Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria

Kazuki Saito, Hanna Kratzat, Annabelle Campbell, Robert Buschauer, A. Maxwell Burroughs, Otto Berninghausen, L. Aravind, Rachel Green, Roland Beckmann () and Allen R. Buskirk ()
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Kazuki Saito: Johns Hopkins University School of Medicine
Hanna Kratzat: University of Munich
Annabelle Campbell: Johns Hopkins University School of Medicine
Robert Buschauer: University of Munich
A. Maxwell Burroughs: National Institutes of Health
Otto Berninghausen: University of Munich
L. Aravind: National Institutes of Health
Rachel Green: Johns Hopkins University School of Medicine
Roland Beckmann: University of Munich
Allen R. Buskirk: Johns Hopkins University School of Medicine

Nature, 2022, vol. 603, issue 7901, 503-508

Abstract: Abstract Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation1,2. In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled in the middle of a transcript from actively translating ribosomes3–6. 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 mRNAs3) 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.

Date: 2022
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DOI: 10.1038/s41586-022-04416-7

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