ライフサイエンスコーパス: glutaminyl-tRNA synthetase

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

3 However, it was previously shown that glutaminyl-tRNA synthetase activity is present in Leishm

4 base frequencies for the seryl, aspartyl and glutaminyl tRNA-synthetase and U1 RNA-protein complexes.

5 Glutaminyl-tRNA synthetase and asparaginyl-tRNA syntheta

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

8 Archaebacteria lack glutaminyl-tRNA synthetase and utilize a two-step pathwa

9 as those for asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase are absent.

10 undwork for the acquisition of the canonical glutaminyl-tRNA synthetase by lateral gene transfer from

11 different from that reported for the tRNAGln-glutaminyl-tRNA synthetase complex.

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.

16 Because glutaminyl-tRNA synthetase does not possess a spatially

17 The binding of glutaminyl-tRNA synthetase from Escherichia coli to seve

18 ells by regulating expression of the E. coli glutaminyl-tRNA synthetase gene in an inducible, cell-ty

19 Concomitant expression of the E. coli glutaminyl-tRNA synthetase gene results in aminoacylatio

20 Glutaminyl-tRNA synthetase generates Gln-tRNA(Gln) 10(7)

21 "21st synthetase-tRNA pairs" include E. coli glutaminyl-tRNA synthetase (GlnRS) along with an amber s

22 ependent on coexpression of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) along with the E. col

23 e free state, and for tRNAGln complexed with glutaminyl-tRNA synthetase (GlnRS) are in good agreement

24 The crystal structure of E. coli glutaminyl-tRNA synthetase (GlnRS) bound to native tRNA1

25 Helicobacter pylori does not have a glutaminyl-tRNA synthetase (GlnRS) but has two divergent

26 alter amino acid specificities of TrpRS and glutaminyl-tRNA synthetase (GlnRS) by mutagenesis withou

27 Eukaryotic glutaminyl-tRNA synthetase (GlnRS) contains an appended

28 The glutaminyl-tRNA synthetase (GlnRS) enzyme, which pairs g

29 Glutaminyl-tRNA synthetase (GlnRS) evolved later and is

30 alysis of aminoacylation of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) has revealed that the

31 due from glutamyl-tRNA synthetase (GluRS) to glutaminyl-tRNA synthetase (GlnRS) improves the K(M) of

32 The structure of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) in complex with tRNAG

33 in the crystal structure of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) in complex with tRNAG

34 The N-terminal appended domain (NTD) of glutaminyl-tRNA synthetase (GlnRS) is intriguing since G

35 Glutaminyl-tRNA synthetase (GlnRS) is one noteworthy exc

36 Cytosolic glutaminyl-tRNA synthetase (GlnRS) is the singular enzym

37 previously described mutant Escherichia coli glutaminyl-tRNA synthetase (GlnRS) proteins that incorre

38 eady-state and transient kinetic analyses of glutaminyl-tRNA synthetase (GlnRS) reveal that the enzym

39 rom the catalytic domain of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) were replaced with th

40 karyotes and some bacteria employ a specific glutaminyl-tRNA synthetase (GlnRS) which other Bacteria,

41 nthesis, which in eukaryotes is catalyzed by glutaminyl-tRNA synthetase (GlnRS), while most bacteria,

42 aminoacyl-tRNA synthetase, including E. coli glutaminyl-tRNA synthetase (GlnRS), yet functions with t

43 glutamine binding pocket in Escherichia coli glutaminyl-tRNA synthetase (GlnRS).

44 acent to the active site of Escherichia coli glutaminyl-tRNA synthetase (GlnRS).

45 on by asparaginyl-tRNA synthetase (AsnRS) or glutaminyl-tRNA synthetase (GlnRS).

46 Most bacteria and all archaea lack a glutaminyl-tRNA synthetase (GlnRS); instead, Gln-tRNA(Gl

47 Here we show for Escherichia coli glutaminyl-tRNA synthetase (GlnRS; EC 6.1.1.18) that the

48 2.5 A crystal structure of Escherichia coli glutaminyl-tRNA synthetase in a quaternary complex with

49 n) that may be preventing the acquisition of glutaminyl-tRNA synthetase in Archaea.

50 A is dependent upon the expression of E.coli glutaminyl-tRNA synthetase, indicating that none of the

51 Glutaminyl-tRNA synthetase is thought to be absent from

52 nsamidation, and the eukaryal cytoplasm uses glutaminyl-tRNA synthetase, it appears that the three do

53 The monomeric yeast Saccharomyces cerevisiae glutaminyl-tRNA synthetase, like several other class I e

54 gical activity of an essential RNA.Bacterial glutaminyl-tRNA synthetase poorly aminoacylates yeast tR

55 dentification of mutations in QARS (encoding glutaminyl-tRNA synthetase [QARS]) as the causative vari

56 catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, respectively.

57 structure of the complex between tRNAGln and glutaminyl-tRNA synthetase shows that the enzyme interac

58 inoacylated in vitro by the Escherichia coli glutaminyl-tRNA synthetase, suggesting that the lack of

59 gly, T. brucei uses the same eukaryotic-type glutaminyl-tRNA synthetase to form mitochondrial and cyt

60 dues were randomly mutated and the resulting glutaminyl-tRNA synthetase variants were screened in viv

61 The cocrystal structure of the class I glutaminyl-tRNA synthetase with tRNAGln revealed an unco