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

Keigo Fujiwara (), Naoko Tsuji, Mayu Yoshida, Hiraku Takada and Shinobu Chiba ()
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Keigo Fujiwara: Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku
Naoko Tsuji: Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku
Mayu Yoshida: Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku
Hiraku Takada: Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku
Shinobu Chiba: Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-46993-3

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