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1 ombination of discriminating asparaginyl and glutaminyl tRNA synthetase (AARS) together with the amid
2 -tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eub
4 base frequencies for the seryl, aspartyl and glutaminyl tRNA-synthetase and U1 RNA-protein complexes.
6 eria lack genes encoding asparaginyl- and/or glutaminyl-tRNA synthetase and consequently rely on an i
7 ecific interactions between Escherichia coli glutaminyl-tRNA synthetase and tRNA(Gln) have been shown
10 undwork for the acquisition of the canonical glutaminyl-tRNA synthetase by lateral gene transfer from
12 dy-state kinetic studies of Escherichia coli glutaminyl-tRNA synthetase conclusively demonstrate the
13 d that residues Asp66, Tyr211, and Phe233 in glutaminyl-tRNA synthetase could potentially facilitate
14 either the cytoplasmic nor the mitochondrial glutaminyl-tRNA synthetase distinguishes between the imp
15 y perturb the enzyme-tRNA interface, E. coli glutaminyl-tRNA synthetase does not charge yeast tRNA.
18 ells by regulating expression of the E. coli glutaminyl-tRNA synthetase gene in an inducible, cell-ty
21 integrity, and translation, and identify the glutaminyl-tRNA synthetase Gln4 as the target of N-pyrim
22 "21st synthetase-tRNA pairs" include E. coli glutaminyl-tRNA synthetase (GlnRS) along with an amber s
23 ependent on coexpression of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) along with the E. col
24 e free state, and for tRNAGln complexed with glutaminyl-tRNA synthetase (GlnRS) are in good agreement
27 alter amino acid specificities of TrpRS and glutaminyl-tRNA synthetase (GlnRS) by mutagenesis withou
31 alysis of aminoacylation of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) has revealed that the
32 due from glutamyl-tRNA synthetase (GluRS) to glutaminyl-tRNA synthetase (GlnRS) improves the K(M) of
34 in the crystal structure of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) in complex with tRNAG
38 previously described mutant Escherichia coli glutaminyl-tRNA synthetase (GlnRS) proteins that incorre
39 eady-state and transient kinetic analyses of glutaminyl-tRNA synthetase (GlnRS) reveal that the enzym
40 rom the catalytic domain of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) were replaced with th
41 karyotes and some bacteria employ a specific glutaminyl-tRNA synthetase (GlnRS) which other Bacteria,
42 nthesis, which in eukaryotes is catalyzed by glutaminyl-tRNA synthetase (GlnRS), while most bacteria,
43 aminoacyl-tRNA synthetase, including E. coli glutaminyl-tRNA synthetase (GlnRS), yet functions with t
49 2.5 A crystal structure of Escherichia coli glutaminyl-tRNA synthetase in a quaternary complex with
52 A is dependent upon the expression of E.coli glutaminyl-tRNA synthetase, indicating that none of the
54 nsamidation, and the eukaryal cytoplasm uses glutaminyl-tRNA synthetase, it appears that the three do
55 The monomeric yeast Saccharomyces cerevisiae glutaminyl-tRNA synthetase, like several other class I e
56 gical activity of an essential RNA.Bacterial glutaminyl-tRNA synthetase poorly aminoacylates yeast tR
57 dentification of mutations in QARS (encoding glutaminyl-tRNA synthetase [QARS]) as the causative vari
58 e aaRSs, the glutamyl-tRNA synthetase (ERS), glutaminyl-tRNA synthetase (QRS), and methionyl-tRNA syn
60 structure of the complex between tRNAGln and glutaminyl-tRNA synthetase shows that the enzyme interac
61 inoacylated in vitro by the Escherichia coli glutaminyl-tRNA synthetase, suggesting that the lack of
62 gly, T. brucei uses the same eukaryotic-type glutaminyl-tRNA synthetase to form mitochondrial and cyt
63 dues were randomly mutated and the resulting glutaminyl-tRNA synthetase variants were screened in viv
64 ells in which arginyl-tRNA synthetase and/or glutaminyl-tRNA synthetase were absent from the MSC.