Presentations
Cross-regulation of [2Fe-2S] cluster synthesis by ferredoxin-2 and frataxin
FRISBI/ReNaFoBis Biophysics Webinar, Online — May 21, 2026
Leveraging FIDA to monitor competitive binding during Fe-S cluster synthesis
FIDA UGM, Paris, France
Iron-Sulfur (Fe-S) clusters constitute ancient cofactors that accompany a versatile range of fundamental biological reactions across eukaryotes and prokaryotes. Mitochondrial eukaryotic [2Fe-2S] cluster synthesis is coordinated by the Iron-Sulfur Cluster (ISC) machinery which encompasses a core (NIAU2) scaffold that interacts with additional proteins FXN and FDX2 during Fe-S biogenesis. FIDA was used to monitor the binding of FXN and FDX2 to the (NIAU2) complex and was further leveraged to validate and characterize a mutually exclusive mode of binding. Through this, we mapped residues critical for the interaction of FDX2 with the (NIAU2) complex and further discovered that high levels of FDX2 disrupts [2Fe-2S] cluster synthesis through both competition with FXN and an auto-inhibitory mechanism involving its C-terminal tail.
Efficient [2Fe-2S] synthesis requires a balanced ratio of Ferredoxin-2 and Frataxin
XI International Conference on Fe-S Proteins, Winston-Salem, NC, USA
Iron-sulfur (FeS) clusters are indispensable molecular entities involved in crucial cellular processes across all domains of life. Using biochemical assays, we demonstrate that modulating FDX2 can mitigate FXN-associated toxicity while also enhancing FeS cluster synthesis efficiency, offering insights for Friedreich's Ataxia therapeutic development.
Friedreich's Ataxia Research Alliance (FARA) Flash Talk Series
FARA Flash Talks, Online
Flash talk for the 2023 FARA Flash Talk Series (begins at 16:37).