Complexome profiling of mitochondrial protein complexes from patients with mutations in either DNAJC30 or ACAD9 compared to an age and gender matched control

We identified the chaperone DNAJC30 as an important factor to maintain NADH:ubiquinone oxidoreductase (complex I) activity. To determine whether DNAJC30 acts as a complex I assembly factor, we used complexome profiling to compare the molecular consequences of DNAJC30 mutations in contrast to defects in the complex I assembly factor ACAD9.