Structure and function of the rotavirus RNA-binding proteins.

@article{Patton1995StructureAF,
  title={Structure and function of the rotavirus RNA-binding proteins.},
  author={John Thomas Patton},
  journal={The Journal of general virology},
  year={1995},
  volume={76 ( Pt 11)},
  pages={
          2633-44
        }
}
  • J. Patton
  • Published 1 November 1995
  • Biology, Medicine
  • The Journal of general virology
Introduction. Of the six structural and six nonstructural proteins encoded by the segmented double-stranded (ds) RNA genome of the rotaviruses, recent studies suggest that as many as seven may have affinity for RNA. While their functions in virus replication have yet to be precisely defined, the RNA-binding proteins may play essential roles in a number of events including: (i) transport of viral mRNAs to the site of replication, (ii) packaging and assortment of viral mRNA, (iii) RNA synthesis… Expand
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The use of UV cross-linking followed by immunoprecipitation and labeling with T4 polynucleotide kinase allowed us to detect interactions between RNA and nonstructural viral proteins and it is shown that the last 3' nucleotide is cross-linked to the protein and that monomeric and multimeric forms of NSP3 are bound to rotavirus mRNA. Expand
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Electrophoretic analysis indicated that replicase particles, purified by centrifugation on CsCl and glycerol gradients, were similar to SS particles, containing the structural proteins VP1, VP2, and VP6, suggesting that, like transcription, this protein may be required for rotavirus RNA replication. Expand
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Comparison of the nucleotide sequences for gene 5 showed that the entire 5'-noncoding region and the first 24 nt of the NS53 ORF are conserved, suggesting that such structures may be common to all rotavirus mRNAs, perhaps functioning as signals for packaging of RNAs into replication intermediates or regulating mRNA translation. Expand
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