ArticleMolecular biology of the cell2012
In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins.
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 27 papers.
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Who cites it
27 citing papers in PubMed, 47 citations in OpenAlex.
- CHCHD4 Oxidoreductase Activity: A Comprehensive Analysis of the Molecular, Functional, and Structural Properties of Its Redox-Regulated Substrates.Molecules (Basel, Switzerland) · 2025Review
- Oxidation ofAntioxidants (Basel, Switzerland) · 2023Article
- The Orf9b protein of SARS-CoV-2 modulates mitochondrial protein biogenesis.The Journal of cell biology · 2023Article
- CHCHD4 (MIA40) and the mitochondrial disulfide relay system.Biochemical Society transactions · 2021Review
- Loss of the Mia40a oxidoreductase leads to hepato-pancreatic insufficiency in zebrafish.PLoS genetics · 2018Article
- Determinants of the cytosolic turnover of mitochondrial intermembrane space proteins.BMC biology · 2018Article
- Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40.BMC biology · 2017Article
- Enzymatic improvement of mitochondrial thiol oxidase Erv1 for oxidized glutathione fermentation by Saccharomyces cerevisiae.Microbial cell factories · 2017Article
- The presence of disulfide bonds reveals an evolutionarily conserved mechanism involved in mitochondrial protein translocase assembly.Scientific reports · 2016Article
- How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016Review
- The Oxidation Status of Mic19 Regulates MICOS Assembly.Molecular and cellular biology · 2015Article
- Article
- Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway.The Journal of biological chemistry · 2015Article
- The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis.Accounts of chemical research · 2015Article
- Retro-translocation of mitochondrial intermembrane space proteins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mitochondrial translocation of APE1 relies on the MIA pathway.Nucleic acids research · 2015Article
- Cox17 Protein Is an Auxiliary Factor Involved in the Control of the Mitochondrial Contact Site and Cristae Organizing System.The Journal of biological chemistry · 2015Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.Molecular biology of the cell · 2015Article
- A discrete pathway for the transfer of intermembrane space proteins across the outer membrane of mitochondria.Molecular biology of the cell · 2014Article
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins. However, the substrates of the MIA typically contain two disulfide bonds. It was unclear what the mechanisms are that ensure that proteins are released from Mia40 in a fully oxidized form. In this work, we dissect the stage of the oxidative folding relay, in which Mia40 binds to its substrate. We identify dynamics of the Mia40-substrate intermediate complex. Our experiments performed in a native environment, both in organello and in vivo, show that Erv1 directly participates in Mia40-substrate complex dynamics by forming a ternary complex. Thus Mia40 in cooperation with Erv1 promotes the formation of two disulfide bonds in the substrate protein, ensuring the efficiency of oxidative folding in the intermembrane space of mitochondria.
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