Trapping oxidative folding intermediates during translocation to the intermembrane space of mitochondria: in vivo and in vitro studies

Sideris, D.P. and Tokatlidis, K. (2010) Trapping oxidative folding intermediates during translocation to the intermembrane space of mitochondria: in vivo and in vitro studies. In: Economou, A. (ed.) Protein Secretion. Series: Methods in molecular biology (619). Humana Press: New York, NY, USA, pp. 411-423. ISBN 9781603271677 (doi: 10.1007/978-1-60327-412-8_25)

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.

• Item Type: Book Sections
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Tokatlidis, Professor Kostas
• Authors: Sideris, D.P., and Tokatlidis, K.
• College/School: College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
• Publisher: Humana Press
• ISSN: 1064-3745
• ISBN: 9781603271677