EC Number   |
General Information |
Reference |
|---|
    6.1.1.17 | more |
analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview |
-, 745552 |
| 6.1.1.17 | physiological function |
cytoplasmic glutamyl tRNA synthetase gene ers1 is an Moc3 interacting element. Cell growth is moderately affected by cGluRS over-expression under de-repressed conditions. Over-expression of ers1 stimulates sexual differentiation |
702746 |
| 6.1.1.17 | malfunction |
EPRS-haploid (Eprs+/-) mice show enhanced viremia and inflammation and delayed viral clearance |
745867 |
| 6.1.1.17 | more |
homology structure modeling using structures of GluRSs identified from Burkholderia thailandensis and Thermosynechococcus elongatus, Uniprot IDs Q2SX36 and Q8DLI5, respectively, as search template, molecular docking |
746179 |
| 6.1.1.17 | physiological function |
in cells containing glutaminyl-tRNA synthetase, GlnRS, discriminating GluRS specifically aminoacylates tRNAGlu with glutamate. One of two GluRSs from the extremophile Acidithiobacillus ferrooxidans, is inactivated when intracellular heme is elevated suggesting a specific role for GluRS1 in the regulation of tetrapyrrole biosynthesis |
714031 |
| 6.1.1.17 | evolution |
many bacterial GluRS are capable of recognizing two tRNA substrates: tRNAGlu and tRNAGln, e.g. GluRS from such as Bacillus subtilis, Thermosynechococcus elongatus, and Mycobacterium tuberculosis. In bacteria such as Escherichia coli and Thermus thermophilus that possess glutaminyl-tRNA synthetase (GlnRS), the cognate aminoacylating enzyme for tRNAGln, GluRS exclusively glutamylates tRNAGlu. tRNA-GluRS interaction in bacteria is also associated with phylum-specific idiosyncrasies, structure-function analysis, overview |
743955 |
| 6.1.1.17 | physiological function |
mechanism of translation control of enzyme EPRS involving increased translation initiation stringency during stress-induced eIF2alpha-P, facilitated ribosome bypass of upstream ORFs, allowing for increased translation of the EPRS coding region. The 5'-leader of the EPRS mRNA directs preferential translation. Although a portion of the ribosomes that translate uORF2 can reinitiate downstream, scanning ribosomes also bypass uORF2 because of its noncanonical UUG1 initiation codon and initiate translation at the downstream coding sequence. UUG1 and CUG2 are overall repressing elements in EPRS translation control. Model for EPRS translation control, overview |
745339 |
| 6.1.1.17 | physiological function |
mitochondrial glutamyl tRNA synthetase gene ers2 is an Moc3 interacting element. Cell growth is severely affected by ers2 over-expression under de-repressed conditions. Under repressed conditions, the cells multiply quickly. In addition, cells over-expressing ers2 show higher mating efficiency than control |
702746 |
| 6.1.1.17 | more |
targets for oxidation-based inhibition are cysteines from a SWIM zinc-binding motif located in the tRNA acceptor helix-binding domain. Oxidation of the metal-binding site cysteine of GluRS1 significantly impaired catalysis. Also, binding of ATP or tRNA protects the distant cysteines of the SWIM motif |
714031 |
| 6.1.1.17 | evolution |
the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. The affinity of GluRS for glutamate is significantly increased when Arc1p is not associated with the enzyme. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme |
-, 745552 |
