ArticleNucleic acids research2021
X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 19 citations in OpenAlex.
- A single viral enzyme drives tRNA-dependent hypermodification of DNA at adenine.Nature communications · 2026Article
- Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Kinetic characterization of amino acid activation by aminoacyl-tRNA synthetases using radiolabelled γ-[FEBS open bio · 2025Article
- Article
- The mechanism of discriminative aminoacylation by isoleucyl-tRNA synthetase based on wobble nucleotide recognition.Nature communications · 2024Article
- A genomic database furnishes minimal functional glycyl-tRNA synthetases homologous to other, designed class II urzymes.Nucleic acids research · 2024Article
- Genomic database furnishes a spontaneous example of a functional Class II glycyl-tRNA synthetase urzyme.bioRxiv : the preprint server for biology · 2024Article
- Mechanism of tRNA recognition by heterotetrameric glycyl-tRNA synthetase from lactic acid bacteria.Journal of biochemistry · 2023Article
- An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening.Nucleic acids research · 2023Article
- Structural basis of a two-step tRNA recognition mechanism for plastid glycyl-tRNA synthetase.Nucleic acids research · 2023Article
- The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements.Science advances · 2023Article
- Identification of Putative Drug Targets in Highly Resistant Gram-Negative Bacteria; and Drug Discovery Against Glycyl-tRNA Synthetase as a New Target.Bioinformatics and biology insights · 2023Article
- The Minimal Translation Machinery: What We Can Learn From Naturally and Experimentally Reduced Genomes.Frontiers in microbiology · 2022Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
AaRSs (aminoacyl-tRNA synthetases) group into two ten-member classes throughout evolution, with unique active site architectures defining each class. Most are monomers or homodimers but, for no apparent reason, many bacterial GlyRSs are heterotetramers consisting of two catalytic α-subunits and two tRNA-binding β-subunits. The heterotetrameric GlyRS from Escherichia coli (EcGlyRS) was historically tested whether its α- and β-polypeptides, which are encoded by a single mRNA with a gap of three in-frame codons, are replaceable by a single chain. Here, an unprecedented X-shaped structure of EcGlyRS shows wide separation of the abutting chain termini seen in the coding sequences, suggesting strong pressure to avoid a single polypeptide format. The structure of the five-domain β-subunit is unique across all aaRSs in current databases, and structural analyses suggest these domains play different functions on α-subunit binding, ATP coordination and tRNA recognition. Moreover, the X-shaped architecture of EcGlyRS largely fits with a model for how two classes of tRNA synthetases arose, according to whether enzymes from opposite classes can simultaneously co-dock onto separate faces of the same tRNA acceptor stem. While heterotetrameric GlyRS remains the last structurally uncharacterized member of aaRSs, our study contributes to a better understanding of this ancient and essential enzyme family.
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