{"id":770,"date":"2025-11-12T05:17:06","date_gmt":"2025-11-11T20:17:06","guid":{"rendered":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/?post_type=information&#038;p=770"},"modified":"2025-11-12T05:17:06","modified_gmt":"2025-11-11T20:17:06","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","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","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><strong>Structural basis of cyclobutane pyrimidine dimer recognition by UV-DDB in the nucleosome<\/strong><\/p>\n\n\n\n<p>Syota Matsumoto, Yoshimasa Takizawa, Mitsuo Ogasawara, Kana Hashimoto, Lumi Negishi, Wenjie Xu, Haruna Tachibana, Junpei Yamamoto, Shigenori Iwai, Kaoru Sugasawa &amp; Hitoshi Kurumizaka<\/p>\n\n\n\n<p><strong>Abstract<\/strong><br>In mammalian global genomic nucleotide excision repair, UV-DDB plays a central role in recognizing DNA lesions, such as 6-4 photoproducts and cyclobutane pyrimidine dimers, within chromatin. In the present study, we perform cryo-electron microscopy analyses coupled with chromatin-immunoprecipitation to reveal that the cellular UV-DDB binds to UV-damaged DNA lesions in a chromatin unit, the nucleosome, at a position approximately 20 base-pairs from the nucleosomal dyad in human cells. An alternative analysis of the in vitro reconstituted UV-DDB-cyclobutane pyrimidine dimer nucleosome structure demonstrates that the DDB2 subunit of UV-DDB specifically recognizes the cyclobutane pyrimidine dimer lesion at this position on the nucleosome. We also determine the structures of UV-DDB bound to DNA lesions at other positions in purified cellular human nucleosomes. These cellular and reconstituted UV-DDB-nucleosome complex structures provide important evidence for understanding the mechanism by which UV lesions in chromatin are recognized and repaired in mammalian cells.<\/p>\n\n\n\n<p><strong><em>Nature Communications<\/em><\/strong>, doi: 10.1038\/s41467-025-65486-5. (2025)<br><a href=\"https:\/\/www.nature.com\/articles\/s41467-025-65486-5\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/www.nature.com\/articles\/s41467-025-65486-5<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Structural basis of cyclobutane pyrimidine dimer recognition by UV-DDB in the nu &#8230; <\/p>\n","protected":false},"featured_media":0,"menu_order":0,"template":"","format":"standard","meta":{"footnotes":""},"class_list":["post-770","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\/770","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\/770\/revisions"}],"predecessor-version":[{"id":771,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/770\/revisions\/771"}],"wp:attachment":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/media?parent=770"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}