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1 pressors reported here, one (JSN2) encodes a tRNAVal, and the other (JSN3) is an antimorphic allele o
2 ular tRNA precursor substrate for tRNA(Ala), tRNA(Val), and tRNA(His).
3 ts in reduced levels of mature tRNA(Asp) and tRNA(Val) and that altered protein production during dev
4 genes, trnD and trnV, encoding tRNA(Asp) and tRNA(Val), respectively, composing an operon at the attB
5 were mainly mitochondrial; and tRNA(Trp) and tRNA(Val) were shared between the two compartments.
6 e)(UAU), tRNA(Gln)(CUG), tRNA(Lys)(UUU), and tRNA(Val)(CAC).
7 that is dependent on the presence of cognate tRNA(Val).
8      Mutational analysis of Escherichia coli tRNA(Val) and identity switch experiments with non-cogna
9 ding of ethidium bromide to Escherichia coli tRNAVal and an RNA minihelix based on the acceptor stem
10 ed the interactions between Escherichia coli tRNAVal and valyl-tRNA synthetase (ValRS) by enzymatic f
11                           As a result 3'-end tRNA(Val) mutants, particularly those with 3'-terminal p
12 healthy growth at 37 degrees C, hypomodified tRNA(Val(AAC)) is at least partially functional and stru
13 tion of the nucleotide U73 of tRNA(Cys) into tRNA(Val) was found to confer the flexibility.
14 3' exonucleases Rat1 and Xrn1 degrade mature tRNA(Val(AAC)) in yeast mutants lacking m(7)G and m(5)C,
15 t both degradation and deacylation of mature tRNA(Val(AAC)) in a trm8-Delta trm4-Delta strain and res
16 rapid tRNA decay (RTD) pathway, since mature tRNA(Val(AAC)) lacking 7-methylguanosine and 5-methylcyt
17 red to human tRNA gene promoters (tRNA(Met), tRNA(Val)), the human small nuclear RNA U6 gene (U6) and
18 -tRNAMetm (CAU anticodon) and mischarged Met-tRNAVal-1 (CAU anticodon) are substrates for the L/F-tra
19 able to hydrolytically deacylate misacylated tRNA(Val) terminating in 3'-pyrimidines but does deacyla
20 on that prevents accumulation of misacylated tRNA(Val).
21 3'-pyrimidines but does deacylate mischarged tRNA(Val) terminating in adenosine or guanosine.
22 r tRNA(Gly) and tRNA(Leu), the mitochondrial tRNA(Val) and tRNA(Pro)) were strongly associated with t
23 on of the deacylated form of the abnormal mt-tRNA(Val).
24 itoribosomes have been shown to integrate mt-tRNA(Val) compared with the porcine use of mt-tRNA(Phe)
25 st and steady-state levels of the mutated mt-tRNA(Val) were greater than in the biopsy material, but
26 estore steady-state levels of the mutated mt-tRNA(Val), consistent with an increased stability of the
27 d strikingly, when steady-state levels of mt-tRNA(Val) are reduced, human mitoribosome biogenesis dis
28 xtremely low (<1%) steady-state levels of mt-tRNA(Val).
29            Our data demonstrate that only mt-tRNA(Val) or mt-tRNA(Phe) are found in the mitoribosomes
30  the generalized decrease in steady-state mt-tRNA(Val) observed in the homoplasmic 1624C>T-cell lines
31 the human mitoribosome when levels of the mt-tRNA(Val) are depleted.
32                                   The mutant tRNA(Val*) showed nuclear accumulation in otherwise wild
33 sis of the aminoacylation kinetics of mutant tRNAVal transcripts.
34        Evidently, a purine at position 76 of tRNA(Val) is essential for translational editing by ValR
35 periments to characterize the interaction of tRNA(Val) with the enzyme provide evidence for two tRNA
36  to the recently refined structural model of tRNA(Val) yields the magnitude, asymmetry, and orientati
37 2'-hydroxyl group, that of the U73 mutant of tRNA(Val) occurred at either the 2' or 3'-hydroxyl group
38 acylation of wild-type and 3'-end mutants of tRNA(Val) with isoleucine.
39 ty determinants to productive recognition of tRNA(Val) at the aminoacylation and editing sites, and b
40 (1) and 6 U-N(3) (15)N nuclei in a sample of tRNA(Val).
41 s results have shown that the 3'-terminus of tRNA(Val) is recognized differently at the two sites.
42                           Multiple copies of tRNA(Val(AAC)) suppress the trm8-delta trm4-delta growth
43 e double mutants indicates reduced levels of tRNA(Val(AAC)), consistent with a role of the correspond
44               The amino acid acceptor arm of tRNAVal contains no other synthetase recognition nucleot
45 elix based on the acceptor stem and T-arm of tRNAVal was investigated by 19F and 1H NMR spectroscopy
46 ix, and the 5' side of the anticodon stem of tRNAVal against cleavage by double- and single-strand-sp
47 g the anticodon stem of tRNAPhe with that of tRNAVal, however, converts the tRNA into a good substrat
48  sequences differ significantly from that of tRNAVal, to efficient valine acceptors.
49 , a monomeric enzyme, may bind more than one tRNA(Val) molecule.
50  of the acceptor-TpsiC helix of tRNA(Ile) or tRNA(Val) were aminoacylated by cognate synthetases sele
51      Similar results were obtained using pre-tRNA(Val)s containing a 5' leader of various lengths.
52 emonstrates rapid degradation of preexisting tRNA(Val(AAC)) accompanied by its de-aminoacylation.
53 oacylation and editing sites, and by probing tRNA(Val) for editing determinants that are distinct fro
54 itment of mitochondrial valine transfer RNA (tRNA(Val)) to play an integral structural role, and chan
55 R spectroscopy of 5-fluorouracil-substituted tRNAVal.
56 e positions in the 5' flanking region of the tRNA(Val) gene were repaired more efficiently than the g
57 he ends of the anticodon- and T-stems in the tRNAVal.ValRS complex is indicative of enzyme-induced co
58 ase.19F NMR also shows that formation of the tRNAVal-valyl-tRNA synthetase complex does not disrupt t
59 y intercalates into the acceptor stem of the tRNAVal.
60 ates between base pairs corresponding to the tRNAVal acceptor stem in this molecule.
61 tase (ValRS) deacylate Val-tRNA(Ile) and Thr-tRNA(Val), respectively.
62 ted mutant tRNAs as well as 3'-end-truncated tRNA(Val) are mixed noncompetitive inhibitors of the ami
63            While valylation of the wild-type tRNA(Val) by the class I ValRS was strictly dependent on
64 alyl-tRNA synthetase does not edit wild-type tRNA(Val)(A76) mischarged with isoleucine, presumably be
65 2 by overexpressing a mutant tRNA(AAC)(Val) (tRNA(Val*)) or the RNA component of RNase MRP encoded by
66 s bound with affinity similar to that of Val-tRNAVal.
67  aminoacylation of alpha-casein, whereas Val-tRNAVal-1 (UAC), Val-tRNAMetm (UAC), and Arg-tRNAMetm (C

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