Targeting and maturation of Erv1/ALR in the mitochondrial intermembrane space

Kallergi, E. et al. (2012) Targeting and maturation of Erv1/ALR in the mitochondrial intermembrane space. ACS Chemical Biology, 7(4), pp. 707-714. (doi:10.1021/cb200485b)

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The interaction of Mia40 with Erv1/ALR is central to the oxidative protein folding in the intermembrane space of mitochondria (IMS) as Erv1/ALR oxidizes reduced Mia40 to restore its functional state. Here we address the role of Mia40 in the import and maturation of Erv1/ALR. The C-terminal FAD-binding domain of Erv1/ALR has an essential role in the import process by creating a transient intermolecular disulfide bond with Mia40. The action of Mia40 is selective for the formation of both intra and intersubunit structural disulfide bonds of Erv1/ALR, but the complete maturation process requires additional binding of FAD. Both of these events must follow a specific sequential order to allow Erv1/ALR to reach the fully functional state, illustrating a new paradigm for protein maturation in the IMS.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Tokatlidis, Professor Kostas
Authors: Kallergi, E., Andreadaki, M., Kritsiligkou, P., Katrakili, N., Pozidis, C., Tokatlidis, K., Banci, L., Bertini, I., Cefaro, C., Ciofi-Baffoni, S., Gajda, K., and Peruzzini, R.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:ACS Chemical Biology
ISSN (Online):1554-8937

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