Architecture of the yeast elongator complex

• Verfasst von: Dauden, Maria I. [VerfasserIn]
• Verfasst von: Beck, Martin [VerfasserIn]
• Verfasst von: Müller, Christoph W. [VerfasserIn]
• Titel: Architecture of the yeast elongator complex
• Verf.angabe: Maria I. Dauden, Jan Kosinski, Olga Kolaj‐Robin, Ambroise Desfosses, Alessandro Ori, Celine Faux, Niklas A. Hoffmann, Osita F. Onuma, Karin D. Breunig, Martin Beck, Carsten Sachse, Bertrand Séraphin, Sebastian Glatt, Christoph W. Müller
• Jahr des Originals: 2016
• Umfang: 16 S.
• Fussnoten: Gesehen am 08.10.2018 ; Published online 14.12.2016
• Titel Quelle: Enthalten in: European Molecular Biology Organization: EMBO reports
• Jahr Quelle: 2017
• Band/Heft Quelle: 18(2017), 2, S. 264-279
• ISSN Quelle: 1469-3178
• DOI: doi:10.15252/embr.201643353
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1581636849

Abstract

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.