ライフサイエンスコーパス: tRNA(Asp)

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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