Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery |
| |
Authors: | Banci Lucia Bertini Ivano Ciofi-Baffoni Simone Boscaro Francesca Chatzi Afroditi Mikolajczyk Maciej Tokatlidis Kostas Winkelmann Julia |
| |
Affiliation: | Magnetic Resonance Center CERM, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy. banci@cerm.unifi.it |
| |
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 CX(2)C 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|