Selected article for: "frameshift stimulator and shift site"
Author: Atkins, John F.; Loughran, Gary; Bhatt, Pramod R.; Firth, Andrew E.; Baranov, Pavel V.
Title: Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use
  • Document date: 2016_9_6
    • ID: 0s8huajd_194
    Snippet: Porcine reproductive and respiratory syndrome virus (family Arteriviridae) frameshifting (22) is trans-activated by a protein complex composed of a virally-encoded replicase subunit, nsp1␤ and a cellular poly(C) binding protein interacting with the mRNA sequence CCCANCUCC 11 nucleotides 3 of the shift site, and so the 3 stimulator potentially permits temporal control during the course of viral infection (23; S. Napthine, E.Treffers, S. Bell, I......
    Document: Porcine reproductive and respiratory syndrome virus (family Arteriviridae) frameshifting (22) is trans-activated by a protein complex composed of a virally-encoded replicase subunit, nsp1␤ and a cellular poly(C) binding protein interacting with the mRNA sequence CCCANCUCC 11 nucleotides 3 of the shift site, and so the 3 stimulator potentially permits temporal control during the course of viral infection (23; S. Napthine, E.Treffers, S. Bell, I. Goodfellow, Y. Fang, A.E.F., E. Snijder and I. Brierley, submitted). Binding of the complex mimics the effect of a structured mRNA frameshift stimulator. Earlier work showed that nsp1␤ interacts with a ribosomal protein, RpS14 (573) . This protein is adjacent to RpS3 which is thought to function in mRNA unwinding activity (512) .

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