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-Structure paper
タイトル | Structural insight into H4K20 methylation on H2A.Z-nucleosome by SUV420H1. |
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ジャーナル・号・ページ | Mol Cell, Vol. 83, Issue 16, Page 2884-22895.e7, Year 2023 |
掲載日 | 2023年8月17日 |
著者 | Li Huang / Youwang Wang / Haizhen Long / Haoqiang Zhu / Zengqi Wen / Liwei Zhang / Wenhao Zhang / Zhenqian Guo / Longge Wang / Fangyi Tang / Jie Hu / Keyan Bao / Ping Zhu / Guohong Li / Zheng Zhou / |
PubMed 要旨 | DNA replication ensures the accurate transmission of genetic information during the cell cycle. Histone variant H2A.Z is crucial for early replication origins licensing and activation in which ...DNA replication ensures the accurate transmission of genetic information during the cell cycle. Histone variant H2A.Z is crucial for early replication origins licensing and activation in which SUV420H1 preferentially recognizes H2A.Z-nucleosome and deposits H4 lysine 20 dimethylation (H4K20me2) on replication origins. Here, we report the cryo-EM structures of SUV420H1 bound to H2A.Z-nucleosome or H2A-nucleosome and demonstrate that SUV420H1 directly interacts with H4 N-terminal tail, the DNA, and the acidic patch in the nucleosome. The H4 (1-24) forms a lasso-shaped structure that stabilizes the SUV420H1-nucleosome complex and precisely projects the H4K20 residue into the SUV420H1 catalytic center. In vitro and in vivo analyses reveal a crucial role of the SUV420H1 KR loop (residues 214-223), which lies close to the H2A.Z-specific residues D97/S98, in H2A.Z-nucleosome preferential recognition. Together, our findings elucidate how SUV420H1 recognizes nucleosomes to ensure site-specific H4K20me2 modification and provide insights into how SUV420H1 preferentially recognizes H2A.Z nucleosome. |
リンク | Mol Cell / PubMed:37536340 |
手法 | EM (単粒子) |
解像度 | 3.2 - 6.5 Å |
構造データ | EMDB-34053, PDB-7yrd: EMDB-34055, PDB-7yrg: EMDB-34056: histone methyltransferase EMDB-34057: histone methyltransferase |
化合物 | ChemComp-ZN: ChemComp-SAM: |
由来 |
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キーワード | GENE REGULATION / histone methyltransferase |