ArticleThe Journal of biological chemistry2012
The mitochondrial oxidase assembly protein1 (Oxa1) insertase forms a membrane pore in lipid bilayers.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 45 citations in OpenAlex.
- Coenzyme Q10 Enhances Resilience of Mitochondrial-like Membranes Against Amyloidogenic Peptides.Membranes · 2025Article
- YidC fromBiomolecules · 2023Article
- NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes.International journal of molecular sciences · 2023Article
- Types and Functions of Mitoribosome-Specific Ribosomal Proteins across Eukaryotes.International journal of molecular sciences · 2022Review
- Extract from the Marine SeaweedMolecules (Basel, Switzerland) · 2021Article
- Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions.International journal of molecular sciences · 2021Review
- Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021Review
- Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.Scientific reports · 2020Article
- JASSY, a chloroplast outer membrane protein required for jasmonate biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Identification of Oxa1 Homologs Operating in the Eukaryotic Endoplasmic Reticulum.Cell reports · 2017Article
- Identification of new channels by systematic analysis of the mitochondrial outer membrane.The Journal of cell biology · 2017Article
- Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import.eLife · 2017Article
- The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology.The Journal of cell biology · 2017Article
- Ribosome-Associated Mba1 Escorts Cox2 from Insertion Machinery to Maturing Assembly Intermediates.Molecular and cellular biology · 2016Article
- Function of specialized regulatory proteins and signaling pathways in exercise-induced muscle mitochondrial biogenesis.Integrative medicine research · 2016Review
- Oms1 associates with cytochrome c oxidase assembly intermediates to stabilize newly synthesized Cox1.Molecular biology of the cell · 2016Article
- Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014Review
- Article
- A conserved cysteine residue of Bacillus subtilis SpoIIIJ is important for endospore development.PloS one · 2014Article
- The channel-forming Sym1 protein is transported by the TIM23 complex in a presequence-independent manner.Molecular and cellular biology · 2012Article
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inner membrane of mitochondria is especially protein-rich. To direct proteins into the inner membrane, translocases mediate transport and membrane insertion of precursor proteins. Although the majority of mitochondrial proteins are imported from the cytoplasm, core subunits of respiratory chain complexes are inserted into the inner membrane from the matrix. Oxa1, a conserved membrane protein, mediates the insertion of mitochondrion-encoded precursors into the inner mitochondrial membrane. The molecular mechanism by which Oxa1 mediates insertion of membrane spans, entailing the translocation of hydrophilic domains across the inner membrane, is still unknown. We investigated if Oxa1 could act as a protein-conducting channel for precursor transport. Using a biophysical approach, we show that Oxa1 can form a pore capable of accommodating a translocating protein segment. After purification and reconstitution, Oxa1 acts as a cation-selective channel that specifically responds to mitochondrial export signals. The aqueous pore formed by Oxa1 displays highly dynamic characteristics with a restriction zone diameter between 0.6 and 2 nm, which would suffice for polypeptide translocation across the membrane. Single channel analyses revealed four discrete channels per active unit, suggesting that the Oxa1 complex forms several cooperative hydrophilic pores in the inner membrane. Hence, Oxa1 behaves as a pore-forming translocase that is regulated in a membrane potential and substrate-dependent manner.
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