7ZW0

FAP-80S Complex - Rotated state

This is a non-PDB format compatible entry.

Summary for 7ZW0

• Entry DOI: 10.2210/pdb7zw0/pdb
• EMDB information: 14990 15655 15656 15657 15658 15659 15660
• Descriptor: 25S ribosomal RNA (RDN25-1), 40S ribosomal protein S5, 40S ribosomal protein S6-B, ... (87 entities in total)
• Functional Keywords: nrd, ubiquitination, e3 ligase, quality control system, ribosome
• Biological source: Saccharomyces cerevisiae W303; More
• Total number of polymer chains: 86
• Total formula weight: 3333332.38

Authors

Ikeuchi, K.,Buschauer, R.,Berninghausen, O.,Becker, T.,Beckmann, R. (deposition date: 2022-05-17, release date: 2022-10-05, Last modification date: 2024-07-24)

Primary citation

Li, S.,Ikeuchi, K.,Kato, M.,Buschauer, R.,Sugiyama, T.,Adachi, S.,Kusano, H.,Natsume, T.,Berninghausen, O.,Matsuo, Y.,Becker, T.,Beckmann, R.,Inada, T.
Sensing of individual stalled 80S ribosomes by Fap1 for nonfunctional rRNA turnover.
Mol.Cell, 82:3424-3437.e8, 2022

PubMed Abstract: 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.

PubMed: 36113412
DOI: 10.1016/j.molcel.2022.08.018

Experimental method

ELECTRON MICROSCOPY (2.4 Å)