Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery

Banci, L., Bertini, I., Ciofi-Baffoni, S., Boscaro, F., Chatzi, A., Mikolajczyk, M., Tokatlidis, K. and Winkelmann, J. (2011) Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery. Chemistry and Biology, 18(6), pp. 794-804. (doi:10.1016/j.chembiol.2011.03.015) (PMID:21700214)

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Abstract

Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded linker; (2), the C-terminal domain binds a [2Fe-2S] cluster through a previously unknown cysteine binding motif in Fe/S proteins; (3), Mia40 specifically introduces two disulfide bonds in a twin CX2C motif of the C-terminal domain; (4), anamorsin and Mia40 interact through an intermolecular disulfide-bonded intermediate; and (5), anamorsin is imported into mitochondria. Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Tokatlidis, Professor Kostas and Chatzi, Ms Afroditi
Authors: Banci, L., Bertini, I., Ciofi-Baffoni, S., Boscaro, F., Chatzi, A., Mikolajczyk, M., Tokatlidis, K., and Winkelmann, J.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Chemistry and Biology
Publisher:Cell Press
ISSN:1074-5521
ISSN (Online):1879-1301
Published Online:23 June 2011

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