The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface

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.