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-Structure paper
| タイトル | Stimulus-responsive assembly of nonviral nucleocapsids. |
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| ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 3576, Year 2024 |
| 掲載日 | 2024年4月27日 |
著者 | Mao Hori / Angela Steinauer / Stephan Tetter / Jamiro Hälg / Eva-Maria Manz / Donald Hilvert / ![]() |
| PubMed 要旨 | Controlled assembly of a protein shell around a viral genome is a key step in the life cycle of many viruses. Here we report a strategy for regulating the co-assembly of nonviral proteins and nucleic ...Controlled assembly of a protein shell around a viral genome is a key step in the life cycle of many viruses. Here we report a strategy for regulating the co-assembly of nonviral proteins and nucleic acids into highly ordered nucleocapsids in vitro. By fusing maltose binding protein to the subunits of NC-4, an engineered protein cage that encapsulates its own encoding mRNA, we successfully blocked spontaneous capsid assembly, allowing isolation of the individual monomers in soluble form. To initiate RNA-templated nucleocapsid formation, the steric block can be simply removed by selective proteolysis. Analyses by transmission and cryo-electron microscopy confirmed that the resulting assemblies are structurally identical to their RNA-containing counterparts produced in vivo. Enzymatically triggered cage formation broadens the range of RNA molecules that can be encapsulated by NC-4, provides unique opportunities to study the co-assembly of capsid and cargo, and could be useful for studying other nonviral and viral assemblies. |
リンク | Nat Commun / PubMed:38678040 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.5 Å |
| 構造データ | ![]() EMDB-16696: NC-4 nonviral nucleocapsids assembled in vitro |
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