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

Nat Commun. 2024 Apr 2;15(1):2711. doi: 10.1038/s41467-024-46993-3.

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.

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Escherichia coli Proteins* / metabolism
  • Peptides / chemistry
  • Phylogeny
  • Protein Biosynthesis*
  • Ribosomes / genetics
  • Ribosomes / metabolism

Substances

  • Peptides
  • Bacterial Proteins
  • Escherichia coli Proteins