Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 38565864.
- Also identified by DOI 10.1038/s41467-024-46993-3 and PMC identifier 10987492.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Protein Biosynthesis
- Escherichia coli Proteins