Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery
Year: 2024
Type: article
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.
Source: Nature Communications
Authors: Keigo Fujiwara, Naoko Tsuji, Mayu Yoshida, Hiraku Takada, Shinobu Chiba
Institution: Kyoto Sangyo University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,790
Awards: G1402995528, G1843756498, G3296740551, Studies of ABC-F translation factors: from antibiotic resistance to translational control., G4053832768, G4619669398, Next generation TnDR for proteome-wide profiling of co-translatinoal protein dynamics, G5363184618, Molecular mechanism of channel-independent protein translocation machinery, G6267484621, G6477599001, Proteome-wide capture of co-translational protein dynamics, G7203320543, G8499196928
OpenAlex ID: W4393396992
