Human mitochondrial ferritin improves respiratory function in yeast mutants deficient in iron-sulfur cluster biogenesis, but is not a functional homologue of yeast frataxin.

ABSTRACT: We overexpressed human mitochondrial ferritin in frataxin-deficient yeast cells (Δyfh1), but also in another mutant affected in [Fe-S] assembly (Δggc1). Ferritin was correctly processed and expressed in the mitochondria of these cells, but the fraction of total mitochondrial iron bound to ferritin was very low, and most of the iron remained in the form of insoluble particles of ferric phosphate in these mitochondria, as evidenced by gel filtration analysis of the mitochondrial matrix (fast protein liquid chromatography [FPLC]) and by Mössbauer spectroscopy. Mutant cells in which ferritin was overexpressed still accumulated iron in the mitochondria and remained deficient in [Fe-S] assembly, suggesting that human mitochondrial ferritin is not a functional homologue of yeast frataxin. However

SUBMITTER: Sutak R 

PROVIDER: S-EPMC3426411 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature