Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@article{Yoon2012MutationIT,
  title={Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.},
  author={Heeyong Yoon and Ramesh Golla and Emmanuel Lesuisse and Jayashree Pain and Jason E. Donald and Elise R. Lyver and Debkumar Pain and Andrew Dancis},
  journal={The Biochemical journal},
  year={2012},
  volume={441 1},
  pages={473-80}
}
Frataxin is a conserved mitochondrial protein deficient in patients with Friedreich's ataxia. Frataxin has been implicated in control of iron homoeostasis and Fe-S cluster assembly. In yeast or human mitochondria, frataxin interacts with components of the Fe-S cluster synthesis machinery, including the cysteine desulfurase Nfs1, accessory protein Isd11 and scaffold protein Isu. In the present paper, we report that a single amino acid substitution (methionine to isoleucine) at position 107 in… CONTINUE READING
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