Best, Katharina; Ikeuchi, Ken; Kater, Lukas; Best, Daniel; Musial, Joanna; Matsuo, Yoshitaka; Berninghausen, Otto; Becker, Thomas; Inada, Toshifumi; Beckmann, Roland (2023): Structural basis for clearing of ribosome collisions by the RQT complex. Nature Communications, 14 (1). ISSN 2041-1723
s41467-023-36230-8.pdf
The publication is available under the license Creative Commons Attribution.
Download (5MB)
Abstract
Translation of aberrant messenger RNAs can cause stalling of ribosomes resulting in ribosomal collisions. Collided ribosomes are specifically recognized to initiate stress responses and quality control pathways. Ribosome-associated quality control facilitates the degradation of incomplete translation products and requires dissociation of the stalled ribosomes. A central event is therefore the splitting of collided ribosomes by the ribosome quality control trigger complex, RQT, by an unknown mechanism. Here we show that RQT requires accessible mRNA and the presence of a neighboring ribosome. Cryogenic electron microscopy of RQT-ribosome complexes reveals that RQT engages the 40S subunit of the lead ribosome and can switch between two conformations. We propose that the Ski2-like helicase 1 (Slh1) subunit of RQT applies a pulling force on the mRNA, causing destabilizing conformational changes of the small ribosomal subunit, ultimately resulting in subunit dissociation. Our findings provide conceptual framework for a helicase-driven ribosomal splitting mechanism.
Doc-Type: | Article (LMU) |
---|---|
Organisational unit (Faculties): | 18 Chemistry and Pharmacy > GeneCenter |
DFG subject classification of scientific disciplines: | Life sciences |
Date Deposited: | 13. Jun 2023 07:20 |
Last Modified: | 07. Dec 2023 12:18 |
URI: | https://oa-fund.ub.uni-muenchen.de/id/eprint/768 |
DFG: | Funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) - 512515806 |
DFG: | Funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) - 491502892 |