Ontology highlight
ABSTRACT:
SUBMITTER: Dauden MI
PROVIDER: S-EPMC5286394 | biostudies-literature | 2017 Feb
REPOSITORIES: biostudies-literature
Dauden Maria I MI Kosinski Jan J Kolaj-Robin Olga O Desfosses Ambroise A Ori Alessandro A Faux Celine C Hoffmann Niklas A NA Onuma Osita F OF Breunig Karin D KD Beck Martin M Sachse Carsten C Séraphin Bertrand B Glatt Sebastian S Müller Christoph W CW
EMBO reports 20161214 2
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 ...[more]