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TitleUbiquitination of stalled ribosome triggers ribosome-associated quality control.
Journal, issue, pagesNat Commun, Vol. 8, Issue 1, Page 159, Year 2017
Publish dateJul 31, 2017
AuthorsYoshitaka Matsuo / Ken Ikeuchi / Yasushi Saeki / Shintaro Iwasaki / Christian Schmidt / Tsuyoshi Udagawa / Fumiya Sato / Hikaru Tsuchiya / Thomas Becker / Keiji Tanaka / Nicholas T Ingolia / Roland Beckmann / Toshifumi Inada /
PubMed AbstractTranslation arrest by polybasic sequences induces ribosome stalling, and the arrest product is degraded by the ribosome-mediated quality control (RQC) system. Here we report that ubiquitination of ...Translation arrest by polybasic sequences induces ribosome stalling, and the arrest product is degraded by the ribosome-mediated quality control (RQC) system. Here we report that ubiquitination of the 40S ribosomal protein uS10 by the E3 ubiquitin ligase Hel2 (or RQT1) is required for RQC. We identify a RQC-trigger (RQT) subcomplex composed of the RNA helicase-family protein Slh1/Rqt2, the ubiquitin-binding protein Cue3/Rqt3, and yKR023W/Rqt4 that is required for RQC. The defects in RQC of the RQT mutants correlate with sensitivity to anisomycin, which stalls ribosome at the rotated form. Cryo-electron microscopy analysis reveals that Hel2-bound ribosome are dominantly the rotated form with hybrid tRNAs. Ribosome profiling reveals that ribosomes stalled at the rotated state with specific pairs of codons at P-A sites serve as RQC substrates. Rqt1 specifically ubiquitinates these arrested ribosomes to target them to the RQT complex, allowing subsequent RQC reactions including dissociation of the stalled ribosome into subunits.Several protein quality control mechanisms are in place to trigger the rapid degradation of aberrant polypeptides and mRNAs. Here the authors describe a mechanism of ribosome-mediated quality control that involves the ubiquitination of ribosomal proteins by the E3 ubiquitin ligase Hel2/RQT1.
External linksNat Commun / PubMed:28757607 / PubMed Central
MethodsEM (single particle)
Resolution7.0 Å
Structure data

EMDB-3732:
Non-rotated ribosome class 1 with A- and P-site tRNAs of the Rqt1-FTP pulldown
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-3734:
Class 1 of rotated ribosomes (rotated 1 state) with A/A- and P/E-site tRNAs of the Rqt1-FTP pulldown
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-3735:
Class 2 of rotated ribosomes (rotated 1 state) with A/A- and P/E-site tRNAs of the Rqt1-FTP pulldown
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-3736:
Class 1 of rotated ribosomes (rotated 2 state) with A/P- and P/E-site tRNAs of the Rqt1-FTP pulldown
Method: EM (single particle) / Resolution: 7.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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