ArticleMolecular biology of the cell2009
Reconstitution of the mia40-erv1 oxidative folding pathway for the small tim proteins.
Article in Molecular biology of the cell, 2009. 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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Who cites it
40 citing papers in PubMed, 66 citations in OpenAlex.
- ALR couples IMS redox and heme biosynthesis beyond the disulfide relay.Science advances · 2026Article
- Global mitochondrial connectivity map reveals the landscape of yeast functional assemblies and conserved protein communities.Nature communications · 2026Article
- Targeting prohibitins activates the ISR through DELE1-HRI by impairing protein import into the mitochondrial matrix.Cell death and differentiation · 2026Article
- Article
- Oxidative protein folding in the intermembrane space of human mitochondria.FEBS open bio · 2024Review
- The Interaction and Effect of a Small MitoBlock Library as Inhibitor of ALR Protein-Protein Interaction Pathway.International journal of molecular sciences · 2024Article
- Oxidation ofAntioxidants (Basel, Switzerland) · 2023Article
- The intermembrane space protein Mix23 is a novel stress-induced mitochondrial import factor.The Journal of biological chemistry · 2020Article
- Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria.The FEBS journal · 2020Article
- Kinetic characterisation of Erv1, a key component for protein import and folding in yeast mitochondria.The FEBS journal · 2020Article
- Cysteine Oxidations in Mitochondrial Membrane Proteins: The Case of VDAC Isoforms in Mammals.Frontiers in cell and developmental biology · 2020Review
- Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40.BMC biology · 2017Article
- Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space.Molecular biology of the cell · 2017Article
- Protein Translocation into the Intermembrane Space and Matrix of Mitochondria: Mechanisms and Driving Forces.Frontiers in molecular biosciences · 2017Review
- Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space.Cell and tissue research · 2017Review
- Article
- How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016Review
- Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway.The Journal of biological chemistry · 2015Article
- Mitochondrial Redox Dysfunction and Environmental Exposures.Antioxidants & redox signaling · 2015Review
- The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis.Accounts of chemical research · 2015Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into the mitochondrial intermembrane space. Here, we have reconstituted the oxidative folding pathway in vitro with Tim13 as a substrate and determined the midpoint potentials of Mia40 and Tim13. Specifically, Mia40 served as a direct oxidant of Tim13, and Erv1 was required to reoxidize Mia40. During oxidation, four electrons were transferred from Tim13 with the insertion of two disulfide bonds in succession. The extent of Tim13 oxidation was directly dependent on Mia40 concentration and independent of Erv1 concentration. Characterization of the midpoint potentials showed that electrons flowed from Tim13 with a more negative midpoint potential of -310 mV via Mia40 with an intermediate midpoint potential of -290 mV to the C130-C133 pair of Erv1 with a positive midpoint potential of -150 mV. Intermediary complexes between Tim13-Mia40 and Mia40-Erv1 were trapped. Last, mutating C133 of the catalytic C130-C133 pair or C30 of the shuttle C30-C33 pair in Erv1 abolished oxidation of Tim13, whereas mutating the cysteines in the redox-active CPC motif, but not the structural disulfide linkages of the CX(9)C motif of Mia40, prevented Tim13 oxidation. Thus, we demonstrate that Mia40, Erv1, and oxygen are the minimal machinery for Tim13 oxidation.
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