ライフサイエンスコーパス: prolyl-tRNA synthetase

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

28 The prolyl-tRNA synthetase inhibitor halofuginone blocks IL-

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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