The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Scientific Reports Année : 2023

The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis

Ornella Bimai
  • Fonction : Auteur
Pierre Legrand
Nadia Touati
  • Fonction : Auteur
Jingjing Zhou
  • Fonction : Auteur
Nisha He
  • Fonction : Auteur
Marine Lénon
  • Fonction : Auteur
Frédéric Barras
  • Fonction : Auteur
Marc Fontecave
  • Fonction : Auteur
Béatrice Golinelli-Pimpaneau
  • Fonction : Auteur

Résumé

Abstract Thiolation of uridine 34 in the anticodon loop of several tRNAs is conserved in the three domains of life and guarantees fidelity of protein translation. U34-tRNA thiolation is catalyzed by a complex of two proteins in the eukaryotic cytosol (named Ctu1/Ctu2 in humans), but by a single NcsA enzyme in archaea. We report here spectroscopic and biochemical experiments showing that NcsA from Methanococcus maripaludis (MmNcsA) is a dimer that binds a [4Fe-4S] cluster, which is required for catalysis. Moreover, the crystal structure of MmNcsA at 2.8 Å resolution shows that the [4Fe-4S] cluster is coordinated by three conserved cysteines only, in each monomer. Extra electron density on the fourth nonprotein-bonded iron most likely locates the binding site for a hydrogenosulfide ligand, in agreement with the [4Fe-4S] cluster being used to bind and activate the sulfur atom of the sulfur donor. Comparison of the crystal structure of MmNcsA with the AlphaFold model of the human Ctu1/Ctu2 complex shows a very close superposition of the catalytic site residues, including the cysteines that coordinate the [4Fe-4S] cluster in MmNcsA. We thus propose that the same mechanism for U34-tRNA thiolation, mediated by a [4Fe-4S]-dependent enzyme, operates in archaea and eukaryotes.

Dates et versions

hal-04492153 , version 1 (06-03-2024)

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Citer

Ornella Bimai, Pierre Legrand, Jean-Luc Ravanat, Nadia Touati, Jingjing Zhou, et al.. The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis. Scientific Reports, 2023, 13 (1), pp.5351. ⟨10.1038/s41598-023-32423-9⟩. ⟨hal-04492153⟩
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