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. 2023 Jun 26;299(8):104968. doi: 10.1016/j.jbc.2023.104968

Figure 2.

Figure 2

Point mutations lead to more closed conformation and DPC binding ability of yYkt6.A, ITC measurements of the interaction between DPC and yYkt6ΔC-T46L/Q57A mutant. B, FRET efficiency distribution profiles of WT yYkt6ΔC (blue), T46L/Q57A mutant (green), and T46L/Q57A/DPC (orange) systems. C, comparison of the populations of conformational states of WT yYkt6ΔC (blue), T46L/Q57A mutant (green), and T46L/Q57A/DPC systems (orange). Significance was determined by the two-tailed t test. ∗p < 0.05, ∗∗p < 0.01. D, fractionations of subcellular localizations of WT rYkt6, WT yYkt6, and yYkt6-T46L/Q57A mutant. The membrane/cytosolic ratios of WT Ykt6 and mutant were quantified. DPC, dodecylphosphocholine; ITC, isothermal titration calorimetry.