{"id":956,"date":"2026-06-24T05:20:18","date_gmt":"2026-06-23T20:20:18","guid":{"rendered":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/?post_type=information&#038;p=956"},"modified":"2026-06-25T05:31:23","modified_gmt":"2026-06-24T20:31:23","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%81%ab%e3%82%88%e3%82%8b%e6%88%90%e6%9e%9c%e3%81%8cnature-communications%e8%aa%8c%e3%81%ab%e6%8e%b2%e8%bc%89-2","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%8cnature-communications%e8%aa%8c%e3%81%ab%e6%8e%b2%e8%bc%89-2","title":{"rendered":"\u80e1\u6843\u5742\u8a08\u753b\u7814\u7a76\u4ee3\u8868\u306b\u3088\u308b\u6210\u679c\u304cNature Communications\u8a8c\u306b\u63b2\u8f09\u3055\u308c\u307e\u3057\u305f!"},"content":{"rendered":"\n<p class=\"wp-block-paragraph\"><strong>Structural basis of nucleosome remodeling by Cockayne syndrome B homologue Komagataella phaffii Rad26<\/strong><\/p>\n\n\n\n<p class=\"wp-block-paragraph\">Yutaro Fukushima, Chiaki Kinoshita, Lumi Negishi, Tomoya Kujirai, Yuki Kobayashi, Mitsuo Ogasawara, Haruhiko Ehara, Shun-ichi Sekine, Wataru Kagawa, Hitoshi Kurumizaka, Yoshimasa Takizawa<\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong>Abstract<\/strong><br>Rad26, a yeast homologue of mammalian Cockayne syndrome protein B (CSB), plays an essential role in transcription-coupled nucleotide excision repair (TC-NER). Rad26\/CSB binds RNA polymerase II stalled at DNA lesions and recruits DNA repair factors, functioning as a molecular scaffold. In addition, Rad26\/CSB possesses nucleosome-remodeling activity that may help restore transcription after DNA repair. Here we determine the cryo-electron microscopy structure of the Rad26\/CSB-nucleosome complex. Rad26\/CSB binds near the nucleosomal entry\/exit region (superhelical location +\/-6) through a unique mechanism in which its ATPase domains, Lobe 1 and Lobe 2, engage nucleosomal DNA in a reverse orientation compared with other remodelers such as Snf2 and Ino80. Mutational, biochemical, and crosslinking mass-spectrometric analyses demonstrate the requirement of the KR loop for nucleosome binding and remodeling. Furthermore, we show that N-terminal auto-inhibition involves long-range contacts between the disordered N-terminus and the Lobe 2 region, and is relieved by mutations of Leu8 and Leu11. These findings reveal the structural basis of Rad26\/CSB-mediated nucleosome remodeling in TC-NER.<\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><em>Nature Communications<\/em><\/strong>, 17, 4881. doi: 10.1038\/s41467-026-73500-7. (2026)<br><a href=\"https:\/\/www.nature.com\/articles\/s41467-026-73500-7\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/www.nature.com\/articles\/s41467-026-73500-7<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Structural basis of nucleosome remodeling by Cockayne syndrome B homologue Komag &#8230; <\/p>\n","protected":false},"featured_media":0,"menu_order":0,"template":"","format":"standard","meta":{"footnotes":""},"class_list":["post-956","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\/956","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\/956\/revisions"}],"predecessor-version":[{"id":957,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/956\/revisions\/957"}],"wp:attachment":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/media?parent=956"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}