%0 Journal Article %1 pusnikMitochondrialPreproteinTranslocase2011 %A Pusnik, Mascha %A Schmidt, Oliver %A Perry, Andrew J. %A Oeljeklaus, Silke %A Niemann, Moritz %A Warscheid, Bettina %A Lithgow, Trevor %A Meisinger, Chris %A Schneider, André %C England %D 2011 %J Current biology : CB %K Anion Bacterial Cells/metabolism,Evolution Channels/genetics/metabolism Conformation,Protein Dehydrogenase/genetics/metabolism,to_read,Trypanosoma Fusion Membrane Membranes/*metabolism,Protein Molecular,Methotrexate/pharmacology,Mitochondrial Outer Proteins,Bacterial Proteins,Eukaryotic Proteins/chemistry/genetics/*metabolism,Mitochondrial Proteins/genetics/metabolism,Escherichia Proteins/genetics/metabolism,Saccharomyces Proteins/metabolism,Tetrahydrofolate Transport Transport,Recombinant brucei brucei/drug cerevisiae coli effects/genetics/*metabolism,Voltage-Dependent %N 20 %P 1738--1743 %R 10.1016/j.cub.2011.08.060 %T Mitochondrial Preprotein Translocase of Trypanosomatids Has a Bacterial Origin. %V 21 %X Mitochondria are found in all eukaryotic cells and derive from a bacterial endosymbiont 1, 2. The evolution of a protein import system was a prerequisite for the conversion of the endosymbiont into a true organelle. Tom40, the essential component of the protein translocase of the outer membrane, is conserved in mitochondria of almost all eukaryotes but lacks bacterial orthologs 3-6. It serves as the gateway through which all mitochondrial proteins are imported. The parasitic protozoa Trypanosoma brucei and its relatives do not have a Tom40-like protein, which raises the question of how proteins are imported by their mitochondria 7, 8. Using a combination of bioinformatics and in vivo and in vitro studies, we have discovered that T. brucei likely employs a different import channel, termed ATOM (archaic translocase of the outer mitochondrial membrane). ATOM mediates the import of nuclear-encoded proteins into mitochondria and is essential for viability of trypanosomes. It is not related to Tom40 but is instead an ortholog of a subgroup of the Omp85 protein superfamily that is involved in membrane translocation and insertion of bacterial outer membrane proteins 9. This suggests that the protein import channel in trypanosomes is a relic of an archaic protein transport system that was operational in the ancestor of all eukaryotes.

@article{pusnikMitochondrialPreproteinTranslocase2011, abstract = {Mitochondria are found in all eukaryotic cells and derive from a bacterial endosymbiont [1, 2]. The evolution of a protein import system was a prerequisite for the conversion of the endosymbiont into a true organelle. Tom40, the essential component of the protein translocase of the outer membrane, is conserved in mitochondria of almost all eukaryotes but lacks bacterial orthologs [3-6]. It serves as the gateway through which all mitochondrial proteins are imported. The parasitic protozoa Trypanosoma brucei and its relatives do not have a Tom40-like protein, which raises the question of how proteins are imported by their mitochondria [7, 8]. Using a combination of bioinformatics and in vivo and in vitro studies, we have discovered that T. brucei likely employs a different import channel, termed ATOM (archaic translocase of the outer mitochondrial membrane). ATOM mediates the import of nuclear-encoded proteins into mitochondria and is essential for viability of trypanosomes. It is not related to Tom40 but is instead an ortholog of a subgroup of the Omp85 protein superfamily that is involved in membrane translocation and insertion of bacterial outer membrane proteins [9]. This suggests that the protein import channel in trypanosomes is a relic of an archaic protein transport system that was operational in the ancestor of all eukaryotes.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {England}, author = {Pusnik, Mascha and Schmidt, Oliver and Perry, Andrew J. and Oeljeklaus, Silke and Niemann, Moritz and Warscheid, Bettina and Lithgow, Trevor and Meisinger, Chris and Schneider, Andr{\'e}}, biburl = {https://www.bibsonomy.org/bibtex/2faff4a7e02621404955d17c276d843d7/warscheidlab}, copyright = {Copyright {\copyright} 2011 Elsevier Ltd. All rights reserved.}, doi = {10.1016/j.cub.2011.08.060}, interhash = {def716bcdb339ce1995ced54fa3aa458}, intrahash = {faff4a7e02621404955d17c276d843d7}, issn = {1879-0445 0960-9822}, journal = {Current biology : CB}, keywords = {Anion Bacterial Cells/metabolism,Evolution Channels/genetics/metabolism Conformation,Protein Dehydrogenase/genetics/metabolism,to_read,Trypanosoma Fusion Membrane Membranes/*metabolism,Protein Molecular,Methotrexate/pharmacology,Mitochondrial Outer Proteins,Bacterial Proteins,Eukaryotic Proteins/chemistry/genetics/*metabolism,Mitochondrial Proteins/genetics/metabolism,Escherichia Proteins/genetics/metabolism,Saccharomyces Proteins/metabolism,Tetrahydrofolate Transport Transport,Recombinant brucei brucei/drug cerevisiae coli effects/genetics/*metabolism,Voltage-Dependent}, langid = {english}, month = oct, number = 20, pages = {1738--1743}, pmid = {22000100}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Mitochondrial Preprotein Translocase of Trypanosomatids Has a Bacterial Origin.}, volume = 21, year = 2011 }