ArticleMolecular biology of the cell2007
Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 95 citations in OpenAlex.
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- Protein insertion into the inner membrane of mitochondria: routes and mechanisms.FEBS open bio · 2024Review
- PHB3 Is Required for the Assembly and Activity of Mitochondrial ATP Synthase in Arabidopsis.International journal of molecular sciences · 2023Article
- Assembly-dependent translation of subunits 6 (Atp6) and 9 (Atp9) of ATP synthase in yeast mitochondria.Genetics · 2022Article
- The ER membrane complex (EMC) can functionally replace the Oxa1 insertase in mitochondria.PLoS biology · 2022Article
- The mitospecific domain of Mrp7 (bL27) supports mitochondrial translation during fermentation and is required for effective adaptation to respiration.Molecular biology of the cell · 2022Article
- Functions of CytochromeInternational journal of molecular sciences · 2020Review
- Mitochondrial OXPHOS Biogenesis: Co-Regulation of Protein Synthesis, Import, and Assembly Pathways.International journal of molecular sciences · 2020Review
- Atco, a yeast mitochondrial complex of Atp9 and Cox6, is an assembly intermediate of the ATP synthase.PloS one · 2020Article
- Current understanding of male sterility systems in vegetable Brassicas and their exploitation in hybrid breeding.Plant reproduction · 2019Review
- The WRB Subunit of the Get3 Receptor is Required for the Correct Integration of its Partner CAML into the ER.Scientific reports · 2019Article
- Article
- Recombination Events Involving the atp9 Gene Are Associated with Male Sterility of CMS PET2 in Sunflower.International journal of molecular sciences · 2018Article
- Plant Mitochondrial Inner Membrane Protein Insertion.International journal of molecular sciences · 2018Review
- MrpL35, a mitospecific component of mitoribosomes, plays a key role in cytochromeMolecular biology of the cell · 2017Article
- Mutational Analysis of the QRRQ Motif in the Yeast Hig1 Type 2 Protein Rcf1 Reveals a Regulatory Role for the CytochromeThe Journal of biological chemistry · 2017Article
- Comparative miRNAs analysis of Two contrasting broccoli inbred lines with divergent head-forming capacity under temperature stress.BMC genomics · 2015Article
- A YidC-like Protein in the Archaeal Plasma Membrane.Structure (London, England : 1993) · 2015Article
- The Arabidopsis protein CONSERVED ONLY IN THE GREEN LINEAGE160 promotes the assembly of the membranous part of the chloroplast ATP synthase.Plant physiology · 2014Article
- A radiation hybrid map of chromosome 1D reveals synteny conservation at a wheat speciation locus.Functional & integrative genomics · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The yeast Oxa1 protein is involved in the biogenesis of the mitochondrial oxidative phosphorylation (OXPHOS) machinery. The involvement of Oxa1 in the assembly of the cytochrome oxidase (COX) complex, where it facilitates the cotranslational membrane insertion of mitochondrially encoded COX subunits, is well documented. In this study we have addressed the role of Oxa1, and its sequence-related protein Cox18/Oxa2, in the biogenesis of the F(1)F(o)-ATP synthase complex. We demonstrate that Oxa1, but not Cox18/Oxa2, directly supports the assembly of the membrane embedded F(o)-sector of the ATP synthase. Oxa1 was found to physically interact with newly synthesized mitochondrially encoded Atp9 protein in a posttranslational manner and in a manner that is not dependent on the C-terminal, matrix-localized region of Oxa1. The stable manner of the Atp9-Oxa1 interaction is in contrast to the cotranslational and transient interaction previously observed for the mitochondrially encoded COX subunits with Oxa1. In the absence of Oxa1, Atp9 was observed to assemble into an oligomeric complex containing F(1)-subunits, but its further assembly with subunit 6 (Atp6) of the F(o)-sector was perturbed. We propose that by directly interacting with newly synthesized Atp9 in a posttranslational manner, Oxa1 is required to maintain the assembly competence of the Atp9-F(1)-subcomplex for its association with Atp6.
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