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Human Molecular Genetics, 2002, Vol. 11, No. 21 2635-2643
© 2002 Oxford University Press

A non-essential function for yeast frataxin in iron–sulfur cluster assembly

Geoffrey Duby1, Françoise Foury1,*, Anna Ramazzotti1, Johannes Herrmann2 and Thomas Lutz2

1Unité de Biochimie Physiologique, Université Catholique de Louvain, Croix du Sud 2-20, B-1348 Louvain-la-Neuve, Belgium and 2lnstitut für Physiologische Chemie der Universität München, Butenandtstrasse 5, 81377 München, 80336, Germany

Received June 14, 2002; Accepted July 30, 2002

Friedreich's ataxia is caused by a deficit in frataxin, a small mitochondrial protein of unknown function that has been conserved during evolution. Previous studies have pointed out a role for frataxin in mitochondrial iron–sulfur (Fe–S) metabolism. Here, we have analyzed the incorporation of Fe–S clusters into yeast ferredoxin imported into isolated energized mitochondria from cells grown in the presence of glycerol, an obligatory respiratory carbon source. Similar amounts of apo-ferredoxin precursor were imported into mitochondria and processed in wild-type and yfh1-deleted ({Delta}YF111) strains. However, the incorporation of Fe–S clusters into apo-ferredoxin was significantly reduced in {Delta}YFH1 mitochondria. The newly assembled ferredoxin was stable, excluding the possibility that the decreased incorporation was a result of increased oxidative damage. When {Delta}YFH1 cells were grown in raffinose medium, the formation of holo-ferredoxin was low, as a consequence of the decrease in ferredoxin precursor import into mitochondria. However, the decrease in the conversion rate of apo- into holo-ferredoxin was in the same range as for glycerol-grown cells, indicating that the extent of the defect in Fe–S protein assembly is similar under different physiological conditions. These data show that frataxin is not essential for Fe–S protein assembly, but improves the efficiency of the process. The large variations observed in the activity of Fe–S cluster proteins under different physiological conditions result from secondary defects in the physiology of {Delta}YFH1 cells.

* To whom correspondence should be addressed. Tel: +32 10474691; Fax: +32 10473872; Email: foury{at}fysa.ucl.ac.be


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