{"id":467,"date":"2025-01-27T05:20:00","date_gmt":"2025-01-26T20:20:00","guid":{"rendered":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/?post_type=information&#038;p=467"},"modified":"2025-03-27T05:21:10","modified_gmt":"2025-03-26T20:21:10","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%8cnat-communications-%e8%aa%8c%e3%81%ab%e6%8e%b2%e8%bc%89%e3%81%95","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%8cnat-communications-%e8%aa%8c%e3%81%ab%e6%8e%b2%e8%bc%89%e3%81%95","title":{"rendered":"\u80e1\u6843\u5742\u8a08\u753b\u7814\u7a76\u4ee3\u8868\u306b\u3088\u308b\u6210\u679c\u304cNat Communications \u8a8c\u306b\u63b2\u8f09\u3055\u308c\u307e\u3057\u305f!"},"content":{"rendered":"\n<p><strong>Chemical catalyst manipulating cancer epigenome and transcription<\/strong><\/p>\n\n\n\n<p>Yuki Yamanashi, Shinpei Takamaru, Atsushi Okabe, Satoshi Kaito, Yuto Azumaya, Yugo R. Kamimura, Kenzo Yamatsugu, Tomoya Kujirai, Hitoshi Kurumizaka, Atsushi Iwama, Atsushi Kaneda, Shigehiro A. Kawashima &amp; Motomu Kanai<\/p>\n\n\n\n<p><strong>Abstract<\/strong><br>The number and variety of identified histone post-translational modifications (PTMs) are continually increasing. However, the specific consequences of each histone PTM remain largely unclear, primarily due to the lack of methods for selectively and rapidly introducing a desired histone PTM in living cells without genetic engineering. Here, we report the development of a cell-permeable histone acetylation catalyst, BAHA-LANA-PEG-CPP44, which selectively enters leukemia cells, binds to chromatin, and acetylates H2BK120 of endogenous histones in a short reaction time. Time-course analyses of this in-cell catalytic reaction revealed that H2BK120 acetylation attenuates the chromatin binding of negative elongation factor E (NELFE), an onco-transcription factor. This H2BK120 acetylation-mediated removal of NELFE from chromatin reshapes transcription, slows leukemia cell viability, and reduces their tumorigenic potential in mice. Therefore, this histone acetylation catalyst provides a unique tool for elucidating the time-resolved consequences of histone PTMs and may offer a modality for cancer chemotherapy.<\/p>\n\n\n\n<p><strong><em>Nat Commun<\/em><\/strong>, doi: 10.1038\/s41467-025-56204-2. (2025)<br><a href=\"https:\/\/www.nature.com\/articles\/s41467-025-56204-2\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/www.nature.com\/articles\/s41467-025-56204-2<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Chemical catalyst manipulating cancer epigenome and transcription Yuki Yamanashi &#8230; <\/p>\n","protected":false},"featured_media":0,"menu_order":0,"template":"","format":"standard","meta":{"footnotes":""},"class_list":["post-467","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\/467","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\/467\/revisions"}],"predecessor-version":[{"id":468,"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/information\/467\/revisions\/468"}],"wp:attachment":[{"href":"https:\/\/www.bioreg.kyushu-u.ac.jp\/ext\/epicode\/wp-json\/wp\/v2\/media?parent=467"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}