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Figure 1. Substitutions of pore-lining residues of Tim23 reduce the channel’s ion selectivity and lead to a growth defect in S. cerevisiae. ; (A) Helical wheel projection of amino acid residues 150–163 of the second transmembrane helix of Tim23. Highlighted residues in green indicate near 100% conservation. Colored hemispheres indicates polar/apolar facing regions of helix. Residues mutated in this study are circled in red. (B) S. cerevisiae strains with chromosomal deletion of the TIM23 gene, complemented by a plasmid carrying both URA3 and TIM23 gene, were transformed with plasmids containing wild type TIM23 or mutants and tested for viability after plasmid loss on 5-FOA containing medium. (C) tim23Δ yeast cells with plasmids containing wild type TIM23 or pore-lining mutants were grown on fermentable (left) or non-fermentable (right) media at 37°C. Strains WT to A156L were grown on a single plate each for glucose and glycerol respectively. (D) Electrophysiological current-voltage (I–V) curves were recorded at asymmetrical buffer conditions with 12.5-fold KCl gradient for Tim23 (grey) or Tim23G153A (red) to determine reversal potentials. (E) Reversal potentials Urev were experimentally determined for wild type Tim23 and all mutants by independent triplicates at asymmetrical buffer conditions, the ion selectivity was calculated from the mean reversal potential following the Goldman-Hodgkin-Katz equation. Errors represent standard deviation.

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