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タイトル: | Pericentric H3K9me3 Formation by HP1 Interaction-defective Histone Methyltransferase Suv39h1 |
著者: | Muramatsu, Daisuke Kimura, Hiroshi Kotoshiba, Kaoru Tachibana, Makoto Shinkai, Yoichi |
著者名の別形: | 村松, 大輔 立花, 誠 |
キーワード: | H3K9 methylation HP1 major satellite repeats Suv39h |
発行日: | 2016 |
出版者: | Japan Society for Cell Biology |
誌名: | Cell Structure and Function |
巻: | 41 |
号: | 2 |
開始ページ: | 145 |
終了ページ: | 152 |
抄録: | Pericentric regions form epigenetically organized, silent heterochromatin structures that accumulate histone H3 lysine 9 tri-methylation (H3K9me3) and heterochromatin protein 1 (HP1), a methylated H3K9-binding protein. At pericentric regions, Suv39h is the major enzyme that generates H3K9me3. Suv39h also interacts directly with HP1. However, the importance of HP1 interaction for Suv39h-mediated H3K9me3 formation at the pericentromere is not well characterized. To address this question, we introduced HP1 binding-defective, N-terminally truncated mouse Suv39h1 (ΔN) into Suv39h-deficient cells. Pericentric H3K9me3-positive cells were not detected by endogenous-level expression of ΔN. Notably, ΔN could induce pericentric accumulation of H3K9me3 as wild type Suv39h1 did if it was overexpressed. These findings demonstrate that the N-terminal region of Suv39h1, presumably via HP1–Suv39h1 interaction, is required for Suv39h1-mediated pericentric H3K9me3 formation, but can be overridden if Suv39h1 is overproduced, indicating that Suv39h1-mediated heterochromatin formation is controlled by multiple modules, including HP1. |
著作権等: | © 2016 by Japan Society for Cell Biology Authors retain the copyright in their work and grant the journal a license to publish. Users have certain rights to share, distribute and re-use published content under the terms of the Creative Commons Attribution 4.0 International (CC BY 4.0) license. |
URI: | http://hdl.handle.net/2433/227293 |
DOI(出版社版): | 10.1247/csf.16013 |
PubMed ID: | 27733730 |
出現コレクション: | 学術雑誌掲載論文等 |
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