Extended Data Fig, 8: Characterization of b₂-DHFR–HB-construct overexpressing mutants.

a, Degradation of the b₂–DHFR–HB precursor by proteinase K in ubx2∆ mitochondria. The data are representative of seven independent experiments. b, The TOM–TIM23–preprotein supercomplex⁴³ on BN–PAGE in cell extracts from wild-type and ubx2∆ strains that express b₂∆–DHFR–HB. The data are representative of three independent experiments. Quantification of the TOM–TIM23–preprotein supercomplex. The amount of the TOM–TIM23–preprotein supercomplex in wild-type cells was set to 100% (control). Mean ± s.e.m. (n = 3). c, Binding of Ubx2 to the TOM complex on BN–PAGE in wild-type and ubx2∆ mitochondria from strains that express b₂–DHFR–HB or b₂∆–DHFR–HB. The data are representative of three (b₂–DHFR–HB) or five (b₂∆–DHFR–HB) independent experiments. Quantification of the Ubx2–TOM complex in cell extracts. The amount of Ubx2–TOM complex in wild-type cells was set to 100% (control). Mean ± s.e.m. (n = 3 for b₂–DHFR–HB; n = 5 for b₂∆–DHFR–HB).