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Supplemental Table 1 Cancer gene mutations evaluated by the SNaPshot genotyping assay.

Mutation of this phenylalanine to a smaller residue such as valine, for example in the double mutation evaluated by Kiriakidou et al. [ 1], would create a void in the core that likely decreases the stability of the mid domain fold.

Gray rows indicate mutations evaluated as probably functionally damaging by our own knowledge-driven functional assessment.

As expected, all other mutations evaluated could not be detected by this method (Tables  1).

The potential effect of the N263D and N260D mutations was evaluated by homology modelling of the mutated sequences using the 3D structure of bovine complex III stored in PDB (1NTM) as a template.

Score variation in canonical splice-site use and potential activation of cryptic splice-sites in the presence of mutations were evaluated by analysis of exon and intron sequences localized in proximity to mutations using default settings (Supp. Table S1).

Additional mutations were evaluated by MAGE combined with amplicon sequencing, revealing role of rho, lrp, pykF, eno, and rpoB on tolerance and fitness in minimal medium.

The randomness of nonsynonymous mutations was evaluated by the runs.test function [ 67] in R [ 68].

Point mutations were evaluated by in silico analyses and an in vitro kinase activity test.

Differences in RNA, protein and mutations were evaluated by Student's t-test.

These mutations were evaluated by SIFT (Sorting intolerant from tolerant) [ 44] and PSSM (Position specific scoring matrix) [ 45] scores.