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http://purl.uniprot.org/citations/27992877http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27992877http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27992877http://www.w3.org/2000/01/rdf-schema#comment"Packaging of the genome into a protein capsid and its subsequent delivery into a host cell are two fundamental processes in the life cycle of a virus. Unlike double-stranded DNA viruses, which pump their genome into a preformed capsid, single-stranded RNA (ssRNA) viruses, such as bacteriophage MS2, co-assemble their capsid with the genome; however, the structural basis of this co-assembly is poorly understood. MS2 infects Escherichia coli via the host 'sex pilus' (F-pilus); it was the first fully sequenced organism and is a model system for studies of translational gene regulation, RNA-protein interactions, and RNA virus assembly. Its positive-sense ssRNA genome of 3,569 bases is enclosed in a capsid with one maturation protein monomer and 89 coat protein dimers arranged in a T = 3 icosahedral lattice. The maturation protein is responsible for attaching the virus to an F-pilus and delivering the viral genome into the host during infection, but how the genome is organized and delivered is not known. Here we describe the MS2 structure at 3.6 Å resolution, determined by electron-counting cryo-electron microscopy (cryoEM) and asymmetric reconstruction. We traced approximately 80% of the backbone of the viral genome, built atomic models for 16 RNA stem-loops, and identified three conserved motifs of RNA-coat protein interactions among 15 of these stem-loops with diverse sequences. The stem-loop at the 3' end of the genome interacts extensively with the maturation protein, which, with just a six-helix bundle and a six-stranded β-sheet, forms a genome-delivery apparatus and joins 89 coat protein dimers to form a capsid. This atomic description of genome-capsid interactions in a spherical ssRNA virus provides insight into genome delivery via the host sex pilus and mechanisms underlying ssRNA-capsid co-assembly, and inspires speculation about the links between nucleoprotein complexes and the origins of viruses."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.org/dc/terms/identifier"doi:10.1038/nature20589"xsd:string
http://purl.uniprot.org/citations/27992877http://purl.org/dc/terms/identifier"doi:10.1038/nature20589"xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Dai X."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Dai X."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Du Y."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Du Y."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Sun R."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Sun R."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Shu S."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Shu S."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Zhou Z.H."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Zhou Z.H."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Lai M."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/author"Lai M."xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/pages"112-116"xsd:string
http://purl.uniprot.org/citations/27992877http://purl.uniprot.org/core/pages"112-116"xsd:string