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)

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Publisher's URL: http://dx.doi.org/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 > Institute of Molecular Cell and Systems Biology
Publisher:Humana Press
ISSN:1064-3745
ISBN:9781603271677

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