ArticleProceedings of the National Academy of Sciences of the United States of America2025
Substrate recognition by a peptide-aminoacyl-tRNA ligase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Proteomic insights into nano-chitosan-induced salinity tolerance in solid matrix-primed mung bean seedlings.Scientific reports · 2026Article
- Aminoacyl-tRNA-dependent enzymes in natural product biosynthesis: structure-function insights.The Journal of antibiotics · 2026Review
- The Biosynthetic Pathway to the Pyrroloiminoquinone Marine Natural Product Ammosamide C.Journal of the American Chemical Society · 2025Article
- Aminoacyl-tRNA Specificity of a Ligase Catalyzing Non-ribosomal Peptide Extension.Journal of the American Chemical Society · 2025Article
- PEARLs of wisdom for ribosome-independent peptide bond synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
- Commented on by
Authors and funding
3 authors.
Funding
Abstract
The continuing discovery of new peptide-aminoacyl-tRNA ligases (PEARLs) has unveiled a diverse array of enzymes with the unique potential to append amino acids to the C terminus of substrate peptides in an aminoacyl-tRNA-dependent manner. To date, PEARLs have been reported that can conjugate Cys, Ala, Trp, Gly, Leu, Asn, and Thr residues, but the basis of peptide substrate and aminoacyl-tRNA recognition is not known. Cell-free expression (CFE) has emerged as a powerful tool to rapidly assay activity of substrate variants, and we used the technique in this study to investigate the peptide substrate specificity of the PEARL [Formula: see text]. This enzyme that adds Trp was discovered previously during genome mining for ribosomally synthesized and posttranslational modified peptides (RiPPs). The enzyme is remarkably tolerant of changes to the C-terminal amino acid of the peptide substrate, and truncation and replacement experiments suggest a minimal sequence requirement. An AlphaFold3 model provided insights into binding interactions of the substrate peptide BhaA-Ala to [Formula: see text] and also generated predictions for tRNA, ATP, and Mg
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.