ライフサイエンスコーパス: tRNA(Asp)

1 ration to separate enzyme-bound and free pre-tRNAAsp.

2 3' ends of 5S rRNA and the dimeric tRNA(Arg)-tRNA(Asp).

3 trast, a discriminating AspRS forms only Asp-tRNA(Asp).

4 ndent fashion and to transfer glutamate onto tRNA(Asp).

5 t esterified to the 3'-terminal adenosine of tRNA(Asp).

6 de occupying the first anticodon position of tRNA(Asp).

7 s AspRS with the anticodon nucleotide C36 of tRNA(Asp).

8 RNA polyanion or required for binding mature tRNA(Asp).

9 spRS enzymes were thought to be specific for tRNA(Asp).

10 and results in a 75-fold increased K(m) for tRNA(Asp)(1.2 x 10(-5) m) compared with full-length TGT.

11 ng the deafness-associated mitochondrial(mt) tRNA(Asp) 7551A > G mutation.

12 ), an enzyme that in addition to forming Asp-tRNA(Asp) also misacylates tRNA(Asn).

13 Mutations in tRNA(Asp) altering or abolishing interactions with the P

14 riminating (ND-AspRS) and generates both Asp-tRNA(Asp) and the noncanonical, misacylated Asp-tRNA(Asn

15 l-tRNA synthetase (AspRS) that acylates both tRNA(Asp) and tRNA(Asn) with aspartate.

16 sequence results in reduced levels of mature tRNA(Asp) and tRNA(Val) and that altered protein product

17 fied two tRNA genes, trnD and trnV, encoding tRNA(Asp) and tRNA(Val), respectively, composing an oper

18 g AspRS (D-AspRS) specifically generates Asp-tRNA(Asp) and usually coexists with asparaginyl-tRNA syn

19 occur between the 5' leader sequence of pre-tRNAAsp and the protein component of RNase P.

20 wo crystallographically defined tRNAs, yeast tRNAAsp and tRNAPhe, were used as substrates for oxidati

21 that this RNA is aspartic acid transfer RNA (tRNA(Asp)) and that DNMT2 specifically methylated cytosi

22 AspRS2 enzymes still capable of forming Asp-tRNA(Asp) but unable to recognize tRNA(Asn).

23 translation by preventing aminoacylation of tRNA(Asp) by aspartyl-tRNA synthetase (AspRS).

24 hylogeny revealed that discrimination toward tRNA(Asp) by AspRS has evolved independently multiple ti

25 , increasing the affinity of RNase P for pre-tRNAAsp by a factor of 10(4) as determined from both the

26 t both tRNA(Gln) species and a bacterial pre-tRNA(Asp) can be imported in vitro into mitochondria iso

27 A failure in metabolism of mt-tRNA(Asp) caused the variable reductions in mtDNA-encode

28 ein component alter the pH dependence of pre-tRNA(Asp) cleavage catalyzed by RNase P, providing furth

29 Nase P in catalysis of B. subtilis precursor tRNAAsp cleavage has been elucidated using steady-state

30 of magnesium ions bound to the RNase P x pre-tRNA(Asp) complex.

31 as determined from both the ratio of the pre-tRNAAsp dissociation and association rate constants meas

32 es substrate affinity >/=15-fold compared to tRNAAsp due to ground-state destabilization of the enzym

33 ain of the Tetrahymena group I intron, yeast tRNAAsp, Escherichia coli tmRNA and a part of rat 18S rR

34 th the PUA domain can compete with wild-type tRNA(Asp) for binding to full-length and truncated TGT e

35 e same DNA library and then screened for Asp-tRNA(Asp) formation in vivo by growth at the non-permiss

36 MT2 protein restored methylation in vitro to tRNA(Asp) from Dnmt2-deficient strains of mouse, Arabido

37 mid into the 3' ends of either of two tandem tRNAAsp genes, trnD1 and trnD2, located within the attB

38 noncoding RNAs and reduced the stability of tRNA(Asp(GTC)) We also demonstrate the importance of m(5

39 aminoacylation and steady-state level of mt-tRNA(Asp) in mutant cybrids, compared with control cybri

40 luctuations calculated for yeast tRNAPhe and tRNAAsp in the free state, and for tRNAGln complexed wit

41 e, atomic groups of the G73 discriminator of tRNAAsp interact with three side chains of the enzyme.

42 synthetase whose co-crystal structure (with tRNAAsp) is known.

43 ase P holoenzyme (but not RNA alone) for pre-tRNAAsp is further enhanced with a substrate containing

44 be showed a striking selectivity of Pmt1 for tRNA(Asp) methylation, which distinguishes Pmt1 from oth

45 acillus subtilis RNase P RNA for B. subtilis tRNA(Asp) more than 10(3)-fold, consistent with at least

46 eficiency by engineering an E. coli knockout tRNA(Asp) strain, thereby allowing a penetrating analysi

47 , thereby allowing a penetrating analysis of tRNA(Asp) structure and function under conditions that p

48 FP/FA) with a 5' end fluorescein-labeled pre-tRNAAsp substrate.

49 f binding and cleavage were analyzed for pre-tRNAAsp substrates containing 5' leader sequences of var

50 ion altered the structure and function of mt-tRNA(Asp) The primer extension assay demonstrated that t

51 ch, we refine base paired positions in yeast tRNA(Asp) to 4 A rmsd without any preexisting informatio

52 We quantify six well-defined transitions for tRNA(Asp) transcripts between 35 and >75 degrees C, incl

53 emphasizes a complexity for the unfolding of tRNA(Asp) transcripts that is not anticipated by current

54 so, although all three AspRS enzymes charged tRNA(Asp) transcripts, only M. thermautotrophicus AspRS

55 In the aminoacylation of tRNA(Asn) or tRNA(Asp) transcripts, the mutant enzymes displayed at l

56 istinguish fine differences in structure for tRNAAsp transcripts at single nucleotide resolution.

57 from C. albicans have thus been identified: tRNA(Asp), tRNA(Ala) and tRNA(Ile).

58 queuosine (Q) for guanine (G) in tRNA(His), tRNA(Asp), tRNA(Asn), and tRNA(Tyr); this changes the op

59 novel class of tRFs derived from tRNA(Glu), tRNA(Asp), tRNA(Gly), and tRNA(Tyr) that, upon induction

60 Yeast tRNAAsp underwent cleavage at G45 and U66; yeast tRNAPhe

61 ation created the m(1)G37 modification of mt-tRNA(Asp) Using cybrid cell lines generated by transferr

62 by the ratio of the k(cat)K(m) values of Asp-tRNA(Asp) vs. Asp-tRNA(Asn) formation.

63 scriminating enzyme (D-AspRS) forms only Asp-tRNA(Asp), whereas the nondiscriminating enzyme (ND-AspR

64 scriminating enzyme (D-AspRS) forms only Asp-tRNA(Asp), while the nondiscriminating one (ND-AspRS) al

65 Neomycin B and kanamycin B bind to pre-tRNAAsp with a Kd value that is comparable to their IC50