ライフサイエンスコーパス: prolyl-tRNA

1 3Gly) in the peptidyl-tRNA binding site, and prolyl-tRNA(2Pro) is bound to the A-site.

2 tmRNA activity results from sequestration of prolyl-tRNA(2Pro) on overexpressed SecM-arrested ribosom

3 Availability of a prolyl-tRNA/aaRS pair should enable site-specific incorp

4 recognize engineered Archaeoglobus fulgidus prolyl-tRNAs (Af-tRNA(Pro)) with three different anticod

5 hetase (ProCysRS) that accurately forms both prolyl-tRNA (Pro-tRNA) and cysteinyl-tRNA (Cys-tRNA) sui

6 somal fine structure to discriminate against prolyl-tRNA(Pro) and promote termination in the absence

7 can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro).

8 report the generation of mutually orthogonal prolyl-tRNA/prolyl-tRNA synthase (ProRS) pairs derived f

9 The evolution of mutually orthogonal prolyl-tRNA/ProRS pairs demonstrates the plasticity of t

10 Specificity is dictated by glutamyl-prolyl tRNA synthetase (EPRS) binding to a 3'UTR element

11 gonist-inducible phosphorylation of glutamyl-prolyl tRNA synthetase (EPRS) by S6K1 in monocytes and a

12 Glutamyl-prolyl tRNA synthetase (EPRS) is a component of the hete

13 mportantly, the EN1-iPeps bound the glutamyl-prolyl tRNA synthetase (EPRS) target, which has been ass

14 entification of a truncated form of glutamyl-prolyl tRNA synthetase (EPRS), a GAIT constituent that m

15 te Ser(886) in the linker domain of glutamyl-prolyl tRNA synthetase (EPRS), the initial event in asse

16 One of these contained the prolyl tRNA synthetase (RS) gene.

17 Our study reveals that the A culicifacies prolyl-tRNA synthetase (AcProRS) is potently inhibited b

18 Here we identify glutamyl-prolyl-tRNA synthetase (EPRS) as an mTORC1-S6K1 target t

19 ere we found that the MSC component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function foll

20 clinical compound that inhibits the glutamyl-prolyl-tRNA synthetase (EPRS) thereby inducing the integ

21 n EPRS1 gene encodes a bifunctional glutamyl-prolyl-tRNA synthetase (EPRS) with two catalytic cores a

22 is heterotetrameric, consisting of glutamyl-prolyl-tRNA synthetase (EPRS), NS1-associated protein 1

23 Glutamyl-prolyl-tRNA synthetase (EPRS1) is a bifunctional aminoac

24 us spike protein, induce binding of glutamyl-prolyl-tRNA synthetase (EPRS1), within an unconventional

25 Here, we show that glutamyl-prolyl-tRNA synthetase (GluProRS), a bifunctional ARS of

26 a novel function of the fused glutamyl- and prolyl-tRNA synthetase (GluProRS).

27 hermautotrophicus contain a dual-specificity prolyl-tRNA synthetase (ProCysRS) that accurately forms

28 Analysis of prolyl-tRNA synthetase (ProRS) across all three taxonomi

29 ermobacter thermautotrophicus proteins using prolyl-tRNA synthetase (ProRS) as the bait.

30 It has previously been proposed that the prolyl-tRNA synthetase (ProRS) enzymes in these organism

31 Class II prolyl-tRNA synthetase (ProRS) from Escherichia coli con

32 Using bacterial prolyl-tRNA synthetase (ProRS) genes as an example, we i

33 discrimination in the synthetic active site, prolyl-tRNA synthetase (ProRS) misactivates and mischarg

34 For the prolyl-tRNA synthetase (ProRS) of Methanococcus jannasch

35 Previous studies have shown that class II prolyl-tRNA synthetase (ProRS) possesses both pre- and p

36 Methanocaldococcus jannaschii prolyl-tRNA synthetase (ProRS) was previously reported t

37 eptor stem contacts made by Escherichia coli prolyl-tRNA synthetase (ProRS), an enzyme of unknown str

38 critical for recognition by Escherichia coli prolyl-tRNA synthetase (ProRS), but not for human ProRS.

39 Here we demonstrate that, for class II prolyl-tRNA synthetase (ProRS), functional coadaptations

40 dococcus jannaschii that was copurified with prolyl-tRNA synthetase (ProRS).

41 ation into proteins due to misrecognition by prolyl-tRNA synthetase (ProRS).

