Interaction of cellular proteins with the poliovirus 5' noncoding region.
The 5' noncoding region (NCR) of poliovirus RNA is folded into a complex structure comprised of multiple, critically spaced, stem-loop domains. Mutations in at least one of these domains markedly affects the neurovirulence of the virus. Two proteins have been identified recently which bind and apparently mediate functions of the 5' NCR in translation. We have demonstrated specific binding of three additional proteins in a Hela cell ribosomal salt wash that can be crosslinked to specific stem-loop segments of the 5' NCR. These same RNA segments inhibit translation of polio RNA in vitro, presumably by competing for protein binding. The Sabin vaccine strain of polio RNA exhibits a reduced affinity of binding for specific proteins. The determinant for this reduction appears to be a single nucleotide difference at position 480 between the neurovirulent and attenuated viral strains.
Department of Molecular Biology and Biochemistry, University of California, Irvine.
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Ehrenfeld
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JG
Gebhard
D001667:Binding, Competitive; D003432:Cross-Linking Reagents; D006367:HeLa Cells; D006801:Humans; D009417:Nerve Tissue / Q000382:microbiology; D009690:Nucleic Acid Conformation; D017955:Poliovirus / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis; D012367:RNA, Viral / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D012045:Regulatory Sequences, Nucleic Acid / Q000235:genetics*; D013045:Species Specificity; D014466:Ultraviolet Rays
D003432:Cross-Linking Reagents; D012367:RNA, Viral; D016601:RNA-Binding Proteins