Skip to main content
. 2024 Jun 5;43(14):2979–3008. doi: 10.1038/s44318-024-00132-2

Figure 2. Native mass spectrometry analysis to detect lipid–protein interaction of Aac2.

Figure 2

(A) FlagAac2 affinity purified from WT mitochondria was associated with CATR and up to three CL molecules. (B) FlagAac2 affinity purified from crd1Δ mitochondria which lack CL did not co-purify other phospholipids. Insets in (A) and (B) show the fractional population of FlagAac2 relative to FlagAac2+CATR when immunoprecipitated from WT and crd1Δ mitochondria, respectively. Mean with SEM (n = 3–6: 3 biological replicates with 1–2 technical replicates). Significant differences as determined by Student’s t-test indicated (****p < 0.0001). (C) CL, PE, PG, or lyso-PC was added to FlagAac2 purified from crd1Δ mitochondria at the indicated concentrations. (D) Fractional population of FlagAac2, FlagAac2+CATR alone or associated with one to three CL molecules was determined for WT and Aac2 CL-binding mutants. Mean with SEM (n = 5–6: three biological replicates with 1–2 technical replicates). Significant differences were obtained by one-way ANOVA with Tukey’s multiple comparisons test (* vs. FlagAac2; † vs. FlagAac2+CATR + 1CL); */† p < 0.05, **/†† p < 0.01, ***/††† p < 0.001, ****/†††† p < 0.0001. Source data are available online for this figure.