ライフサイエンスコーパス: tRNA(Val

1 (1) and 6 U-N(3) (15)N nuclei in a sample of tRNA(Val).

2 on of the deacylated form of the abnormal mt-tRNA(Val).

3 xtremely low (<1%) steady-state levels of mt-tRNA(Val).

4 ics and flexibility of native and unmodified tRNA(val).

5 es are very similar in native and unmodified tRNA(val).

6 that is dependent on the presence of cognate tRNA(Val).

7 on that prevents accumulation of misacylated tRNA(Val).

8 A) modifications, including aminoacylated CP-tRNA(Val).

9 s bound with affinity similar to that of Val-tRNAVal.

10 R spectroscopy of 5-fluorouracil-substituted tRNAVal.

11 y intercalates into the acceptor stem of the tRNAVal.

12 -tRNAMetm (CAU anticodon) and mischarged Met-tRNAVal-1 (CAU anticodon) are substrates for the L/F-tra

13 aminoacylation of alpha-casein, whereas Val-tRNAVal-1 (UAC), Val-tRNAMetm (UAC), and Arg-tRNAMetm (C

14 alyl-tRNA synthetase does not edit wild-type tRNA(Val)(A76) mischarged with isoleucine, presumably be

15 emonstrates rapid degradation of preexisting tRNA(Val(AAC)) accompanied by its de-aminoacylation.

16 t both degradation and deacylation of mature tRNA(Val(AAC)) in a trm8-Delta trm4-Delta strain and res

17 3' exonucleases Rat1 and Xrn1 degrade mature tRNA(Val(AAC)) in yeast mutants lacking m(7)G and m(5)C,

18 healthy growth at 37 degrees C, hypomodified tRNA(Val(AAC)) is at least partially functional and stru

19 rapid tRNA decay (RTD) pathway, since mature tRNA(Val(AAC)) lacking 7-methylguanosine and 5-methylcyt

20 Multiple copies of tRNA(Val(AAC)) suppress the trm8-delta trm4-delta growth

21 e double mutants indicates reduced levels of tRNA(Val(AAC)), consistent with a role of the correspond

22 ates between base pairs corresponding to the tRNAVal acceptor stem in this molecule.

23 ix, and the 5' side of the anticodon stem of tRNAVal against cleavage by double- and single-strand-sp

24 ding of ethidium bromide to Escherichia coli tRNAVal and an RNA minihelix based on the acceptor stem

25 demonstrated for high-resolution analysis of tRNAval and its mutants, including a three-nucleotide de

26 ed the interactions between Escherichia coli tRNAVal and valyl-tRNA synthetase (ValRS) by enzymatic f

27 Mutational analysis of Escherichia coli tRNA(Val) and identity switch experiments with non-cogna

28 ts in reduced levels of mature tRNA(Asp) and tRNA(Val) and that altered protein production during dev

29 r tRNA(Gly) and tRNA(Leu), the mitochondrial tRNA(Val) and tRNA(Pro)) were strongly associated with t

30 A showed severe reduction in abundance of mt-tRNA(Val) , and mildly increased mt-tRNA(Phe) , in subje

31 ular tRNA precursor substrate for tRNA(Ala), tRNA(Val), and tRNA(His).

32 pressors reported here, one (JSN2) encodes a tRNAVal, and the other (JSN3) is an antimorphic allele o

33 the human mitoribosome when levels of the mt-tRNA(Val) are depleted.

34 ted mutant tRNAs as well as 3'-end-truncated tRNA(Val) are mixed noncompetitive inhibitors of the ami

35 d strikingly, when steady-state levels of mt-tRNA(Val) are reduced, human mitoribosome biogenesis dis

36 (un-3(ts)) that has high levels of uncharged tRNA(Val) at all times of the day.

37 ty determinants to productive recognition of tRNA(Val) at the aminoacylation and editing sites, and b

38 nstrate that the dynamics and flexibility of tRNA(val), but not the local or global structure, are si

39 While valylation of the wild-type tRNA(Val) by the class I ValRS was strictly dependent on

40 e)(UAU), tRNA(Gln)(CUG), tRNA(Lys)(UUU), and tRNA(Val)(CAC).

