Key result
Evolutionarily unrelated mitochondrial protein import receptors can share the same substrate preferences, while receptors with the same domain structure can have different substrate specificity.
Why the study?
Targeting signals of imported mitochondrial proteins are conserved within eukaryotes, but the mitochondrial outer membrane receptors recognizing these signals are not.
The study illustrates how determinism and contingencies have shaped the evolution of mitochondrial import receptors.
Animal data on mitochondrial receptor evolution warrant no clinical changes; leaves open cardiac bioenergetics research in mammals.
Significance All mitochondria import most of their proteins from the cytosol. Even though the targeting signals of imported proteins are well conserved within eukaryotes, this is not the case for the mitochondrial outer membrane receptors that recognize these signals. Here we compare the substrate preferences of protein import receptors from the parasitic protozoans Trypanosoma brucei and Trichomonas vaginalis , as well as from yeast. Using biochemical and proteomic analysis, combined with complementation experiments, we show that evolutionarily unrelated receptors can share the same substrate preferences. Moreover, we provide evidence that receptors sharing the same domain structure and topology can have different substrate specificity. In summary, our study illustrates how determinism and contingencies have shaped the evolution of mitochondrial import receptors.
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Samuel et al. (2021) studied this question. Evolutionarily unrelated mitochondrial protein import receptors can share the same substrate preferences, while receptors with the same domain structure can have different substrate specificity.
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