ArticleThe EMBO journal2010
Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 49 citations in OpenAlex.
- Structure of ergosteryl-aspartate synthase reveals how an entrapped tRNA is used like a prosthetic swinging arm in the synthesis of aminoacylated sterols.Nature communications · 2026Article
- The Evolution of the First Code.Genes · 2026Review
- The RNA Revolution in the Central Molecular Biology Dogma Evolution.International journal of molecular sciences · 2024Review
- Proteome-Wide Identification of RNA-dependent proteins and an emerging role for RNAs in Plasmodium falciparum protein complexes.Nature communications · 2024Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Clinically Relevant Mutations of Mycobacterial GatCAB Inform Regulation of Translational Fidelity.mBio · 2021Article
- Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways.PLoS computational biology · 2019Article
- Structural analysis of a plant fatty acid amide hydrolase provides insights into the evolutionary diversity of bioactive acylethanolamides.The Journal of biological chemistry · 2019Article
- Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Crystal structure of Saccharomyces cerevisiae mitochondrial GatFAB reveals a novel subunit assembly in tRNA-dependent amidotransferases.Nucleic acids research · 2014Article
- The predatory bacterium Bdellovibrio bacteriovorus aspartyl-tRNA synthetase recognizes tRNAAsn as a substrate.PloS one · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- Structure and function of allophanate hydrolase.The Journal of biological chemistry · 2013Article
- A tRNA-independent mechanism for transamidosome assembly promotes aminoacyl-tRNA transamidation.The Journal of biological chemistry · 2013Article
- Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase.Nucleic acids research · 2012Article
- Simplification of the genetic code: restricted diversity of genetically encoded amino acids.Nucleic acids research · 2012Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Four out of the 22 aminoacyl-tRNAs (aa-tRNAs) are systematically or alternatively synthesized by an indirect, two-step route requiring an initial mischarging of the tRNA followed by tRNA-dependent conversion of the non-cognate amino acid. During tRNA-dependent asparagine formation, tRNA(Asn) promotes assembly of a ribonucleoprotein particle called transamidosome that allows channelling of the aa-tRNA from non-discriminating aspartyl-tRNA synthetase active site to the GatCAB amidotransferase site. The crystal structure of the Thermus thermophilus transamidosome determined at 3 A resolution reveals a particle formed by two GatCABs, two dimeric ND-AspRSs and four tRNAs(Asn) molecules. In the complex, only two tRNAs are bound in a functional state, whereas the two other ones act as an RNA scaffold enabling release of the asparaginyl-tRNA(Asn) without dissociation of the complex. We propose that the crystal structure represents a transient state of the transamidation reaction. The transamidosome constitutes a transfer-ribonucleoprotein particle in which tRNAs serve the function of both substrate and structural foundation for a large molecular machine.
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