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Mutagenesis of key LaM residues for poly(A) binding. (A) Sequence alignment of LaM domains with the amino acid residues selected for mutagenesis. (B) ITC results reveal reduced affinity of the Q333A, Y336A and F348A LaM mutants, and complete loss of binding for Q333A/F348A and Y336A/F348A double mutants. The mutations also prevented binding of A25 RNA in the context of the larger LARP1 fragment (323-509). (C) ITC thermograms of Q333A and Q333A/F348A mutants.
