Ontology highlight
ABSTRACT:
SUBMITTER: Foury F
PROVIDER: S-EPMC1796776 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
EMBO reports 20061222 2
Friedreich ataxia is caused by decreased levels of frataxin, a mitochondrial acidic protein that is assumed to act as chaperone in the assembly of Fe-S clusters on the scaffold Isu protein. Frataxin has the in vitro capacity to form iron-loaded multimers, which also suggests an iron storage function. It has been reported that alanine substitution of residues in an acidic ridge of yeast frataxin (Yfh1) elicits loss of iron binding in vitro but has no effect on Fe-S cluster synthesis in vivo. Here ...[more]