7ZS5

Structure of 60S ribosomal subunit from S. cerevisiae with eIF6 and tRNA

This is a non-PDB format compatible entry.

Summary for 7ZS5

• Entry DOI: 10.2210/pdb7zs5/pdb
• Related: 7zpq 7zrs
• EMDB information: 14926
• Descriptor: 25S ribosomal RNA, 60S ribosomal protein L4-A, 60S ribosomal protein L5, ... (47 entities in total)
• Functional Keywords: collision, splitting, rqc, eif6, tif6p, ribosome
• Biological source: Saccharomyces cerevisiae (brewer's yeast); More
• Total number of polymer chains: 46
• Total formula weight: 1939940.07

Authors

Best, K.M.,Ikeuchi, K.,Kater, L.,Best, D.M.,Musial, J.,Matsuo, Y.,Berninghausen, O.,Becker, T.,Inada, T.,Beckmann, R. (deposition date: 2022-05-06, release date: 2023-02-22, Last modification date: 2025-02-05)

Primary citation

Best, K.,Ikeuchi, K.,Kater, L.,Best, D.,Musial, J.,Matsuo, Y.,Berninghausen, O.,Becker, T.,Inada, T.,Beckmann, R.
Structural basis for clearing of ribosome collisions by the RQT complex.
Nat Commun, 14:921-921, 2023

PubMed 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.

PubMed: 36801861
DOI: 10.1038/s41467-023-36230-8

Experimental method

ELECTRON MICROSCOPY (3.2 Å)