ArticleMolecular biology of the cell2012
An essential novel component of the noncanonical mitochondrial outer membrane protein import system of trypanosomatids.
Article in Molecular biology of the cell, 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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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Evolution and Adaptation of the Mitochondrial Protein Import Machinery in Parasitic Protists: Beyond the Canonical TOM Complex.International journal of molecular sciences · 2026Review
- Disruption of GxxxG motifs in pATOM36 impairs biogenesis of the mitochondrial protein translocase of the outer membrane in Trypanosoma brucei.The Journal of biological chemistry · 2026Article
- The segregation of organelles and organellar genomes across eukaryotic biology.Biochemical Society transactions · 2026Review
- Assembly of the mitochondrial outer membrane module of the trypanosomal tripartite attachment complex.PLoS pathogens · 2025Article
- Plant-derived products as anti-leishmanials which target mitochondria: a review.Expert reviews in molecular medicine · 2025Review
- A Msp1-containing complex removes orphaned proteins in the mitochondrial outer membrane ofLife science alliance · 2023Article
- Is the mitochondrion a promising drug target in trypanosomatids?Memorias do Instituto Oswaldo Cruz · 2022Article
- Mitochondrial protein import in trypanosomatids: Variations on a theme or fundamentally different?PLoS pathogens · 2018Review
- Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes.eLife · 2018Article
- Biogenesis of the mitochondrial DNA inheritance machinery in the mitochondrial outer membrane of Trypanosoma brucei.PLoS pathogens · 2017Article
- Biogenesis of a Mitochondrial Outer Membrane Protein inThe Journal of biological chemistry · 2017Article
- Characterization of a novel β-barrel protein (AtOM47) from the mitochondrial outer membrane of Arabidopsis thaliana.Journal of experimental botany · 2016Article
- The Import of Proteins into the Mitochondrion of Toxoplasma gondii.The Journal of biological chemistry · 2016Article
- Novel Hydrogenosomes in the Microaerophilic Jakobid Stygiella incarcerata.Molecular biology and evolution · 2016Article
- Outer membrane protein functions as integrator of protein import and DNA inheritance in mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives.BMC genomics · 2016Article
- Mitochondrial protein import receptors in Kinetoplastids reveal convergent evolution over large phylogenetic distances.Nature communications · 2015Article
- Functional complementation analyses reveal that the single PRAT family protein of trypanosoma brucei is a divergent homolog of Tim17 in saccharomyces cerevisiae.Eukaryotic cell · 2015Article
- 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
- Trypanosome alternative oxidase possesses both an N-terminal and internal mitochondrial targeting signal.Eukaryotic cell · 2014Article
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Authors and funding
10 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial outer membrane protein Tom40 is the general entry gate for imported proteins in essentially all eukaryotes. Trypanosomatids lack Tom40, however, and use instead a protein termed the archaic translocase of the outer mitochondrial membrane (ATOM). Here we report the discovery of pATOM36, a novel essential component of the trypanosomal outer membrane protein import system that interacts with ATOM. pATOM36 is not related to known Tom proteins from other organisms and mediates the import of matrix proteins. However, there is a group of precursor proteins whose import is independent of pATOM36. Domain-swapping experiments indicate that the N-terminal presequence-containing domain of the substrate proteins at least in part determines the dependence on pATOM36. Secondary structure profiling suggests that pATOM36 is composed largely of α-helices and its assembly into the outer membrane is independent of the sorting and assembly machinery complex. Taken together, these results show that pATOM36 is a novel component associated with the ATOM complex that promotes the import of a subpopulation of proteins into the mitochondrial matrix.
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