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. 2022 Aug 18;50(16):9534–9547. doi: 10.1093/nar/gkac696

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Isothermal titration calorimetry of RNA binding to LARP1 LaM domain. (A) ITC thermograms of LARP1 constructs binding to A₂₅. The RRM region is dispensable for full affinity binding. (B) Affinities of LARP1 fragments binding poly(A) and a TOP RNA. The LaM domain binds A₂₅ with high nanomolar affinity but only micromolar affinity for a 20-mer TOP RNA. (C) Affinities of different ligands confirms specificity of the LaM domain for the 3′ end of poly(A) RNA. See Supplementary Table S1 and Supplementary Figure S4 for a complete listing of the ITC experiments.