Protein oxidation in the intermembrane space of mitochondria is substrate-specific rather than general

Authors:

Valentina Peleh1, Jan Riemer2, Andrew Dancis3 and Johannes M. Herrmann1
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Affiliations:

1 Cell Biology, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13, 67663 Kaiserslautern, Germany.

2 Cellular Biochemistry, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13, 67663 Kaiserslautern, Germany.

3 Division of Hematology-Oncology, Department of Medicine, University of Pennsylvania, 421 Curie Blvd., Philadelphia PA 19104, USA.

Keywords: 

cysteine oxidation; disulfide bonds; Dre2; Fe-S clusters; Mia40; mitochondria; oxidative protein folding.

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Corresponding Author(s):

Johannes M. Herrmann, Cell Biology, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13; 67663 Kaiserslautern, Germany hannes.herrmann@biologie.uni-kl.de

Conflict of interest statement:

The authors declare no conflict of interest.

Please cite this article as:

Valentina Peleh, Jan Riemer, Andrew Dancis and Johannes M. Herrmann (2014). Protein oxidation in the intermembrane space of mitochondria is substrate-specific rather than general. Microbial Cell 1(3): 81-93.

© Peleh et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.

Abstract:

In most cellular compartments cysteine residues are predominantly reduced. However, in the bacterial periplasm, the ER and the mitochondrial intermembrane space (IMS), sulfhydryl oxidases catalyze the formation of disulfide bonds. Nevertheless, many IMS proteins contain reduced cysteines that participate in binding metal- or heme-cofactors. In this study, we addressed the substrate specificity of the mitochondrial protein oxidation machinery. Dre2 is a cysteine-rich protein that is located in the cytosol. A large fraction of Dre2 bound to the cytosolic side of the outer membrane of mitochondria. Even when Dre2 is artificially targeted to the IMS, its cysteine residues remain in the reduced state. This indicates that protein oxidation in the IMS of mitochondria is not a consequence of the apparent oxidizing environment in this compartment but rather is substrate-specific and determined by the presence of Mia40-binding sites.

doi: 10.15698/mic2014.01.130
Volume 1, pp. 81 to 93, published 03/03/2014.