Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly

Alok Pandey, Donna M. Gordon, Jayashree Pain, Timothy L. Stemmler, Andrew Dancis, Debkumar Pain

Research output: Contribution to journalArticlepeer-review

65 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)36773-36786
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number52
DOIs
StatePublished - Dec 27 2013

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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