Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu.
Friedreich ataxia is caused by reduced activity of frataxin, a conserved iron-binding protein of the mitochondrial matrix, thought to supply iron for formation of Fe-S clusters on the scaffold protein Isu. Frataxin binds Isu in an iron-dependent manner in vitro. However, the biological relevance of this interaction and whether in ... vivo the interaction between frataxin and Isu is mediated by adaptor proteins is a matter of debate. Here, we report that alterations of conserved, surface-exposed residues of yeast frataxin, which have deleterious effects on cell growth, impair Fe-S cluster biogenesis and interaction with Isu while altering neither iron binding nor oligomerization. Our results support the idea that the surface of the beta-sheet, adjacent to the acidic, iron binding ridge, is important for interaction of Yfh1 with the Fe-S cluster scaffold and point to a critical role for frataxin in Fe-S cluster biogenesis.
Mesh Terms:
Amino Acid Sequence, Amino Acids, Electron Transport, Friedreich Ataxia, Humans, Iron, Iron-Binding Proteins, Iron-Sulfur Proteins, Mitochondria, Mitochondrial Proteins, Models, Molecular, Molecular Sequence Data, Mutant Proteins, Mutation, Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Up-Regulation
Amino Acid Sequence, Amino Acids, Electron Transport, Friedreich Ataxia, Humans, Iron, Iron-Binding Proteins, Iron-Sulfur Proteins, Mitochondria, Mitochondrial Proteins, Models, Molecular, Molecular Sequence Data, Mutant Proteins, Mutation, Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Up-Regulation
J. Biol. Chem.
Date: May. 02, 2008
PubMed ID: 18319250
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