ArticleNucleic acids research2007
Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 37 citations in OpenAlex.
- Global conformations ofScience advances · 2025Article
- A Ribosomal Protein Homolog Governs Gene Expression and Virulence in a Bacterial Pathogen.Journal of bacteriology · 2022Article
- Glutaminyl-tRNA Synthetase from Pseudomonas aeruginosa: Characterization, structure, and development as a screening platform.Protein science : a publication of the Protein Society · 2020Article
- Combining multi-mutant and modular thermodynamic cycles to measure energetic coupling networks in enzyme catalysis.Structural dynamics (Melville, N.Y.) · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- tRNA acceptor stem and anticodon bases form independent codes related to protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Evolutionary insights about bacterial GlxRS from whole genome analyses: is GluRS2 a chimera?BMC evolutionary biology · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA.Journal of molecular biology · 2013Article
- Utilization of protein intrinsic disorder knowledge in structural proteomics.Biochimica et biophysica acta · 2013Article
- Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase.Nucleic acids research · 2012Article
- Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formation.Nucleic acids research · 2010Article
- Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.The EMBO journal · 2010Article
- Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate tRNA recognition.Nucleic acids research · 2010Article
- Insights into tRNA-dependent amidotransferase evolution and catalysis from the structure of the Aquifex aeolicus enzyme.Journal of molecular biology · 2009Article
- Amino acid modifications on tRNA.Acta biochimica et biophysica Sinica · 2008Review
- From one amino acid to another: tRNA-dependent amino acid biosynthesis.Nucleic acids research · 2008Review
- On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE.Journal of molecular biology · 2008Article
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6 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln) formation. To analyze the peculiarities of the structure-function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 A and a docking model of the synthetase complexed to tRNA(Gln) constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions.
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