Fig. 6: mtHsp70 controls the assembly of Atp5.
From: The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase
a [35S]Atp4, [35S]Atp5, or [35S]Atp14 were imported into wild-type (WT) and ssc1-62 mitochondria from non-stressed cells for the indicated time period. Non-imported precursor proteins were removed by proteinase K (Prot. K). In control reactions, the membrane potential (Δψ) was depleted. Samples were analysed via SDS-PAGE and autoradiography. p, precursor, m, mature band. b Upper panels, [35S]Atp5, [35S]Atp4 or [35S]Atp14 were imported into WT and ssc1-62 mitochondria from non-stressed cells for the indicated time periods. In control reactions, the membrane potential (Δψ) was depleted. Samples were analysed via blue native electrophoresis and autoradiography. VD, dimer of the ATP synthase, VM, monomer of the ATP synthase. Lower panels: Quantification of Atp5, Atp4 or Atp14 assembled into the dimer of the ATP synthase. Depicted are mean values ± SEM of 3 independent experiments for Atp4 and Atp14, and mean values ± SEM of 4 independent experiments for Atp5. The amounts of Atp5, Atp4 or Atp14 assembled into the ATP synthase dimer in WT mitochondria at the longest import time point were set to 100% (control). Source data are provided as a Source Data file. c, d [35S]Atp5 (c) or [35S]Atp5G183A (d) were imported into WT and ssc1-62 mitochondria isolated from non-stressed cells for the indicated time periods. In control reactions, the membrane potential (Δψ) was depleted. Samples were analysed via blue native electrophoresis and autoradiography. VD, dimer of the ATP synthase, VM, monomer of the ATP synthase. d Right panel: quantification of Atp5G183A assembled into the monomer and dimer of the ATP synthase. Depicted are mean values ± SEM of 4 independent experiments. The amounts of assembled Atp5G183A in WT mitochondria at the longest import time point were set to 100% (control). Source data are provided as a Source Data file.
