Selected article for: "amino acid and silent mutation"

Author: Jamie A. Kelly; Jonathan D. Dinman
Title: Structural and functional conservation of the programmed -1 ribosomal frameshift signal of SARS-CoV-2
  • Document date: 2020_3_15
  • ID: 62izhj8d_11
    Snippet: Comparative functional analyses of the two -1 PRF signals. Standard dual-luciferase assays were used to monitor -1 PRF activities of the two -1 PRF signals (15, 16) in HEK and HeLa cells. For both of the elements, -1 PRF activity was ~20% in HEK ( Fig. 2A) and ~30% in HeLa (Fig. 2B) . Amino acid sequence silent coding mutation of the U UUA AAC slippery sites to C CUC AAC (the incoming 0-frame codons are indicated by spaces) ablated -1 PRF activit.....
    Document: Comparative functional analyses of the two -1 PRF signals. Standard dual-luciferase assays were used to monitor -1 PRF activities of the two -1 PRF signals (15, 16) in HEK and HeLa cells. For both of the elements, -1 PRF activity was ~20% in HEK ( Fig. 2A) and ~30% in HeLa (Fig. 2B) . Amino acid sequence silent coding mutation of the U UUA AAC slippery sites to C CUC AAC (the incoming 0-frame codons are indicated by spaces) ablated -1 PRF activity in both cases, to less than 1% (Fig. 2) . These findings support the hypothesis that structure and function of the -1 PRF signals has been conserved between the two viruses.

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