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1 azei pyrrolysyl-tRNA, as well as a bacterial tyrosyl-tRNA.
2 hat different mode of recognition of the two tyrosyl-tRNAs.
3 has a mutation in the gene (dtd) encoding D-tyrosyl-tRNA deacylase, an enzyme that prevents the misi
4 this is kinetic, based on relative rates of tyrosyl-tRNA formation and tyrosine degradation and expo
5 We also show that the RNAP III-transcribed tyrosyl tRNA gene, SUP4-o, is subject to position effect
7 derived from a Methanocaldococcus jannaschii tyrosyl-tRNA (MjtRNATyrCUA) are expressed under control
8 In this manner, a natural fragment of human tyrosyl tRNA synthetase (TyrRS), mini-TyrRS, has been sh
9 etic code, only the Methanococcus jannaschii tyrosyl tRNA synthetase and tRNA have been used extensiv
10 P design algorithm we then designed a mutant tyrosyl tRNA synthetase to activate O-methyl-l-tyrosine
12 alleles of the nuclear-encoded mitochondrial tyrosyl-tRNA synthetase (Aatm) and the mitochondrial-enc
13 ivation of tyrosine in B. stearothermophilus tyrosyl-tRNA synthetase (Cys-35, His-48, and Lys-233) ar
14 bifunctional Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacyla
16 The Neurospora crassa mitochondrial (mt) tyrosyl-tRNA synthetase (CYT-18 protein) functions in sp
21 ly truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions
22 ility of the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) to suppress mut
23 this technology by introducing an engineered tyrosyl-tRNA synthetase (EcTyrRS) and a tryptophanyl-tRN
24 y explores the twin attributes of Leishmania tyrosyl-tRNA synthetase (LdTyrRS) namely, aminoacylation
26 ne encoding the desired mutant M. jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expressed under con
27 is encoded by human YARS2 for mitochondrial tyrosyl-tRNA synthetase (mt-TyrRS), which aminoacylates
30 , for use in yeast, and mutants of the yeast tyrosyl-tRNA synthetase (TyrRS) along with an amber supp
31 Biological fragments of two human enzymes, tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA sy
34 nation of methods, here we showed that human tyrosyl-tRNA synthetase (TyrRS) distributes to the nucle
40 Structures in isolation and those bound to tyrosyl-tRNA synthetase (TyrRS) show that this ~55-kilod
41 in catalysis by Bacillus stearothermophilus tyrosyl-tRNA synthetase (TyrRS), the temperature depende
43 ecent work demonstrated that RSV facilitates tyrosyl-tRNA synthetase (TyrRS)-dependent activation of
44 We previously showed that tyrosine inhibits tyrosyl-tRNA synthetase (TyrRS)-mediated activation of p
47 protein, the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (TyrRS; CYT-18), is bifunctional
48 children homozygous for a novel mutation in tyrosyl-tRNA synthetase (YARS, c.499C > A, p.Pro167Thr)
49 Previous cellular studies have demonstrated tyrosyl-tRNA synthetase (YARS1 or TyrRS) as a stress res
51 reviously reported that an activated form of tyrosyl-tRNA synthetase (YRS(ACT)) has an extratranslati
52 Notably, a variant within the mitochondrial tyrosyl-tRNA synthetase 2 (YARS2) gene exhibited a signi
54 ssed in Escherichia coli indicate that human tyrosyl-tRNA synthetase aminoacylates human but not B. s
55 for both d-tyrosine activation by wild-type tyrosyl-tRNA synthetase and activation of l-tyrosine by
56 he tyrosine activation reaction in the human tyrosyl-tRNA synthetase and whether it can be replaced b
57 -terminal domain that is unique to the human tyrosyl-tRNA synthetase and whose primary structure is 4
63 ations in glycyl-tRNA synthetase (GlyRS) and tyrosyl-tRNA synthetase cause Charcot-Marie-Tooth (CMT)
64 sequenced several clones identified as human tyrosyl-tRNA synthetase cDNAs by the Human Genome Projec
66 ed sigmoidal behavior presents a paradox, as tyrosyl-tRNA synthetase displays an extreme form of nega
67 K233A variant of Bacillus stearothermophilus tyrosyl-tRNA synthetase displays sigmoidal kinetics simi
68 , was used as a model to explore how a human tyrosyl-tRNA synthetase during evolution acquired novel
69 Arc1p, the carboxyl-terminal domain of human tyrosyl-tRNA synthetase evolved from gene duplication of
71 Furthermore, as is the case for l-tyrosine, tyrosyl-tRNA synthetase exhibits "half-of-the-sites" rea
