Background: The cysteine desulfurase Nfs1 provides sulfur for Fe-S cluster biogenesis in mitochondria. Results: Frataxin or a mutant Fe-S scaffold protein (Isu1Sup) with frataxin-bypassing ability stimulates cysteine binding to Nfs1. Conclusion: Frataxin or Isu1Sup likely induces a conformational change in Nfs1, exposing substrate-binding sites. Significance: Data presented here may help develop a drug for treating Friedreich ataxia associated with frataxin deficiency.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology