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


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.

SUBMITTER: Fujiwara K 

PROVIDER: S-EPMC10987492 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature

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

Fujiwara Keigo K   Tsuji Naoko N   Yoshida Mayu M   Takada Hiraku H   Chiba Shinobu S  

Nature communications 20240402 1


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, bu  ...[more]

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