74 h position of the 'KMSKS' signature motif in tyrosyl-tRNA synthetase have been analyzed to test the h
75 sine suggests that their side chains bind to tyrosyl-tRNA synthetase in similar orientations and that
76 e van't Hoff plots for the binding of ATP to tyrosyl-tRNA synthetase in the absence and presence of s
77 Catalysis of tRNA(Tyr) aminoacylation by tyrosyl-tRNA synthetase involves two steps: activation o
81 the archaebacterial Methanococcus jannaschii tyrosyl-tRNA synthetase may give insights into the histo
82 dy, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding
83 noacyl-tRNA synthetase pair derived from the tyrosyl-tRNA synthetase of Methanococcus jannaschii can
84 dy-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase revealed a 25-fold lower specifi
85 ional comparisons of mammalian and bacterial tyrosyl-tRNA synthetase revealed key differences at resi
86 re motif is absent from all known eukaryotic tyrosyl-tRNA synthetase sequences, except those of highe
87 hypothesis that the KMSSS sequence in human tyrosyl-tRNA synthetase stabilizes the transition state
88 sine activation step is higher for the human tyrosyl-tRNA synthetase than for the B. stearothermophil
89 is appears to be significantly less in human tyrosyl-tRNA synthetase than it is in the B. stearotherm
90 ora crassa CYT-18 protein is a mitochondrial tyrosyl-tRNA synthetase that also promotes self-splicing
91 DI-CMTC is due to a defect in the ability of tyrosyl-tRNA synthetase to catalyze the aminoacylation o
92 ytokine function of the 528-amino acid human tyrosyl-tRNA synthetase was associated with pinpointed u
93 charging of tRNA(Tyr) with noncognate Phe by tyrosyl-tRNA synthetase was responsible for mistranslati
94 tal structure of an active fragment of human tyrosyl-tRNA synthetase with its cognate amino acid anal
95 rmore, we find that downregulation of yars-2/tyrosyl-tRNA synthetase, an NMD target transcript, by da
97 ora crassa CYT-18 protein, the mitochondrial tyrosyl-tRNA synthetase, functions in splicing group I i
98 The Bacillus subtilis tyrS gene, encoding tyrosyl-tRNA synthetase, is a member of the T-box family
99 tant for the initial binding of tRNA(Tyr) to tyrosyl-tRNA synthetase, it does not play a catalytic ro
100 of tyrosyl adenylate by the dimeric class I tyrosyl-tRNA synthetase, operates as well in this homote
102 and "KMSKS." In Bacillus stearothermophilus tyrosyl-tRNA synthetase, the KMSKS motif (230KFGKT234) h
104 ability of an amino acid binding pocket of a tyrosyl-tRNA synthetase, we identified three new variant
105 ly>Val) in YARS2 gene encoding mitochondrial tyrosyl-tRNA synthetase, which interacts with m.11778G>A
117 ineer an orthogonal Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA pair for encoding thioxanth
118 zed 1 and evolved a Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA(CUA) pair to genetically en
121 netic reconstruction, two types of bacterial tyrosyl-tRNA synthetases (TyrRS) form distinct clades wi
122 ing domains of the tryptophanyl (TrpRS)- and tyrosyl-tRNA synthetases (TyrRS) of Bacillus stearotherm
123 a-helix (H0), which is absent from bacterial tyrosyl-tRNA synthetases (TyrRSs), and a downstream regi
124 This insertion is shared with all other tyrosyl-tRNA synthetases and is needed for a critical mi
126 in the Bacillus stearothermophilus and human tyrosyl-tRNA synthetases are largely conserved, several
127 recombinant human and B. stearothermophilus tyrosyl-tRNA synthetases expressed in Escherichia coli i
128 synthetase are 52, 36, and 16% identical to tyrosyl-tRNA synthetases from S. cerevisiae, Methanococc
129 bacterial homologues, a number of eukaryotic tyrosyl-tRNA synthetases require potassium to catalyze t
130 the active sites of the bacterial and human tyrosyl-tRNA synthetases that could be exploited to desi
132 f genomic sequences shows that mitochondrial tyrosyl-tRNA synthetases with structural adaptations sim
133 synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterize
135 and two amino acids that are present only in tyrosyl-tRNA synthetases, Lys82 and Arg86, stabilize the
137 ognition differs between bacterial and human tyrosyl-tRNA synthetases, we sequenced several clones id