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Recent work with RNA phages and an ssRNA plant satellite virus challenges the widely held view that the sequences and structures of genomic RNAs are unimportant for virion assembly. In the T=3 phages, RNA-coat protein interactions occur throughout the genome, defining the quasiconformers of their protein shells. In the plant virus, there are multiple packaging signals dispersed throughout the genome that overcome electrostatic barriers to protein self-assembly. Both viral coat proteins cause the solution structures of their cognate genomes to collapse into a form that is readily encapsidated in a two-stage assembly process. Such similar behavior in two structurally unrelated viral protein folds implies that this might be a conserved feature of many viral assembly reactions. These results suggest a highly defined structure for the RNA in the virions, consistent with recent structural studies. They also have implications both for subsequent genome release during infection and for the evolution of viral sequences.
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