin mark. DEK stimulates the methyltransferase activity of Polycomb repressive complex 2 (PRC2), which is responsible for H3K27me3 deposition in vitro. Cryo-electron microscopy structures of the DEK\u2013nucleosome complexes reveal that DEK binds the nucleosome by its tripartite DNA-binding mode on the dyad and linker DNAs and interacts with the nucleosomal acidic patch by its newly identified histone-binding region. The DEK\u2013nucleosome interaction mediates linker DNA reorientation and induces chromatin compaction, which may facilitate PRC2 activation. These findings provide mechanistic insights into chromatin structure-mediated gene regulation by DEK.<\/p>\n\n\n\n<p><strong><em>Nature Structural &amp; Molecular Biology<\/em><\/strong>, doi: 10.1038\/s41594-025-01493-w. (2025)<br><a href=\"https:\/\/www.nature.com\/articles\/s41594-025-01493-w\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/www.nature.com\/articles\/s41594-025-01493-w<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Structural insights into how DEK nucleosome binding facilitates H3K27 trimethyla &#8230; <\/p>\n","protected":false},"featured_media":0,"menu_order":0,"template":"","format":"standard","meta":{"footnotes":""},"class_list":["post-440","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\/440","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":2,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/440\/revisions"}],"predecessor-version":[{"id":444,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/440\/revisions\/444"}],"wp:attachment":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/media?parent=440"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}