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={Nicolas Soler and Emmanuelle Delagoutte and Simona Miron and C{\'e}line Facca and Doroth{\'e}e Ba{\"i}lle and B D'autr{\'e}aux and Gil Craescu and Yves-Michel Frapart and Daniel Mansuy and Giuseppe Baldacci and Meng-Er Huang and Laurence Vernis},
  journal={Molecular microbiology},
  year={2011},
  volume={82 1},
  pages={54-67}
}
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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