Interaction between the reductase Tah18 and highly conserved Fe-S containing Dre2 C-terminus is essential for yeast viability. - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Molecular Microbiology Année : 2011

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

Emmanuelle Delagoutte
Simona Miron
  • Fonction : Auteur
Céline Facca
  • Fonction : Auteur
Dorothée Baïlle
  • Fonction : Auteur
Benoit d'Autreaux
  • Fonction : Auteur
Gil Craescu
  • Fonction : Auteur
Yves-Michel Frapart
  • Fonction : Auteur
Daniel Mansuy
  • Fonction : Auteur
  • PersonId : 756474
  • IdRef : 132533553
Giuseppe Baldacci
  • Fonction : Auteur
Meng-Er Huang
Laurence Vernis
  • Fonction : Auteur

Résumé

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 Tah18 and Dre2, and analysed how it conditions yeast viability. We show that Dre2 C-terminus interacts in vivo and in vitro with the flavin mononucleotide- and flavin adenine dinucleotide-binding sites of Tah18. Neither the absence of the electron donor nicotinamide adenine dinucleotide phosphate-binding domain in purified Tah18 nor the absence of Fe-S in aerobically purified Dre2 prevents the binding in vitro. In vivo, when this interaction is affected in a dre2 mutant, yeast viability is reduced. Conversely, enhancing artificially the interaction between mutated Dre2 and Tah18 restores cellular viability despite still reduced cytosolic Fe-S cluster biosynthesis. We conclude that Tah18-Dre2 interaction in vivo is essential for yeast viability. Our study may provide new insight into the survival/death switch involving this complex in yeast and in human cells.

Domaines

Chimie organique
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Dates et versions

hal-00634151 , version 1 (20-10-2011)

Identifiants

Citer

Nicolas Soler, Emmanuelle Delagoutte, Simona Miron, Céline Facca, Dorothée Baïlle, et al.. Interaction between the reductase Tah18 and highly conserved Fe-S containing Dre2 C-terminus is essential for yeast viability.. Molecular Microbiology, 2011, 82 (1), pp.54-67. ⟨10.1111/j.1365-2958.2011.07788.x⟩. ⟨hal-00634151⟩
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