41 itoribosomes have been shown to integrate mt-tRNA(Val) compared with the porcine use of mt-tRNA(Phe)

42 estore steady-state levels of the mutated mt-tRNA(Val), consistent with an increased stability of the

43 The amino acid acceptor arm of tRNAVal contains no other synthetase recognition nucleot

44 oacylation and editing sites, and by probing tRNA(Val) for editing determinants that are distinct fro

45 e positions in the 5' flanking region of the tRNA(Val) gene were repaired more efficiently than the g

46 mutation in the mitochondrial tRNA(Val) (mt-tRNA(Val) ) gene, m.1661A>G, present at nearly 100% hete

47 g the anticodon stem of tRNAPhe with that of tRNAVal, however, converts the tRNA into a good substrat

48 ie-Tooth (CMT) disease, a mutation in the mt-tRNA(Val) , in a Venezuelan family.

49 Evidently, a purine at position 76 of tRNA(Val) is essential for translational editing by ValR

50 s results have shown that the 3'-terminus of tRNA(Val) is recognized differently at the two sites.

51 , a monomeric enzyme, may bind more than one tRNA(Val) molecule.

52 A identified a mutation in the mitochondrial tRNA(Val) (mt-tRNA(Val) ) gene, m.1661A>G, present at ne

53 As a result 3'-end tRNA(Val) mutants, particularly those with 3'-terminal p

54 the generalized decrease in steady-state mt-tRNA(Val) observed in the homoplasmic 1624C>T-cell lines

55 2'-hydroxyl group, that of the U73 mutant of tRNA(Val) occurred at either the 2' or 3'-hydroxyl group

56 Our data demonstrate that only mt-tRNA(Val) or mt-tRNA(Phe) are found in the mitoribosomes

57 2 by overexpressing a mutant tRNA(AAC)(Val) (tRNA(Val*)) or the RNA component of RNase MRP encoded by

58 , and increases the rate of near-cognate Val-tRNA(Val) reacting on a PsiUU codon.

59 plification was performed targeting 16S rRNA/tRNA(val) region having an amplicon size of 530bp using

60 genes, trnD and trnV, encoding tRNA(Asp) and tRNA(Val), respectively, composing an operon at the attB

61 tase (ValRS) deacylate Val-tRNA(Ile) and Thr-tRNA(Val), respectively.

62 Similar results were obtained using pre-tRNA(Val)s containing a 5' leader of various lengths.

63 The mutant tRNA(Val*) showed nuclear accumulation in otherwise wild

64 able to hydrolytically deacylate misacylated tRNA(Val) terminating in 3'-pyrimidines but does deacyla

65 3'-pyrimidines but does deacylate mischarged tRNA(Val) terminating in adenosine or guanosine.

66 red to human tRNA gene promoters (tRNA(Met), tRNA(Val)), the human small nuclear RNA U6 gene (U6) and

67 itment of mitochondrial valine transfer RNA (tRNA(Val)) to play an integral structural role, and chan

68 sequences differ significantly from that of tRNAVal, to efficient valine acceptors.

69 sis of the aminoacylation kinetics of mutant tRNAVal transcripts.

70 , including tRNA(Glu), tRNA(Gly), tRNA(Lys), tRNA(Val), tRNA(His), tRNA(Asp), and tRNA(SeC) to produc

71 he ends of the anticodon- and T-stems in the tRNAVal.ValRS complex is indicative of enzyme-induced co

72 ase.19F NMR also shows that formation of the tRNAVal-valyl-tRNA synthetase complex does not disrupt t

73 elix based on the acceptor stem and T-arm of tRNAVal was investigated by 19F and 1H NMR spectroscopy

74 tion of the nucleotide U73 of tRNA(Cys) into tRNA(Val) was found to confer the flexibility.

75 of the acceptor-TpsiC helix of tRNA(Ile) or tRNA(Val) were aminoacylated by cognate synthetases sele

76 st and steady-state levels of the mutated mt-tRNA(Val) were greater than in the biopsy material, but

77 were mainly mitochondrial; and tRNA(Trp) and tRNA(Val) were shared between the two compartments.

78 e structure and dynamics of Escherichia coli tRNA(val) were studied by NMR spectroscopy.

79 acylation of wild-type and 3'-end mutants of tRNA(Val) with isoleucine.

80 periments to characterize the interaction of tRNA(Val) with the enzyme provide evidence for two tRNA

81 to the recently refined structural model of tRNA(Val) yields the magnitude, asymmetry, and orientati