ライフサイエンスコーパス: tRNA(Ile

1 inica ileS T-box in complex with its cognate tRNA(Ile).

2 ylates Nva-tRNA(Ile) at slower rate than Val-tRNA(Ile).

3 ady-state levels of the mature mitochondrial tRNA(Ile).

4 f a small group I ribozyme from Azoarcus pre-tRNA(ile).

5 diting being optimized for hydrolysis of Nva-tRNA(Ile).

6 more efficiently than 5'-extended precursor tRNA(Ile).

7 us been identified: tRNA(Asp), tRNA(Ala) and tRNA(Ile).

8 ylate synthesis but no detectable binding to tRNA(Ile).

9 leRS), by partially mimicking the binding of tRNA(Ile).

10 activated valine from being stably joined to tRNAIle.

11 ied a pathogenic, heteroplasmic mitochondria tRNA(Ile) (4274T>C) mutation.

12 Here we show that tRNA(Ile) affects both the synthetic and editing reactio

13 hat class I IleRS also releases misaminoacyl-tRNAIle and edits it in trans.

14 noacyl-tRNA synthetases, IleRS can mischarge tRNA(Ile) and correct this misacylation through a separa

15 f Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin shows the acceptor strand of the

16 valyl-tRNA synthetase (ValRS) deacylate Val-tRNA(Ile) and Thr-tRNA(Val), respectively.

17 demonstrated specific binding to the cognate tRNA(Ile) and tRNA(Ile)-dependent structural rearrangeme

18 A(Gln) was mainly cytosolic in localization; tRNA(Ile) and tRNA(Lys) were mainly mitochondrial; and t

19 omprised of just the acceptor-TPsiC helix of tRNAIle are substrates for specific aminoacylation by Il

20 n human mitochondrial isoleucine tRNA (hs mt tRNA(Ile)) are associated with cardiomyopathy and opthal

21 r RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes in

22 and consequently IleRS misaminoacylates Nva-tRNA(Ile) at slower rate than Val-tRNA(Ile).

23 es valine (to produce valyl adenylate or Val-tRNA(Ile)) at its active site.

24 hat the RM-A molecule occupies the substrate tRNA(Ile) binding site of Saccharomyces cerevisiae IleRS

25 t-tRNA(Leu(UUR)) or with mutations in the mt-tRNA(Ile), both of which are aminoacylated by Class I mt

26 pecific binding to the cognate tRNA(Ile) and tRNA(Ile)-dependent structural rearrangements consistent

27 eRS.Ile-AMP and IleRS.Ile-tRNAIle, IleRS.Val-tRNAIle does not react with thiols.

28 The conformation of a group I pre-tRNA(ile) from the bacterium Azoarcus was probed by ribo

29 ned a tRNA(Ala) gene, while ISR2 contained a tRNA(Ile) gene.

30 2) for C(32) in the Saccharomyces cerevisiae tRNA(Ile)(IAU) anticodon stem and loop domain (ASL) nega

31 Our data indicate that tRNA(Ile) identity elements were established late and in

32 fficiently as do IleRS.Ile-AMP and IleRS.Ile-tRNAIle, IleRS.Val-tRNAIle does not react with thiols.

33 d Mupirocin shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformati

34 omic deletion or inducible overexpression of tRNA(Ile) introns led to corresponding increases or decr

35 n RNA hairpin that mimics the D-stem/loop of tRNAIle is also unable to induce the hydrolysis of misac

36 Thus, the native tertiary fold of tRNAIle is required to promote efficient editing.

37 t the mischarged valine residue in IleRS.Val-tRNAIle is, most likely, positioned off the enzyme.

38 ize, the 205 nt group I intron from Azoarcus tRNA(Ile) is an exceptionally stable self-splicing RNA.

39 biguity exists in the recognition of certain tRNA(Ile) isoacceptors that are initially transcribed wi

40 encoding tRNA(Gln), the control region, and tRNA(Ile) located downstream of the two ribosomal RNA ge

41 e must be modified at the wobble position by tRNA(Ile) lysidine synthetase (TilS) prior to aminoacyla

42 solated in which the essential gene encoding tRNA(Ile)-lysidine synthetase was deleted for the first

43 so be a determinant for the essential enzyme tRNA(Ile)-lysidine synthetase.

44 s during the mechanistic characterization of tRNA(Ile)-lysidine synthetase.

45 endent formation of lysidine is catalyzed by tRNA(Ile)-lysidine synthetase.

46 Here we show that, in contrast to tRNAIle, minihelixIle is unable to trigger the hydrolysi

47 33P) mutant of Bacillus subtilis that allows tRNA(Ile) mischarging while retaining wild-type Ile-tRNA

48 Finally, the extent to which tRNA(Ile) modulates activation and pre-transfer editing

49 its probable occurrence in the AUA decoding tRNA(Ile) of euryarchaea and crenarchaea.

50 these enzymatic reactions occur between Ile-tRNAIle or Ile-AMP (bound in the synthetic sub-site) and

51 ces comprised of the acceptor-TpsiC helix of tRNA(Ile) or tRNA(Val) were aminoacylated by cognate syn

52 However, the molecular mechanisms by which tRNA(Ile) organizes the synthetic site to enhance pre-tr

53 organisms, the C34 wobble position in these tRNA(Ile) precursors is rapidly modified to lysidine to

54 PCR amplification of the 16S-tRNA(Ile) region of ISR2 permitted rapid phylotyping of

55 he actual distribution of lysidine-dependent tRNA(Ile) rejection by MRS, we have investigated the abi

56 of a small group I intron from Azoarcus pre-tRNA(Ile) showed that tertiary interactions between heli

57 e) mischarging while retaining wild-type Ile-tRNA(Ile) synthesis activity.

58 or-prone and kinetically optimized isoleucyl-tRNA(Ile) synthesis under cellular conditions.

59 etase (MRS) and production of a chimeric Met-tRNA(Ile) that would compromise translational fidelity.

60 first anticodon position of the AUA decoding tRNA(Ile) (tRNA2(Ile)) of bacteria and archaea is essent

61 fl-tRNA(Ile)UAU-generated FRET signals were specifically en

62 5'- and 3'-end maturation of tRNA(Trp)(CCA), tRNA(Ile)(UAU), tRNA(Gln)(CUG), tRNA(Lys)(UUU), and tRNA

63 stent with this model, T7-transcribed mature tRNA(Ile) underwent importation in vitro into isolated m

64 ing group-I intron interrupting the Azoarcus tRNA(Ile) was shortened by ~10% with the removal of heli

65 ructure of Aquifex aeolicus Trbp111 bound to tRNA(Ile), which reveals that Trbp recognizes tRNAs sole

66 ing reaction is dependent on the presence of tRNAIle, which contains discrete D-loop nucleotides that

67 nding assays confirm that RM-A competes with tRNA(Ile) while binding synergistically with L-isoleucin

68 ucine codons, resulting from misacylation of tRNAIle with valine by wildtype IARS1.

69 whose essential function is to aminoacylate tRNA(Ile) with isoleucine.