Article abstract
Nature Chemical Biology 3, 278 - 286 (2007)
Published online: 1 April 2007 | doi:10.1038/nchembio872
The Cfd1–Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
Daili J A Netz1, Antonio J Pierik1, Martin Stümpfig1, Ulrich Mühlenhoff1 & Roland Lill1
Abstract
Biogenesis of iron-sulfur ([Fe-S]) proteins in eukaryotes requires the function of complex proteinaceous machineries in both mitochondria and cytosol. In contrast to the mitochondrial pathway, little is known about [Fe-S] protein assembly in the cytosol. So far, four highly conserved proteins (Cfd1, Nbp35, Nar1 and Cia1) have been identified as members of the cytosolic [Fe-S] protein assembly machinery, but their molecular function is unresolved. Using in vivo and in vitro approaches, we found that the soluble P-loop NTPases Cfd1 and Nbp35 form a complex and bind up to three [4Fe-4S] clusters, one at the N terminus of Nbp35 and one each at a new C-terminal cysteine-rich motif present in both proteins. These labile [Fe-S] clusters can be rapidly transferred and incorporated into target [Fe-S] apoproteins in a Nar1- and Cia1-dependent fashion. Our data suggest that the Cfd1–Nbp35 complex functions as a novel scaffold for [Fe-S] cluster assembly in the eukaryotic cytosol.
- Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, D-35033 Marburg, Germany.
Correspondence to: Roland Lill1 e-mail: lill@staff.uni-marburg.de
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