Fig. 3: OxPhos complexes are structurally compromised in the absence of MRM2 due to impaired mitochondrial translation. | Nature Communications

Fig. 3: OxPhos complexes are structurally compromised in the absence of MRM2 due to impaired mitochondrial translation.

From: A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit

Fig. 3

a Quantitative mass spectrometric analysis of the mitochondrial proteome of MRM2 knock-out and parental control cells. Datapoints corresponding to structural components (circles) or assembly factors (diamonds) of OxPhos complexes, and other proteins of interest are highlighted. b Metabolic labelling of de novo translated mitochondrial proteins (top, quantification in Supplementary Fig. 2a, b) and immunoblotting assessment of steady-state levels of mitochondrial proteins (bottom). Molecular weights of protein standards are presented in kDa to the right of each blot; an asterisk marks a band generated in a previous blot for TOM22. Coomassie brilliant blue (CBB) staining is shown as a loading indicator. This experiment was replicated three times with similar results. c Occupancy of mitochondrial transcripts by mitochondrial ribosomes. Experimental values and mean are shown. Data from parental and MRM2 knock-out (KO) cell lines are represented in black and red, respectively. Source data are provided as a Source Data file.

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