Architecture of the yeast elongator complex
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...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
01 February 2017
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| In: |
EMBO reports
Year: 2016, Jahrgang: 18, Heft: 2, Pages: 264-279 |
| ISSN: | 1469-3178 |
| DOI: | 10.15252/embr.201643353 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.15252/embr.201643353 Verlag, Volltext: http://embor.embopress.org/content/18/2/264 
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| Verfasserangaben: | 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 |
| Zusammenfassung: | 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. |
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| Beschreibung: | Gesehen am 08.10.2018 Published online 14.12.2016 |
| Beschreibung: | Online Resource |
| ISSN: | 1469-3178 |
| DOI: | 10.15252/embr.201643353 |