Interaction between the reductase Tah18 and highly conserved Fe‐S containing Dre2 C‐terminus is essential for yeast viability

@article{Soler2011InteractionBT,
  title={Interaction between the reductase Tah18 and highly conserved Fe‐S containing Dre2 C‐terminus is essential for yeast viability},
  author={N. Soler and E. Delagoutte and S. Miron and C. Facca and Doroth{\'e}e Ba{\"i}lle and B. D'autr{\'e}aux and Gil Craescu and Yves-Michel Frapart and D. Mansuy and G. Baldacci and M. Huang and Laurence Vernis},
  journal={Molecular Microbiology},
  year={2011},
  volume={82}
}
  • N. Soler, E. Delagoutte, +9 authors Laurence Vernis
  • Published 2011
  • Biology, Medicine
  • Molecular Microbiology
  • Tah18–Dre2 is a recently identified yeast protein complex, which is highly conserved in human and has been implicated in the regulation of oxidative stress induced cell death and in cytosolic Fe‐S proteins synthesis. Tah18 is a diflavin oxido‐reductase with binding sites for flavin mononucleotide, flavin adenine dinucleotide and nicotinamide adenine dinucleotide phosphate, which is able to transfer electrons to Dre2 Fe‐S clusters. In this work we characterized in details the interaction between… CONTINUE READING
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