ArticleNucleic acids research2010
Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate tRNA recognition.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 31 citations in OpenAlex.
- Loss of the ApJournal of bacteriology · 2026Article
- Resurrecting tRNAs of the Last Universal Common Ancestor (Commonote) Toward Rebuilding the Ancient Translation System.Journal of molecular evolution · 2026Article
- Global conformations ofScience advances · 2025Article
- Clinically Relevant Mutations of Mycobacterial GatCAB Inform Regulation of Translational Fidelity.mBio · 2021Article
- Forward Genetics Reveals aFrontiers in microbiology · 2020Article
- Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Pathogenic variants in glutamyl-tRNANature communications · 2018Article
- Plasmodium Apicoplast Gln-tRNAGln Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites.The Journal of biological chemistry · 2015Article
- Computational analysis of ammonia transfer along two intramolecular tunnels in Staphylococcus aureus glutamine-dependent amidotransferase (GatCAB).The journal of physical chemistry. B · 2015Article
- 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
- The Dnmt2 RNA methyltransferase homolog of Geobacter sulfurreducens specifically methylates tRNA-Glu.Nucleic acids research · 2014Article
- Crystal structure of Saccharomyces cerevisiae mitochondrial GatFAB reveals a novel subunit assembly in tRNA-dependent amidotransferases.Nucleic acids research · 2014Article
- Article
- The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA.Journal of molecular biology · 2013Article
- Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase.Nucleic acids research · 2012Article
- Gln-tRNAGln synthesis in a dynamic transamidosome from Helicobacter pylori, where GluRS2 hydrolyzes excess Glu-tRNAGln.Nucleic acids research · 2011Article
- Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.Nature · 2010Article
- Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.The EMBO journal · 2010Article
- The archaeal transamidosome for RNA-dependent glutamine biosynthesis.Nucleic acids research · 2010Article
- A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli.FEBS letters · 2010Article
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6 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
In many prokaryotes the biosynthesis of the amide aminoacyl-tRNAs, Gln-tRNA(Gln) and Asn-tRNA(Asn), proceeds by an indirect route in which mischarged Glu-tRNA(Gln) or Asp-tRNA(Asn) is amidated to the correct aminoacyl-tRNA catalyzed by a tRNA-dependent amidotransferase (AdT). Two types of AdTs exist: bacteria, archaea and organelles possess heterotrimeric GatCAB, while heterodimeric GatDE occurs exclusively in archaea. Bacterial GatCAB and GatDE recognize the first base pair of the acceptor stem and the D-loop of their tRNA substrates, while archaeal GatCAB recognizes the tertiary core of the tRNA, but not the first base pair. Here, we present the crystal structure of the full-length Staphylococcus aureus GatCAB. Its GatB tail domain possesses a conserved Lys rich motif that is situated close to the variable loop in a GatCAB:tRNA(Gln) docking model. This motif is also conserved in the tail domain of archaeal GatCAB, suggesting this basic region may recognize the tRNA variable loop to discriminate Asp-tRNA(Asn) from Asp-tRNA(Asp) in archaea. Furthermore, we identified a 3(10) turn in GatB that permits the bacterial GatCAB to distinguish a U1-A72 base pair from a G1-C72 pair; the absence of this element in archaeal GatCAB enables the latter enzyme to recognize aminoacyl-tRNAs with G1-C72 base pairs.
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