ArticleNucleic acids research2012
Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Peculiarities of aminoacyl-tRNA synthetases from trypanosomatids.The Journal of biological chemistry · 2021Article
- Article
- Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation.The Journal of biological chemistry · 2016Article
- The crystal structure of human GlnRS provides basis for the development of neurological disorders.Nucleic acids research · 2016Article
- Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions.The Journal of biological chemistry · 2015Article
- Asc1, homolog of human RACK1, prevents frameshifting in yeast by ribosomes stalled at CGA codon repeats.RNA (New York, N.Y.) · 2015Article
- A new view on crystal harvesting.Journal of applied crystallography · 2014Article
- Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures.American journal of human genetics · 2014Article
- Architecture and metamorphosis.Topics in current chemistry · 2014Review
- An insertion peptide in yeast glycyl-tRNA synthetase facilitates both productive docking and catalysis of cognate tRNAs.Molecular and cellular biology · 2013Article
- The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA.Journal of molecular biology · 2013Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
In all organisms, aminoacyl tRNA synthetases covalently attach amino acids to their cognate tRNAs. Many eukaryotic tRNA synthetases have acquired appended domains, whose origin, structure and function are poorly understood. The N-terminal appended domain (NTD) of glutaminyl-tRNA synthetase (GlnRS) is intriguing since GlnRS is primarily a eukaryotic enzyme, whereas in other kingdoms Gln-tRNA(Gln) is primarily synthesized by first forming Glu-tRNA(Gln), followed by conversion to Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. We report a functional and structural analysis of the NTD of Saccharomyces cerevisiae GlnRS, Gln4. Yeast mutants lacking the NTD exhibit growth defects, and Gln4 lacking the NTD has reduced complementarity for tRNA(Gln) and glutamine. The 187-amino acid Gln4 NTD, crystallized and solved at 2.3 Å resolution, consists of two subdomains, each exhibiting an extraordinary structural resemblance to adjacent tRNA specificity-determining domains in the GatB subunit of the GatCAB amidotransferase, which forms Gln-tRNA(Gln). These subdomains are connected by an apparent hinge comprised of conserved residues. Mutation of these amino acids produces Gln4 variants with reduced affinity for tRNA(Gln), consistent with a hinge-closing mechanism proposed for GatB recognition of tRNA. Our results suggest a possible origin and function of the NTD that would link the phylogenetically diverse mechanisms of Gln-tRNA(Gln) synthesis.
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