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-Structure paper
タイトル | Molecular mechanism for target recognition, dimerization, and activation of Pyrococcus furiosus Argonaute. |
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ジャーナル・号・ページ | Mol Cell, Vol. 84, Issue 4, Page 675-686.e4, Year 2024 |
掲載日 | 2024年2月15日 |
著者 | Longyu Wang / Wanping Chen / Chendi Zhang / Xiaochen Xie / Fuyong Huang / Miaomiao Chen / Wuxiang Mao / Na Yu / Qiang Wei / Lixin Ma / Zhuang Li / |
PubMed 要旨 | The Argonaute nuclease from the thermophilic archaeon Pyrococcus furiosus (PfAgo) contributes to host defense and represents a promising biotechnology tool. Here, we report the structure of a PfAgo- ...The Argonaute nuclease from the thermophilic archaeon Pyrococcus furiosus (PfAgo) contributes to host defense and represents a promising biotechnology tool. Here, we report the structure of a PfAgo-guide DNA-target DNA ternary complex at the cleavage-compatible state. The ternary complex is predominantly dimerized, and the dimerization is solely mediated by PfAgo at PIWI-MID, PIWI-PIWI, and PAZ-N interfaces. Additionally, PfAgo accommodates a short 14-bp guide-target DNA duplex with a wedge-type N domain and specifically recognizes 5'-phosphorylated guide DNA. In contrast, the PfAgo-guide DNA binary complex is monomeric, and the engagement of target DNA with 14-bp complementarity induces sufficient dimerization and activation of PfAgo, accompanied by movement of PAZ and N domains. A closely related Argonaute from Thermococcus thioreducens adopts a similar dimerization configuration with an additional zinc finger formed at the dimerization interface. Dimerization of both Argonautes stabilizes the catalytic loops, highlighting the important role of Argonaute dimerization in the activation and target cleavage. |
リンク | Mol Cell / PubMed:38295801 |
手法 | EM (単粒子) |
解像度 | 2.9 Å |
構造データ | EMDB-36489, PDB-8jpx: EMDB-37457, PDB-8wd8: |
化合物 | ChemComp-MG: ChemComp-ZN: |
由来 |
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キーワード | GENE REGULATION (遺伝子発現の調節) / nuclease (ヌクレアーゼ) / DNA BINDING PROTEIN/DNA / DNA BINDING PROTEIN-DNA COMPLEX |