ArticleNucleic acids research2009
Aminoacyl-tRNA recognition by the FemXWv transferase for bacterial cell wall synthesis.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- A single viral enzyme drives tRNA-dependent hypermodification of DNA at adenine.Nature communications · 2026Article
- Structure and Mechanism of Aminoacyl-tRNA-Protein L/F- and R-transferases.Journal of molecular biology · 2025Review
- Article
- Amino-acyl tXNA as inhibitors or amino acid donors in peptide synthesis.Nucleic acids research · 2022Article
- Proteome ofInternational journal of molecular sciences · 2022Article
- Unique anticodon loop conformation with the flipped-out wobble nucleotide in the crystal structure of unbound tRNARNA (New York, N.Y.) · 2021Article
- Flexizyme-aminoacylated shortened tRNAs demonstrate that only the aminoacylated acceptor arms of the two tRNA substrates are required for cyclodipeptide synthase activity.Nucleic acids research · 2020Article
- Stereospecificity control in aminoacyl-tRNA-synthetases: new evidence of d-amino acids activation and editing.Nucleic acids research · 2019Article
- Flexizyme-catalyzed synthesis of 3'-aminoacyl-NH-tRNAs.Nucleic acids research · 2019Article
- Investigation of Amide Bond Formation during Dehydrophos Biosynthesis.ACS chemical biology · 2018Article
- Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biology.Molecular microbiology · 2016Review
- Activities and regulation of peptidoglycan synthases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Bacterial transfer RNAs.FEMS microbiology reviews · 2015Review
- The determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferase.RNA (New York, N.Y.) · 2014Article
- Resistance to antibiotics targeted to the bacterial cell wall.Protein science : a publication of the Protein Society · 2014Review
- tRNAs as regulators of biological processes.Frontiers in genetics · 2014Review
- Direction of aminoacylated transfer RNAs into antibiotic synthesis and peptidoglycan-mediated antibiotic resistance.FEBS letters · 2013Review
- tRNA-dependent peptide bond formation by the transferase PacB in biosynthesis of the pacidamycin group of pentapeptidyl nucleoside antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Structural basis for nonribosomal peptide synthesis by an aminoacyl-tRNA synthetase paralog.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis.Biology direct · 2010Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transferases of the Fem family catalyse peptide-bond formation by using aminoacyl-tRNAs and peptidoglycan precursors as donor and acceptor substrates, respectively. The specificity of Fem transferases is essential since mis-incorporated amino acids could act as chain terminators thereby preventing formation of a functional stress-bearing peptidoglycan network. Here we have developed chemical acylation of RNA helices with natural and non-proteinogenic amino acids to gain insight into the specificity of the model transferase FemX(Wv). Combining modifications in the RNA and aminoacyl moieties of the donor substrate revealed that unfavourable interactions of FemX(Wv) with the acceptor arm of tRNA(Gly) and with L-Ser or larger residues quantitatively accounts for the preferential transfer of L-Ala observed with complete aminoacyl-tRNAs. The main FemX(Wv) identity determinant was identified as the penultimate base pair (G(2)-C(71)) of the acceptor arm instead of G(3)*U(70) for the alanyl-tRNA synthetase. FemX(Wv) tolerated a configuration inversion of the Calpha of L-Ala but not the introduction of a second methyl on this atom. These results indicate that aminoacyl-tRNA recognition by FemX(Wv) is distinct from other components of the translation machinery and relies on the exclusion of bulky amino acids and of the sequence of tRNA(Gly) from the active site.
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