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

Keigo FujiwaraNaoko TsujiMayu YoshidaHiraku TakadaShinobu Chiba
Published in: Nature communications (2024)
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.
Keyphrases
  • amino acid
  • cell cycle
  • transcription factor
  • cell proliferation
  • genome wide
  • dna methylation