Architecture of the yeast Elongator complex.
Fiche publication
Date publication
février 2017
Journal
EMBO reports
Auteurs
Membres identifiés du Cancéropôle Est :
Dr SERAPHIN Bertrand
Tous les auteurs :
Dauden MI, Kosinski J, Kolaj-Robin O, Desfosses A, Ori A, Faux C, Hoffmann NA, Onuma OF, Breunig KD, Beck M, Sachse C, Séraphin B, Glatt S, Müller CW
Lien Pubmed
Résumé
The highly conserved eukaryotic Elongator complex performs specific chemical modifications on wobble base uridines of tRNAs, which are essential for proteome stability and homeostasis. The complex is formed by six individual subunits (Elp1-6) that are all equally important for its tRNA modification activity. However, its overall architecture and the detailed reaction mechanism remain elusive. Here, we report the structures of the fully assembled yeast Elongator and the Elp123 sub-complex solved by an integrative structure determination approach showing that two copies of the Elp1, Elp2, and Elp3 subunits form a two-lobed scaffold, which binds Elp456 asymmetrically. Our topological models are consistent with previous studies on individual subunits and further validated by complementary biochemical analyses. Our study provides a structural framework on how the tRNA modification activity is carried out by Elongator.
Mots clés
Saccharomyces cerevisiae , Elongator, electron microscopy, tRNA modification, yeast
Référence
EMBO Rep.. 2017 Feb;18(2):264-279