Fates of Sec, Tat, and YidC Translocases in Mitochondria and Other Eukaryotic Compartments

Formation of mitochondria by the conversion of a bacterial endosymbiont was a key moment in the evolution of eukaryotes. It was made possible by outsourcing the endosymbiont's genetic control to the host nucleus, while developing the import machinery for proteins synthesized on cytosolic ribosomes. The original protein export machines of the nascent organelle remained to be repurposed or were completely abandoned. This review follows the evolutionary fates of three prokaryotic inner membrane translocases Sec, Tat, and YidC. Homologs of all three translocases can still be found in current mitochondria, but with different importance for mitochondrial function. Although the mitochondrial YidC homolog, Oxa1, became an omnipresent independent insertase, the other two remained only sporadically present in mitochondria. Only a single substrate is known for the mitochondrial Tat and no function has yet been assigned for the mitochondrial Sec. Finally, this review compares these ancestral mitochondrial proteins with their paralogs operating in the plastids and the endomembrane system.

Automated summary

The formation of mitochondria by converting a bacterial endosymbiont was crucial in the evolution of eukaryotes. Evolutionary fates of prokaryotic inner membrane translocases Sec, Tat, and YidC in mitochondria differ, with YidC homolog being an omnipresent insertase, while Sec and Tat homologs are sporadically present. Comparisons of ancestral mitochondrial proteins with their paralogs in plastids and the endomembrane system are also made in this review.