ライフサイエンスコーパス: glutaminyl-tRNA

1 e and glutamine amidotransferase to generate glutaminyl-tRNA.

2 synthetase to synthesize Glu-tRNA(Gln) and a glutaminyl-tRNA amidotransferase to convert Glu-tRNA(Gln

3 alysis of the x-ray crystal structure of the glutaminyl-tRNA aminoacyl synthetase (GlnRS)-tRNA2Gln co

4 y prokaryotes form the amide aminoacyl-tRNAs glutaminyl-tRNA and asparaginyl-tRNA by tRNA-dependent a

5 Archaea make glutaminyl-tRNA (Gln-tRNA(Gln)) in a two-step process; a

6 Asparaginyl-tRNA (Asn-tRNA) and glutaminyl-tRNA (Gln-tRNA) are essential components of p

7 Glutaminyl-tRNA(Gln) and asparaginyl-tRNA(Asn) were like

8 ombination of discriminating asparaginyl and glutaminyl tRNA synthetase (AARS) together with the amid

9 "21st synthetase-tRNA pairs" include E. coli glutaminyl-tRNA synthetase (GlnRS) along with an amber s

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

37 -tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eub

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

39 Glutaminyl-tRNA synthetase and asparaginyl-tRNA syntheta

40 eria lack genes encoding asparaginyl- and/or glutaminyl-tRNA synthetase and consequently rely on an i

41 ecific interactions between Escherichia coli glutaminyl-tRNA synthetase and tRNA(Gln) have been shown

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

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

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

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

46 dy-state kinetic studies of Escherichia coli glutaminyl-tRNA synthetase conclusively demonstrate the

47 d that residues Asp66, Tyr211, and Phe233 in glutaminyl-tRNA synthetase could potentially facilitate

48 either the cytoplasmic nor the mitochondrial glutaminyl-tRNA synthetase distinguishes between the imp

49 y perturb the enzyme-tRNA interface, E. coli glutaminyl-tRNA synthetase does not charge yeast tRNA.

50 Because glutaminyl-tRNA synthetase does not possess a spatially

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

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

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

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

55 2.5 A crystal structure of Escherichia coli glutaminyl-tRNA synthetase in a quaternary complex with

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

57 Glutaminyl-tRNA synthetase is thought to be absent from

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

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

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

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

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

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

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

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

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

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

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