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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

42 The prolyl-tRNA synthetase inhibitor halofuginone blocks IL-

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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