Selected article for: "catalytic activity and wild type"

Author: Elsie Yekwa; Chutima Aphibanthammakit; Xavier Carnec; Bruno Coutard; Caroline Picard; Bruno Canard; Sylvain Baize; François Ferron
Title: Arenaviridae exoribonuclease presents genomic RNA edition capacity
  • Document date: 2019_2_8
  • ID: fvp45ho6_22
    Snippet: We mutated each catalytic residue to alanine in order to assess their respective contribution in the conserved DEDDh catalytic motif, and tested them for ExoN activity. For the NP-exo MOPV mutants D390A, E392A and D534A, the 3'-5' ExoN activity is completely abolished whereas D467A and H529A are still able to slowly excise up to two nucleotides. For the NP-exo LCMV mutants, a slightly different result is observed. D382A and E384A show a complete .....
    Document: We mutated each catalytic residue to alanine in order to assess their respective contribution in the conserved DEDDh catalytic motif, and tested them for ExoN activity. For the NP-exo MOPV mutants D390A, E392A and D534A, the 3'-5' ExoN activity is completely abolished whereas D467A and H529A are still able to slowly excise up to two nucleotides. For the NP-exo LCMV mutants, a slightly different result is observed. D382A and E384A show a complete loss of activity, D459A excises two nucleotides but more efficiently than D467A of NP-exo MOPV as judged by the diminution of the 22 nts band-product. The H517A also shows residual activity while the D522A is able to degrade almost the total amount of 22 nt dsRNA up to 20/19 nts (Fig 1A) . We compared the efficacy of cleavage between the wild type NP-exo MOPV and NP-exo LCMV to their corresponding mutants D467A and D459A respectively. Our kinetic experiment indicates that the initial excision rate of NP-exo MOPV and NP-exo LCMV wild types are similar, the rate of D459A

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