| |  Online-Ressource |
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| Verfasst von: | Filbeck, Sebastian [VerfasserIn]  |
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| | Cerullo, Federico [VerfasserIn] |
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| | Paternoga, Helge [VerfasserIn] |
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| | Tsaprailis, George [VerfasserIn] |
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| | Joazeiro, Claudio A. P. [VerfasserIn] |
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| | Pfeffer, Stefan [VerfasserIn] |
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| Titel: | Mimicry of canonical translation elongation underlies alanine tail synthesis in RQC |
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| Verf.angabe: | Sebastian Filbeck, Federico Cerullo, Helge Paternoga, George Tsaprailis, Claudio A.P. Joazeiro, and Stefan Pfeffer |
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| E-Jahr: | 2021 |
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| Jahr: | 7 January 2021 |
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| Umfang: | 18 S. |
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| Fussnoten: | Online veröffentlicht am 30. November 2020, Artikelversion vom 7. Januar 2021 ; Gesehen am 21.05.2021 |
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| Titel Quelle: | Enthalten in: Molecular cell |
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| Ort Quelle: | [Cambridge, Mass.] : Cell Press, 1997 |
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| Jahr Quelle: | 2021 |
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| Band/Heft Quelle: | 81(2021), 1 vom: Jan., Seite 104-114, e1-e6 |
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| ISSN Quelle: | 1097-4164 |
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| Abstract: | Aborted translation produces large ribosomal subunits obstructed with tRNA-linked nascent chains, which are substrates of ribosome-associated quality control (RQC). Bacterial RqcH, a widely conserved RQC factor, senses the obstruction and recruits tRNAAla(UGC) to modify nascent-chain C termini with a polyalanine degron. However, how RqcH and its eukaryotic homologs (Rqc2 and NEMF), despite their relatively simple architecture, synthesize such C-terminal tails in the absence of a small ribosomal subunit and mRNA has remained unknown. Here, we present cryoelectron microscopy (cryo-EM) structures of Bacillus subtilis RQC complexes representing different Ala tail synthesis steps. The structures explain how tRNAAla is selected via anticodon reading during recruitment to the A-site and uncover striking hinge-like movements in RqcH leading tRNAAla into a hybrid A/P-state associated with peptidyl-transfer. Finally, we provide structural, biochemical, and molecular genetic evidence identifying the Hsp15 homolog (encoded by rqcP) as a novel RQC component that completes the cycle by stabilizing the P-site tRNA conformation. Ala tailing thus follows mechanistic principles surprisingly similar to canonical translation elongation. |
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| DOI: | doi:10.1016/j.molcel.2020.11.001 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1016/j.molcel.2020.11.001 |
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| | Volltext: https://www.sciencedirect.com/science/article/pii/S1097276520307796 |
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| | DOI: https://doi.org/10.1016/j.molcel.2020.11.001 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | alanine tailing |
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| | cryo-EM |
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| | Hsp15 |
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| | ribosome-associated quality control |
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| | ribosomes |
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| | RQC |
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| | RqcH |
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| | RqcP |
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| | SsrA |
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| | translation elongation |
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| K10plus-PPN: | 1758317434 |
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| Verknüpfungen: | → Zeitschrift |
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Mimicry of canonical translation elongation underlies alanine tail synthesis in RQC / Filbeck, Sebastian [VerfasserIn]; 7 January 2021 (Online-Ressource)
