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-Structure paper
Title | Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria. |
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Journal, issue, pages | Nature, Vol. 603, Issue 7901, Page 503-508, Year 2022 |
Publish date | Mar 9, 2022 |
Authors | Kazuki Saito / Hanna Kratzat / Annabelle Campbell / Robert Buschauer / A Maxwell Burroughs / Otto Berninghausen / L Aravind / Rachel Green / Roland Beckmann / Allen R Buskirk / |
PubMed Abstract | Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation. In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled ...Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation. In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled in the middle of a transcript from actively translating ribosomes. Here, using a genetic screen in Escherichia coli, we discovered a new rescue factor that has endonuclease activity. SmrB cleaves mRNAs upstream of stalled ribosomes, allowing the ribosome rescue factor tmRNA (which acts on truncated mRNAs) to rescue upstream ribosomes. SmrB is recruited to ribosomes and is activated by collisions. Cryo-electron microscopy structures of collided disomes from E. coli and Bacillus subtilis show distinct and conserved arrangements of individual ribosomes and the composite SmrB-binding site. These findings reveal the underlying mechanisms by which ribosome collisions trigger ribosome rescue in bacteria. |
External links | Nature / PubMed:35264790 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.37 - 13.29 Å |
Structure data | EMDB-13952, PDB-7qg8: EMDB-13955, PDB-7qgh: EMDB-13956, PDB-7qgn: EMDB-13958, PDB-7qgr: EMDB-13959, PDB-7qgu: EMDB-13961, PDB-7qh4: EMDB-13964: |
Chemicals | ChemComp-MG: ChemComp-K: ChemComp-HOH: |
Source |
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Keywords | RIBOSOME / Ribosome rescue / disome / ribosome collision / stalling / no-go complex / nuclease / SmrB |