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TitleRQC2 is a major player in peptide release from stalled ribosomes.
Journal, issue, pagesStructure, Vol. 33, Issue 6, Page 1112-11121.e5, Year 2025
Publish dateJun 5, 2025
AuthorsCéline Fabret / Emmanuel Giudice / Sophie Chat / Reynald Gillet / Olivier Namy /
PubMed AbstractEukaryotic cells prevent the accumulation of potentially toxic aberrant polypeptides and maintain ribosome availability through surveillance and clearance mechanisms, including the evolutionarily ...Eukaryotic cells prevent the accumulation of potentially toxic aberrant polypeptides and maintain ribosome availability through surveillance and clearance mechanisms, including the evolutionarily conserved ribosome-associated quality control complex (RQC). RQC pathways have been widely investigated, with the identification of several factors ANKZF1/Vms1p, Ptrh1, and Arb1p involved in release/cleavage of the peptide-tRNA from 60S subunits. We aimed here to identify the genes involved in peptide release from stalled ribosomes. Using a genetic screen, we identified a mutant allele of RQC2 as involved in this process. We present the cryoelectron microscopy (cryo-EM) structure of RQC, which reveals how the F340I mutation affects mutant binding. This altered binding, in turn, disrupts the A-site's ability to bind the tRNA in the presence of Ltn1. These data account for the limitation of C-terminal alanine and threonine (CAT) tailing by the F340I mutation and suggest a model explaining the role of the Rqc2 protein in peptide release.
External linksStructure / PubMed:40187343
MethodsEM (single particle)
Resolution2.9 Å
Structure data

EMDB-19352: Cryo-EM structure of the 60S subunit with the RQC complex containing the mutant F340I Rqc2 protein and the Flag tagged Ltn1-Delta_ring
Method: EM (single particle) / Resolution: 2.9 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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