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. 2019 Aug;25(8):1020–1037. doi: 10.1261/rna.070649.119

FIGURE 2.

FIGURE 2.

Cus2 and its UHM interact with the ULM of Hsh155 with high affinity in vitro. (A) Apparent equilibrium affinities (KA) of Hsh155 ULM (residues 95–109) binding to full-length Cus2 (isotherm B), D204K mutant Cus2 (isotherm C), Cus2 UHM (isotherm D, residues 177–269), or Tat-SF1 (isotherm E, residues 1–360). The KA’s of the ULM-containing SF3b1 region (SF3b1ULM, residues 190–344) or SF3b1 ULM5 (residues 333–351) binding Tat-SF1 were determined under matching conditions (Loerch et al. 2018) and are shown for comparison. Unpaired, two-tailed t-tests with Welch's correction: (*) P < 0.05, (**) P < 0.007. (B–E) Representative isotherms of three replicates for each of the indicated pairs of proteins or protein domains. The average fitted KA’s and SDs are plotted in A and given in Table 1.