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TitleStimulus-responsive assembly of nonviral nucleocapsids.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3576, Year 2024
Publish dateApr 27, 2024
AuthorsMao Hori / Angela Steinauer / Stephan Tetter / Jamiro Hälg / Eva-Maria Manz / Donald Hilvert /
PubMed AbstractControlled 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.
External linksNat Commun / PubMed:38678040 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

EMDB-16696: NC-4 nonviral nucleocapsids assembled in vitro
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • Aquifex aeolicus (bacteria)

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