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hGW182 Argonaute-binding motifs binding to hAgo2 and hAgo1. (A) Schematic domain organization of hGW182 (TNRC6A). The different Ago-binding motifs within the Ago-binding domain (ABD) are colored in yellow. (B–C) Isothermal titration calorimetry (ITC) analysis of the interaction between hGW182 Ago-binding motifs and hAgo2 (B) hAgo1 (C). In all experiments the ITC cell was filled with either hAgo2 or hAgo1 and the different hGW182 Ago-binding motifs were titrated as the ligands. Affinities are reported as dissociation constants (Kd) ± standard errors calculated from the fit. (D–E) <t>Fluorescence</t> <t>Polarization</t> (FP) binding experiments of FITC-labeled hGW182 hook motif with hAgo2 (D) and hAgo1 (E) showing increased affinity of the hook motif to both hAgo2 and hAgo1 that are loaded with endogenous RNA (solid blue line) compared to RNA-free hAgo2 and hAgo1 (dashed red line). Dissociation constants (Kd) were calculated by fitting data from three different experiments and are shown as the average ± standard deviation. See also Figure S1.
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hGW182 Argonaute-binding motifs binding to hAgo2 and hAgo1. (A) Schematic domain organization of hGW182 (TNRC6A). The different Ago-binding motifs within the Ago-binding domain (ABD) are colored in yellow. (B–C) Isothermal titration calorimetry (ITC) analysis of the interaction between hGW182 Ago-binding motifs and hAgo2 (B) hAgo1 (C). In all experiments the ITC cell was filled with either hAgo2 or hAgo1 and the different hGW182 Ago-binding motifs were titrated as the ligands. Affinities are reported as dissociation constants (Kd) ± standard errors calculated from the fit. (D–E) Fluorescence Polarization (FP) binding experiments of FITC-labeled hGW182 hook motif with hAgo2 (D) and hAgo1 (E) showing increased affinity of the hook motif to both hAgo2 and hAgo1 that are loaded with endogenous RNA (solid blue line) compared to RNA-free hAgo2 and hAgo1 (dashed red line). Dissociation constants (Kd) were calculated by fitting data from three different experiments and are shown as the average ± standard deviation. See also Figure S1.

Journal: Molecular cell

Article Title: Multivalent recruitment of human Argonaute by GW182

doi: 10.1016/j.molcel.2017.07.007

Figure Lengend Snippet: hGW182 Argonaute-binding motifs binding to hAgo2 and hAgo1. (A) Schematic domain organization of hGW182 (TNRC6A). The different Ago-binding motifs within the Ago-binding domain (ABD) are colored in yellow. (B–C) Isothermal titration calorimetry (ITC) analysis of the interaction between hGW182 Ago-binding motifs and hAgo2 (B) hAgo1 (C). In all experiments the ITC cell was filled with either hAgo2 or hAgo1 and the different hGW182 Ago-binding motifs were titrated as the ligands. Affinities are reported as dissociation constants (Kd) ± standard errors calculated from the fit. (D–E) Fluorescence Polarization (FP) binding experiments of FITC-labeled hGW182 hook motif with hAgo2 (D) and hAgo1 (E) showing increased affinity of the hook motif to both hAgo2 and hAgo1 that are loaded with endogenous RNA (solid blue line) compared to RNA-free hAgo2 and hAgo1 (dashed red line). Dissociation constants (Kd) were calculated by fitting data from three different experiments and are shown as the average ± standard deviation. See also Figure S1.

Article Snippet: Fluorescence polarization binding data were plotted and fit using GraphPad Prism 6.

Techniques: Binding Assay, Isothermal Titration Calorimetry, Fluorescence, Labeling, Standard Deviation

Mutational analysis of the GW binding pockets of hAgo1 and hAgo2. (A) Fluorescence Polarization (FP) binding experiments of FITC-labeled hGW182 hook to hAgo2. (B) Same as (A) but with hAgo1. GW binding pockets mutants shows drastic decrease in hGW182 hook binding when residues from both binding pockets are mutated simultaneously. Data shown are from three different experiments and presented as the average± standard deviation. The lines for fitted curves with Rsquare<0.7 were omitted from the figure. (C) FP binding experiments of hAgo2 “gate” residue mutants with FITC-labeled hGW182 showing a substantial decrease in binding compared to wild-type. (D) Similar experiments for gate residue mutants of hAgo1. Dissociation constant (Kd) were calculated by fitting data from three different experiments and are shown as average ± standard deviation. See also Table S1.

Journal: Molecular cell

Article Title: Multivalent recruitment of human Argonaute by GW182

doi: 10.1016/j.molcel.2017.07.007

Figure Lengend Snippet: Mutational analysis of the GW binding pockets of hAgo1 and hAgo2. (A) Fluorescence Polarization (FP) binding experiments of FITC-labeled hGW182 hook to hAgo2. (B) Same as (A) but with hAgo1. GW binding pockets mutants shows drastic decrease in hGW182 hook binding when residues from both binding pockets are mutated simultaneously. Data shown are from three different experiments and presented as the average± standard deviation. The lines for fitted curves with Rsquare<0.7 were omitted from the figure. (C) FP binding experiments of hAgo2 “gate” residue mutants with FITC-labeled hGW182 showing a substantial decrease in binding compared to wild-type. (D) Similar experiments for gate residue mutants of hAgo1. Dissociation constant (Kd) were calculated by fitting data from three different experiments and are shown as average ± standard deviation. See also Table S1.

Article Snippet: Fluorescence polarization binding data were plotted and fit using GraphPad Prism 6.

Techniques: Binding Assay, Fluorescence, Labeling, Standard Deviation, Residue