Trapping Oxidative Folding Intermediates During Translocation to the Intermembrane Space of Mitochondria: In Vivo and In Vitro Studies
Abstract
The MIA40 pathway is a novel import pathway in mitochondria specific for cysteine-rich proteins of the intermembrane space (IMS). The newly synthesised precursors are trapped in the IMS by a disulfide relay mechanism that involves introduction of disulfides from the sulfhydryl oxidase Erv1 to the redox-regulated import receptor Mia40 and then on to the substrate. This thiol-disulfide exchange mechanism is essential for the import and oxidative folding of the incoming cysteine-rich substrate proteins. In this chapter we will describe the experimental methods that have been developed in order to study and characterise disulfide-trapped intermediates in yeast mitochondria.
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The FAD-containing sulfhydryl oxidase Erv1 maintains the intermembrane protein Mia40 in an oxidized form.
“A crucial component of this system is the FAD-containing sulfhydryl oxidase Erv1, which maintains the intermembrane protein Mia40 in an oxidized form (40, 391).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [391]
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- Authors
- Sideris, D. P., & Tokatlidis, K.
- Affiliations
- University of Crete (GR)
- ORCID
- Tokatlidis, Kostas
- Venue
- Methods in Molecular Biology
- Publisher
- Humana Press
- Published
- 2010
- Volume
- 619
- Pages
- 411-423
- ISSN
- 1064-3745 (ISSN-L)
- 1940-6029
- OpenAlex
- W2305731542
- Cited by
- 8
- References
- 37
- Citations by year
- 2020: 1 · 2017: 1 · 2016: 2 · 2015: 1
- FWCI
- 1.16
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Methods in molecular biology (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- mitochondrial intermembrane space, oxidative protein folding, Mia40, Erv1, sulfhydryl oxidase, thiol-disulfide exchange, cysteine-rich proteins, protein import, folding intermediates, yeast mitochondria
- MeSH terms
- Autoradiography, Electrophoresis, Electrophoresis, Polyacrylamide Gel, Intracellular Membranes, Mitochondria, Models, Biological, Oxidation-Reduction, Proteins, Yeasts, Protein Folding, Protein Transport
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