Structural basis for clearing of ribosome collisions by the RQT complex

Katharina Best, Ken Ikeuchi, Lukas Kater, Daniel Best, Joanna Musial, Yoshitaka Matsuo, Otto Berninghausen, Thomas Becker, Toshifumi Inada () and Roland Beckmann ()
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Katharina Best: University of Munich
Ken Ikeuchi: University of Munich
Lukas Kater: University of Munich
Daniel Best: University of Munich
Joanna Musial: University of Munich
Yoshitaka Matsuo: The University of Tokyo
Otto Berninghausen: University of Munich
Thomas Becker: University of Munich
Toshifumi Inada: The University of Tokyo
Roland Beckmann: University of Munich

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-36230-8

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