ArticleThe Journal of biological chemistry2012
Bacterial origin of a mitochondrial outer membrane protein translocase: new perspectives from comparative single channel electrophysiology.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 36 citations in OpenAlex.
- Revealing the single-channel characteristics of OprD (OccAB1) porins from hospital strains of Acinetobacter baumannii.European biophysics journal : EBJ · 2023Article
- Is the mitochondrion a promising drug target in trypanosomatids?Memorias do Instituto Oswaldo Cruz · 2022Article
- Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase.International journal of molecular sciences · 2021Review
- Novel IM-associated protein Tim54 plays a role in the mitochondrial import of internal signal-containing proteins in Trypanosoma brucei.Biology of the cell · 2021Article
- Fake It 'Till You Make It-The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics.International journal of molecular sciences · 2020Review
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
- tRNA import across the mitochondrial inner membrane in T. brucei requires TIM subunits but is independent of protein import.Nucleic acids research · 2020Article
- The single CCA-adding enzyme ofThe Journal of biological chemistry · 2020Article
- Divergent Small Tim Homologues Are Associated with TbTim17 and Critical for the Biogenesis of TbTim17 Protein Complexes inmSphere · 2018Article
- Biogenesis of the mitochondrial DNA inheritance machinery in the mitochondrial outer membrane of Trypanosoma brucei.PLoS pathogens · 2017Article
- tRNAs and proteins use the same import channel for translocation across the mitochondrial outer membrane of trypanosomes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Peptide translocation across MOMP, the major outer membrane channel fromBiochemistry and biophysics reports · 2017Article
- Biogenesis of a Mitochondrial Outer Membrane Protein inThe Journal of biological chemistry · 2017Article
- Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids.Journal of bioenergetics and biomembranes · 2017Review
- Mitochondrial protein import - Functional analysis of the highly diverged Tom22 orthologue of Trypanosoma brucei.Scientific reports · 2017Article
- Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10.Nature communications · 2016Article
- Mitochondrial protein import receptors in Kinetoplastids reveal convergent evolution over large phylogenetic distances.Nature communications · 2015Article
- Protein targeting and transport as a necessary consequence of increased cellular complexity.Cold Spring Harbor perspectives in biology · 2014Review
- Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mitochondrial outer membrane proteome of Trypanosoma brucei reveals novel factors required to maintain mitochondrial morphology.Molecular & cellular proteomics : MCP · 2013Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondria are of bacterial ancestry and have to import most of their proteins from the cytosol. This process is mediated by Tom40, an essential protein that forms the protein-translocating pore in the outer mitochondrial membrane. Tom40 is conserved in virtually all eukaryotes, but its evolutionary origin is unclear because bacterial orthologues have not been identified so far. Recently, it was shown that the parasitic protozoon Trypanosoma brucei lacks a conventional Tom40 and instead employs the archaic translocase of the outer mitochondrial membrane (ATOM), a protein that shows similarities to both eukaryotic Tom40 and bacterial protein translocases of the Omp85 family. Here we present electrophysiological single channel data showing that ATOM forms a hydrophilic pore of large conductance and high open probability. Moreover, ATOM channels exhibit a preference for the passage of cationic molecules consistent with the idea that it may translocate unfolded proteins targeted by positively charged N-terminal presequences. This is further supported by the fact that the addition of a presequence peptide induces transient pore closure. An in-depth comparison of these single channel properties with those of other protein translocases reveals that ATOM closely resembles bacterial-type protein export channels rather than eukaryotic Tom40. Our results support the idea that ATOM represents an evolutionary intermediate between a bacterial Omp85-like protein export machinery and the conventional Tom40 that is found in mitochondria of other eukaryotes.
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