42 amblia indicated the presence of an archaeal prolyl-tRNA synthetase (ProRS).

43 ory AKT signaling is coordinated by glutamyl-prolyl-tRNA synthetase 1 (EPRS1).

44 tase activity being only 4.5-fold lower than prolyl-tRNA synthetase activity.

45 ), accuracy is difficult because the cognate prolyl-tRNA synthetase also recognizes and aminoacylates

46 etase per amino acid, these organisms employ prolyl-tRNA synthetase as the enzyme that carries out Cy

47 NA synthetase and the bifunctional glutamyl-/prolyl-tRNA synthetase at the base of this asymmetric "V

48 nalyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRN

49 s the catalytic glutamyl-tRNA synthetase and prolyl-tRNA synthetase domains.

50 This study uses antibodies directed against prolyl-tRNA synthetase for immunoelectron microscopic lo

51 Translation of the glutamyl-prolyl-tRNA synthetase gene EPRS is enhanced in response

52 The prolyl-tRNA synthetase inhibitor halofuginone blocks IL-

53 complexes, we develop a set of high-affinity prolyl-tRNA synthetase inhibitors, including previously

54 Additionally, we purified recombinant prolyl-tRNA synthetase of A culicifacies and performed e

55 It was reported that M. jannaschii prolyl-tRNA synthetase or the M. jannaschii MJ1477 prote

56 These data place the glutamyl-/prolyl-tRNA synthetase polypeptide in a defined area of

57 insertion domain characteristic of bacterial prolyl-tRNA synthetase species, which is the site of pos

58 ansfer editing mechanism of Escherichia coli prolyl-tRNA synthetase was probed in detail.

59 ain UQ818 with archaeal proS genes (encoding prolyl-tRNA synthetase) or with the Deinococcus radiodur

60 Inhibition of EPRS using a PRS (prolyl-tRNA synthetase)-specific inhibitor, halofuginone

61 4444 C > A; p.Pro1482Thr), encoding glutamyl-prolyl-tRNA synthetase, consistent with HLD15.

62 years, aminoacyl-tRNA synthetases, including prolyl-tRNA synthetase, have emerged as attractive targe

63 A freestanding homologue of the prolyl-tRNA synthetase-editing domain, the PrdX protein

64 establish a path for rational development of prolyl-tRNA synthetase-targeted anti-malarial therapies.

65 is not required for pre-transfer editing by prolyl-tRNA synthetase.

66 chii is an auxiliary function of a canonical prolyl-tRNA synthetase.

67 in corresponded to the predicted sequence of prolyl-tRNA synthetase.

68 c localization of the bifunctional glutamyl-/prolyl-tRNA synthetase.

69 d Ala-tRNA(Pro) that has been synthesized by prolyl-tRNA synthetase.

70 sion of a distinct isoform of bacterial-type prolyl-tRNA synthetase.

71 to the change in the recognition element for prolyl-tRNA-synthetase.

72 Prolyl-tRNA synthetases (ProRS) have been shown to misac

73 Prolyl-tRNA synthetases (ProRS) mischarge tRNA(Pro) with

74 cific editing domain (INS) of most bacterial prolyl-tRNA synthetases (ProRSs) and an autonomous singl

75 Prolyl-tRNA synthetases (ProRSs) are notable due to thei

76 Prolyl-tRNA synthetases (ProRSs) can be divided into two

77 Prolyl-tRNA synthetases (ProRSs) from all three domains

78 Through primary sequence alignments, prolyl-tRNA synthetases (ProRSs) have been divided into

79 For example, prolyl-tRNA synthetases (ProRSs) mischarge alanine and c

80 Bacterial prolyl-tRNA synthetases and some smaller paralogs, YbaK

81 tionship between the evolutionary pattern of prolyl-tRNA synthetases and the emergence of two enzymat

82 Prolyl-tRNA synthetases are known to mischarge tRNA(Pro)

83 we conclude that the evolutionary pattern of prolyl-tRNA synthetases does not obviously conform to th

84 he pre-transfer editing activity of class II prolyl-tRNA synthetases from five species representing a

85 iting domain (INS) present in most bacterial prolyl-tRNA synthetases that hydrolyzes smaller Ala-tRNA

86 p biochemical assay for Plasmodium and human prolyl-tRNA synthetases that overcomes critical limitati

87 ar, the entire set of available sequences of prolyl-tRNA synthetases was analyzed in this way.