ArticleFEBS letters2011
β-Lysine discrimination by lysyl-tRNA synthetase.
Article in FEBS letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026Article
- Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-D-glucose epimerization in Pseudomonas putida KT2440.Scientific reports · 2021Article
- Arginine-rhamnosylation as new strategy to activate translation elongation factor P.Nature chemical biology · 2015Article
- Identification and functional characterization of a novel bacterial type asparagine synthetase A: a tRNA synthetase paralog from Leishmania donovani.The Journal of biological chemistry · 2014Article
- Molecular evolution of protein-RNA mimicry as a mechanism for translational control.Nucleic acids research · 2014Article
- (R)-β-lysine-modified elongation factor P functions in translation elongation.The Journal of biological chemistry · 2013Article
- Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major.BMC genomics · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Elongation factor P is modified with (R)-β-lysine by the lysyl-tRNA synthetase (LysRS) paralog PoxA. PoxA specificity is orthogonal to LysRS, despite their high similarity. To investigate α- and β-lysine recognition by LysRS and PoxA, amino acid replacements were made in the LysRS active site guided by the PoxA structure. A233S LysRS behaved as wild type with α-lysine, while the G469A and A233S/G469A variants decreased stable α-lysyl-adenylate formation. A233S LysRS recognized β-lysine better than wildtype, suggesting a role for this residue in discriminating α- and β-amino acids. Both enantiomers of β-lysine were substrates for tRNA aminoacylation by LysRS, which, together with the relaxed specificity of the A233S variant, suggest a possible means to develop systems for in vivo co-translational insertion of β-amino acids.
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Registered trials
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