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Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p

By Ulrich Mühlenhoff, Jana Gerber, Nadine Richhardt and Roland Lill

Abstract

The mitochondrial proteins Isu1p and Isu2p play an essential role in the maturation of cellular iron–sulfur (Fe/S) proteins in eukaryotes. By radiolabelling of yeast cells with (55)Fe we demonstrate that Isu1p binds an oxygen-resistant non-chelatable Fe/S cluster providing in vivo evidence for a scaffolding function of Isu1p during Fe/S cluster assembly. Depletion of the cysteine desulfurase Nfs1p, the ferredoxin Yah1p or the yeast frataxin homologue Yfh1p by regulated gene expression causes a strong decrease in the de novo synthesis of Fe/S clusters on Isu1p. In contrast, depletion of the Hsp70 chaperone Ssq1p, its co-chaperone Jac1p or the glutaredoxin Grx5p markedly increased the amount of Fe/S clusters bound to Isu1p, even though these mitochondrial proteins are crucial for maturation of Fe/S proteins. Hence Ssq1p/Jac1p and Grx5p are required in a step after Fe/S cluster synthesis on Isu1p, for instance in dissociation of preassembled Fe/S clusters from Isu1p and/or their insertion into apoproteins. We propose a model that dissects Fe/S cluster biogenesis into two major steps and assigns its central components to one of these two steps

Topics: Articles
Publisher: Oxford University Press
Year: 2003
DOI identifier: 10.1093/emboj/cdg446
OAI identifier: oai:pubmedcentral.nih.gov:212715
Provided by: PubMed Central
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