Nature Communications (Apr 2024)

Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery

  • Keigo Fujiwara,
  • Naoko Tsuji,
  • Mayu Yoshida,
  • Hiraku Takada,
  • Shinobu Chiba

DOI
https://doi.org/10.1038/s41467-024-46993-3
Journal volume & issue
Vol. 15, no. 1
pp. 1 – 16

Abstract

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Abstract Regulatory arrest peptides interact with specific residues on bacterial ribosomes and arrest their own translation. Here, we analyse over 30,000 bacterial genome sequences to identify additional Sec/YidC-related arrest peptides, followed by in vivo and in vitro analyses. We find that Sec/YidC-related arrest peptides show patchy, but widespread, phylogenetic distribution throughout the bacterial domain. Several of the identified peptides contain distinct conserved sequences near the C-termini, but are still able to efficiently stall bacterial ribosomes in vitro and in vivo. In addition, we identify many arrest peptides that share an R-A-P-P-like sequence, suggesting that this sequence might serve as a common evolutionary seed to overcome ribosomal structural differences across species.