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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Acknowledgments
This work was supported by intramural funds from IMBB-FORTH, the University of Crete and the European Social Fund and national resources (to KT). DS was supported by a PENED grant. We are grateful to members of our lab for comments.
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Sideris, D.P., Tokatlidis, K. (2010). Trapping Oxidative Folding Intermediates During Translocation to the Intermembrane Space of Mitochondria: In Vivo and In Vitro Studies. In: Economou, A. (eds) Protein Secretion. Methods in Molecular Biology, vol 619. Humana Press. https://doi.org/10.1007/978-1-60327-412-8_25
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DOI: https://doi.org/10.1007/978-1-60327-412-8_25
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