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1 nding fold surface opposite that which binds tRNATyr.
2 motif is also important for interacting with tRNA(Tyr).
3 t of human TyrRS is regulated by its cognate tRNA(Tyr).
4 uclear distribution of TyrRS is regulated by tRNA(Tyr).
5 s signature feature of the anticodon loop in tRNA(Tyr).
6 and its subsequent transfer to the 3' end of tRNA(Tyr).
7 t which the tyrosyl moiety is transferred to tRNA(Tyr).
8 nding surface distinct from that which binds tRNA(Tyr).
9 r of both l- and d-tyrosine to the 3' end of tRNA(Tyr).
10 h the viral TLS was replaced with a cellular tRNA(Tyr).
11 with the D-/anticodon arm stacked helices of tRNA(Tyr).
12 e from the tyrosyl-adenylate intermediate to tRNA(Tyr).
13 e from the tyrosyl-adenylate intermediate to tRNA(Tyr).
14 oup I introns, in addition to aminoacylating tRNA(Tyr).
18 suggest that catalysis of the second step of tRNA(Tyr) aminoacylation involves stabilization of a tra
19 ylalanine (AzF) through the use of bacterial tRNA(Tyr) and a modified version of TyrRS, AzFRS, in Sch
20 onal proteins that both charge mitochondrial tRNA(Tyr) and act as splicing cofactors for autocatalyti
21 18 protein) both aminoacylates mitochondrial tRNA(Tyr) and acts as a structure-stabilizing splicing c
23 nal proteins that aminoacylate mitochondrial tRNA(Tyr) and are structure-stabilizing splicing cofacto
25 ious studies showed that CYT-18 has distinct tRNA(Tyr) and group I intron-binding sites, with the lat
26 ctional and both aminoacylates mitochondrial tRNA(Tyr) and promotes the splicing of mitochondrial gro
27 ce of the dihydrouridine (DHU) arm stem from tRNA(Tyr) and the use of CCG as an initiation codon for
28 d on the B.subtilis tyrS antiterminator with tRNA(Tyr) and tRNA acceptor stem models, using a gel shi
29 d analysis of structural differences between tRNA(Tyr) and tRNA species which interact inefficiently
30 endent and -independent pathways on the SUP4 tRNA(Tyr) and U6 snRNA (SNR6) genes, respectively, and f
31 on mechanism for the transfer of tyrosine to tRNA(Tyr), and suggest that catalysis of the second step
32 acylates human but not B. stearothermophilus tRNATyr, and vice versa, supporting the original hypothe
33 hermodynamic properties of Bacillus subtilis tRNA(Tyr) anticodon arms containing the natural base mod
34 us subtilis Our structure of QueG bound to a tRNA(Tyr) anticodon stem loop shows how this enzyme uses
36 ty of tRNACys at a cognate codon and that of tRNATyr at a near-cognate codon, suggesting that i6A37 p
37 al bi-ter kinetic mechanism in which preQ(1)-tRNA(Tyr) binds first followed by AdoMet, with product r
39 merase III produces not only full-length pre-tRNATyr but also short oligonucleotides, indicating that
41 ity and TyrRS activity with the N. crassa mt tRNA(Tyr), but not for TyrRS activity with Escherichia c
42 SU and ND1 introns with that in N. crassa mt tRNA(Tyr) by constructing three-dimensional models based
43 turnover kinetics for the aminoacylation of tRNA(Tyr) by D-tyrosine were monitored using stopped-flo
44 l for Val-tRNA(Glu) to -8.1 kcal/mol for Val-tRNA(Tyr), clearly establishing EF-Tu*GTP as a sequence-
46 ependently, interactions of RNase P with pre-tRNA(Tyr) containing either the 5' leader, the 3' traile
49 pectation was confirmed by RNAi knockdown of tRNA(Tyr) expression, which led to robust nuclear import
54 /-2 on the nontranscribed strand of the SUP4 tRNATyr gene along with an [alpha-32P]dNMP by primer ext
57 TFIIIB with the region upstream of the SUP4 tRNATyr gene was extensively probed by use of photoreact
58 merase III transcription complex on the SUP4 tRNATyr gene was probed at distances of approximately 10
61 a brucei, the single intron-containing tRNA (tRNA(Tyr)GUA) is responsible for decoding all tyrosine c
62 cal editing events, within the intron of pre-tRNA(Tyr)GUA, involving guanosine-to-adenosine transitio
63 ation of tyrosine and subsequent transfer to tRNA(Tyr) has been determined using single turnover kine
64 not for TyrRS activity with Escherichia coli tRNA(Tyr), implying a somewhat different mode of recogni
65 an overexpression system was constructed for tRNA(Tyr) in an E. coli queA deletion mutant to allow fo
66 clear import of TyrRS directly controlled by tRNA(Tyr) in higher organisms, the NLS of lower eukaryot
67 , 5'-unphosphorylated in vitro transcript of tRNA(Tyr) induced IFN-alpha, thus revealing posttranscri
71 haracterized substrate-enzyme conjugate [pre-tRNA(Tyr)-Methanocaldococcus jannaschii (Mja) RPR] to in
72 ld decrease in the self-cleavage rate of pre-tRNA(Tyr)-MjaDeltaU RPR compared to the wild type, and t
73 a large shift on its flexible linker to bind tRNA(Tyr) or the intron RNA on either side of the cataly
76 ns affects either the initial binding of the tRNA(Tyr) substrate or the stability of the transition s
78 e does not affect the initial binding of the tRNA(Tyr) substrate, it destabilizes the transition stat
79 inoacylate the amber suppressor derived from tRNATyr (supF) with glutamine were cocrystallized with w
81 Consistently, overexpression of a mutant pre-tRNA(Tyr) that cannot be processed by RNase P had a Gcd(
82 ed from tRNA(Glu), tRNA(Asp), tRNA(Gly), and tRNA(Tyr) that, upon induction, suppress the stability o
83 (G) in tRNA(His), tRNA(Asp), tRNA(Asn), and tRNA(Tyr); this changes the optimal binding from codons
84 otif is important for the initial binding of tRNA(Tyr) to tyrosyl-tRNA synthetase, it does not play a
88 approach based on catalytic DNA, a panel of tRNA(Tyr) variants featuring differential modification p
91 synthetase to catalyze the aminoacylation of tRNA(Tyr), we have expressed each of these variants as r
92 cylated efficiency and steady-state level of tRNA(Tyr) were markedly decreased in the cell lines deri
94 physically with tRNAs and in particular with tRNA(Tyr), which are present in the modifier and with th
95 o acid pools, suggesting that mischarging of tRNA(Tyr) with noncognate Phe by tyrosyl-tRNA synthetase
96 ynthetase where contacts of Escherichia coli tRNA(Tyr) with the alpha2 dimeric protein have been loca
97 and noncompetitive patterns against preQ(1)-tRNA(Tyr), with K(i) values of 133 +/- 18 and 4.6 +/- 0.
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