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. 2016 Sep;22(9):1360–1372. doi: 10.1261/rna.057315.116

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© 2016 Wurm et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article, published in RNA, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 4. — Fluorescence anisotropy measurements to extract the K_D for the interaction between Dcp1 and Edc1 (A), Dcp1:Dcp2_RD and Edc1 (B), and Dcp1:Dcp2_RD+CD and Edc1 (C). The interaction between Edc1 and the decapping complex appears to be mediated through contacts with Dcp1 and the regulatory domain of Dcp2. (D) Fluorescence anisotropy competition experiments. The truncation of Edc1 and the removal of the YAG motif have no influence on the interaction between the activator and the enzyme. (E) Fluorescence anisotropy measurements to extract the affinity between capped RNA and different version of the Edc1:Dcp1:Dcp2_{RD + CD}. The YAG motif in Edc1 appears to play an important role in the recognition of the capped RNA.