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TitleSensing of individual stalled 80S ribosomes by Fap1 for nonfunctional rRNA turnover.
Journal, issue, pagesMol Cell, Vol. 82, Issue 18, Page 3424-33437.e8, Year 2022
Publish dateSep 15, 2022
AuthorsSihan Li / Ken Ikeuchi / Misaki Kato / Robert Buschauer / Takato Sugiyama / Shungo Adachi / Hideo Kusano / Tohru Natsume / Otto Berninghausen / Yoshitaka Matsuo / Thomas Becker / Roland Beckmann / Toshifumi Inada /
PubMed AbstractCells can respond to stalled ribosomes by sensing ribosome collisions and employing quality control pathways. How ribosome stalling is resolved without collisions, however, has remained elusive. ...Cells can respond to stalled ribosomes by sensing ribosome collisions and employing quality control pathways. How ribosome stalling is resolved without collisions, however, has remained elusive. Here, focusing on noncolliding stalling exhibited by decoding-defective ribosomes, we identified Fap1 as a stalling sensor triggering 18S nonfunctional rRNA decay via polyubiquitination of uS3. Ribosome profiling revealed an enrichment of Fap1 at the translation initiation site but also an association with elongating individual ribosomes. Cryo-EM structures of Fap1-bound ribosomes elucidated Fap1 probing the mRNA simultaneously at both the entry and exit channels suggesting an mRNA stasis sensing activity, and Fap1 sterically hinders the formation of canonical collided di-ribosomes. Our findings indicate that individual stalled ribosomes are the potential signal for ribosome dysfunction, leading to accelerated turnover of the ribosome itself.
External linksMol Cell / PubMed:36113412
MethodsEM (single particle)
Resolution2.4 - 5.8 Å
Structure data

14990

7zw0

EMDB-14990, PDB-7zw0:
FAP-80S Complex - Rotated state
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-14992: FAP-80S Complex - Non-rotated state with empty A site
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-14994: FAP-80S Complex - Non-rotated state with eRF1-ABCE1
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-15655: A Consensus Map of Yeast FAP-80S Complex in Rotated State.
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-15656: Yeast FAP-80S Complex in Rotated State - Body 1 - 60S subunit
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-15657: Yeast FAP-80S in rotated state - Body 3 - 40S head and Fap1-Fpr1
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-15658: Local refined map of Fap1-arm and Yil161w/Smu2 of yeast FAP-80S complex in rotated state.
Method: EM (single particle) / Resolution: 5.8 Å

EMDB-15659: Local refined map of Fap1 RING-finger domain with partial 40S subunit of yeast FAP-80S complex in rotated state.
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-15660: Yeast FAP-80S Complex in Rotated State - Body 2 - 40S body with Fap1 R3H domain.
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SPD:
SPERMIDINE / Spermidine

ChemComp-ZN:
Unknown entry

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae w303 (yeast)
KeywordsRIBOSOME / NRD / Ubiquitination / E3 ligase / Quality Control System

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