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Comment
. 2022 May 23;32(10):R469-R472.
doi: 10.1016/j.cub.2022.04.038.

Ribosome collisions: New ways to initiate ribosome rescue

Affiliations
Comment

Ribosome collisions: New ways to initiate ribosome rescue

Stephanie L Leedom et al. Curr Biol. .

Abstract

When ribosomes collide while translating the same mRNA, a MutS-like protein can pry apart the leading ribosome and a nuclease can cut the mRNA between the collided ribosomes to initiate ribosome rescue and recycling.

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Conflict of interest statement

Declaration of interests The authors declare no competing interests.

Figures

Figure 1.
Figure 1.. SMR domains in factors that initiate ribosome rescue.
Domain architectures are represented for Saccharomyces cerevisiae Cue2, E. coli SmrB, and B. subtilis MutS2.
Figure 2.
Figure 2.. Pathways for rescuing collided disomes in bacteria.
The fates of the trailing ribosome (blue) and stalled ribosome (red) are indicated for MutS2 and SmrB. Following disome collision, ribosomes can be targeted for rescue by MutS2 (in B. subtilis) or SmrB (in E. coli). MutS2 splits the 50S and 30S subunits on the stalled ribosome. The 50S subunit is then targeted by RqcH and RqcP which hydrolyze the peptidyl-tRNA. The fate of the trailing ribosome is not known, but mRNA cleavage by MutS2 would produce a substrate for ribosome rescue pathways. Alternatively, if no cleavage occurs, the trailing ribosome may continue translating the mRNA after the stalled ribosome is removed (not shown). SmrB cuts between collided ribosomes and targets the trailing ribosome for ribosome rescue. The fate of the stalled ribosome is not known, but other nucleases may cleave the mRNA 3’ of the stalled ribosome and target it for ribosome rescue.

Comment on

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