Iron-binding activity in yeast frataxin entails a trade off with stability in the alpha1/beta1 acidic ridge region.

ABSTRACT: Frataxin is a highly conserved mitochondrial protein whose deficiency in humans results in Friedreich's ataxia (FRDA), an autosomal recessive disorder characterized by progressive ataxia and cardiomyopathy. Although its cellular function is still not fully clear, the fact that frataxin plays a crucial role in Fe-S assembly on the scaffold protein Isu is well accepted. In the present paper, we report the characterization of eight frataxin variants having alterations on two putative functional regions: the alpha1/beta1 acidic ridge and the conserved beta-sheet surface. We report that frataxin iron-binding capacity is quite robust: even when five of the most conserved residues from the putative iron-binding region are altered, at least two iron atoms per monomer can be bound, although with de

SUBMITTER: Correia AR 

PROVIDER: S-EPMC2819628 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature