Journal of Virology · 1998 · 53 citations · 29 references
Life SciencesBiochemistryMolecular BiologyMolecular VirologyRna ProcessingVirologyRna-binding ProteinsViral Rna BiologyViral StructureViral TranscriptionVirus StructureDouble-stranded Rna VirusesRna TriphosphataseRna-binding SpecificityTranscriptsViral Core StructureViral Rna StructureViral Rna SynthesisViral Rna Translation
The reovirus M1, L1, and L2 genes encode proteins found at each vertex of the viral core and are likely to form a structural unit involved in RNA synthesis. Genetic analyses have implicated the M1 gene in viral RNA synthesis and core nucleoside triphosphatase activity, but there have been no direct biochemical studies of mu2 function. Here, we expressed mu2 in vitro and assessed its RNA-binding activity. The expressed mu2 binds both poly(I-C)- and poly(U)-Sepharose, and binding activity is greater in Mn2+ than in Mg2+. Heterologous RNA competes for mu2 binding to reovirus RNA transcripts as effectively as homologous reovirus RNA does, providing no evidence for sequence-specific RNA binding by mu2. Protein mu2 is now the sixth reovirus protein demonstrated to have RNA-binding activity.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
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Arginine-Mediated RNA Recognition: the Arginine Fork
Barbara J. Calnan, Bruce Tidor, Sara Biancalana et al. · Science · 1991 · 755 citations