Fig. 3: The C-terminal intrinsically disordered region boosts the RNA-binding capacity of DCP2. | Nature Communications

Fig. 3: The C-terminal intrinsically disordered region boosts the RNA-binding capacity of DCP2.

From: Conserved and divergent features of human mRNA decapping revealed by biochemical reconstitution

Fig. 3: The C-terminal intrinsically disordered region boosts the RNA-binding capacity of DCP2.The alternative text for this image may have been generated using AI.

a Left, crystal structure of the Sp Dcp2 Nudix domain (PDB 2QKM) with the four lysines that mediate Box B RNA binding (Lys230, Lys231, Lys234, Lys235) shown as blue sticks. Right, AlphaFold model of the human DCP2 Nudix domain (AF-Q8IU60-F1) with the residues occupying the equivalent positions (Arg236, Asp237, Ser240, Arg241) rendered as sticks. Backbones are colored slate in both views. b Electrophoretic mobility-shift assays (EMSA) were performed with a 5′-labeled Rrp41 2 × DE RNA probe and increasing concentrations (0, 0.25, 1.0 µM) of the indicated DCP2 constructs. Full-length Sp Dcp2(1–504) and human DCP2 produce robust shifts, whereas their catalytic cores, lacking most or all of the C-terminal IDR, Sp Dcp2(1–242) and Hs DCP2(1–245), display markedly reduced binding. The gel shown is representative of three independent experiments.

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