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.
CITATION STYLE
Sideris, D. P., & Tokatlidis, K. (2010). Trapping oxidative folding intermediates during translocation to the intermembrane space of mitochondria: in vivo and in vitro studies. Methods in Molecular Biology (Clifton, N.J.), 619, 411–423. https://doi.org/10.1007/978-1-60327-412-8_25
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