ライフサイエンスコーパス: aminoacylation

1 ted with RNA and thioester cofactor-mediated aminoacylation.

2 ate amino acids that are misactivated during aminoacylation.

3 et trimmed before addition of the 3'-CCA and aminoacylation.

4 inct active site structures to catalyze tRNA aminoacylation.

5 zing the bound charging amino acid following aminoacylation.

6 ction, requires accurate transfer RNA (tRNA) aminoacylation.

7 had the same two complementary modes of tRNA aminoacylation.

8 , which is distinct from the active site for aminoacylation.

9 hmtRNA(Met), which significantly reduces its aminoacylation.

10 tion and is intrinsic to the active site for aminoacylation.

11 nd regulation molecules for functions beyond aminoacylation.

12 the same structural determinants as used for aminoacylation.

13 and is directly responsible for proper tRNA aminoacylation.

14 (m1)G37 in the anticodon loop for efficient aminoacylation.

15 rved overall accuracy of DNA replication and aminoacylation.

16 rid system and to measure in vitro tRNA(Pyl) aminoacylation.

17 by most leucyl-tRNA synthetases (LeuRS) for aminoacylation.

18 n can sequester free, uncharged tRNAs during aminoacylation.

19 mechanisms ensuring the selectivity of tRNA aminoacylation.

20 RNA during amino acid activation and/or tRNA aminoacylation.

21 r thermautotrophicus that enhances tRNA(Pro) aminoacylation.

22 eptide is not important for the kcat of tRNA aminoacylation.

23 xisting tRNA(Val(AAC)) accompanied by its de-aminoacylation.

24 id recognition but less efficient in cognate aminoacylation.

25 re delayed relative to the loss of G(-1) and aminoacylation.

26 A at their 3'-ends, representing the site of aminoacylation.

27 is highly sensitive to the kinetics of tRNA aminoacylation.

28 to facilitate high-affinity tRNA binding and aminoacylation.

29 tase (aaRS) utilizes BMAA as a substrate for aminoacylation.

30 to tyrosine, and significantly reduces tRNA aminoacylation.

31 near the active center of GltX and inhibits aminoacylation, a unique example of an aminoacyl-tRNA sy

32 LeuRS) is a class I enzyme, which houses its aminoacylation active site in a canonical core that is d

33 site is located approximately 30 A from the aminoacylation active site in the canonical core of the

34 The aminoacylation active site plays a significant role in p

35 o MST1 induces conformational changes in the aminoacylation active site, and it positions a potential

36 Because of its proximity to the aminoacylation active site, we propose that this domain

37 matic pre-transfer editing occurs within the aminoacylation active site.

38 lly present as an insertion (INS) within the aminoacylation active site.

39 tion of dimeric T1 into monomers deprived of aminoacylation activity and simultaneous induction of T2

40 ants S57C and N280S both displayed wild-type aminoacylation activity and stability with respect to th

41 ses TyrRS(Mini), which not only has the same aminoacylation activity as native TyrRS but also has str

42 207A) remained cytosolic and maintained full aminoacylation activity but failed to rescue infectivity

43 In vitro, the G34A mutation decreases aminoacylation activity by 100-fold, but does not affect

44 catalytic core and completely disrupted QARS aminoacylation activity in vitro.

45 owever, previous studies showed that loss of aminoacylation activity is not required to cause CMT.

46 tive stress, while the cognate Phe-tRNA(Phe) aminoacylation activity is unchanged.

47 Aminoacylation activity of HARS2 p.V368L and HARS2 p.L20

48 does not affect Phe or Tyr activation or the aminoacylation activity of PheRS.

49 ltered highly conserved amino acids, and the aminoacylation activity of QARS was significantly impair

50 inked RNA-protein complex blocks the overall aminoacylation activity of the enzyme.

51 ro, as well as the oligomerization state and aminoacylation activity of the synthetase.

52 gative effect of the p.His257Arg mutation on aminoacylation activity of TrpRS, which subsequently com

53 east mitochondrial LeuRS has compromised its aminoacylation activity to some extent and adapted its C

54 The mutant GlyRS enzyme retains aminoacylation activity, and a loss-of-function allele,

55 Apart from their parent aminoacylation activity, several aaRSs perform non-canon

56 y is rooted in an ancient adaptation for its aminoacylation activity, these results suggest that the

57 showed that shortening its tether stimulated aminoacylation activity.

58 henotype is shown here to not correlate with aminoacylation activity.

59 titution showed an over 10-fold reduction in aminoacylation activity.

60 cRNAs could implement all the steps for auto-aminoacylation: amino acid coordination, intermediate ac

61 yzing aminoacyl-adenylate formation and tRNA aminoacylation and a second editing or proofreading site

62 These results suggest a regulatory role for aminoacylation and abortion during stress, and our study

63 ondrial LeuRS C-terminal domain enhanced its aminoacylation and amino acid editing activities.

64 ic C-terminal domain in tRNA recognition for aminoacylation and amino acid editing has adapted differ

65 association in a MARS complex enhances tRNA-aminoacylation and contributes to parasite fitness.

66 h, rather than its sequence, was critical to aminoacylation and editing activities.

67 Aminoacylation and editing by leucyl-tRNA synthetases (L

68 minal domain as LeuRS transitions between an aminoacylation and editing complex or, in the case of ye

69 d forms unique sets of interactions with the aminoacylation and editing complexes.

70 he function of independent but collaborative aminoacylation and editing domains of alanyl-tRNA synthe

71 if that promotes cooperative binding of both aminoacylation and editing domains to tRNA(Ala).

72 xpense to the protein's housekeeping role in aminoacylation and editing.

73 LeuRS-F, contains canonical active sites for aminoacylation and editing.

74 TP is utilized in protein synthesis via tRNA aminoacylation and guanosine triphosphate regeneration.

75 mplex (MSC) that maintains and regulates the aminoacylation and nuclear functions of LysRS.

76 of the hexapeptide simultaneously attenuated aminoacylation and nuclear localization.

77 two sites: one for amino acid activation and aminoacylation and one for editing misactivated amino ac

78 ion so that, remarkably, two motifs (one for aminoacylation and one for editing) in the same enzyme i

79 ssignment of protein domains associated with aminoacylation and phosphate binding, the HisZ-HisG octa

80 This finding decouples aminoacylation and pre-transfer editing within the IleRS

81 platform for the synthesis by enzymatic tRNA aminoacylation and ribosomal translation of cyclic pepti

82 e A3243G mutation improved the efficiency of aminoacylation and stability of mitochondrial tRNAs and

83 e significant decreases in the efficiency of aminoacylation and steady-state level of mt-tRNA(Asp) in

84 lting from the historical study of tRNA(Cys) aminoacylation and the integrative perspective of sequen

85 tion domains had catalytic functions for the aminoacylation and the molecular switch-driven transport

86 ols and energy charge to control the rate of aminoacylation and thus protein synthesis.

87 Mispairs boost aminoacylation and translation primarily because they ac

88 ispairs are significantly more important for aminoacylation and translation than previously realized.

89 ssed in a series of reactions culminating in aminoacylation and translation.

90 in a series of required reactions leading to aminoacylation and translation.

91 canonical structures that are competent for aminoacylation and translation.

92 shes cross-subunit communication between the aminoacylation and tRNA-binding sites.

93 ay be important for substrate recognition in aminoacylation and/or amino acid editing.

94 for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite create

95 ia tyrosyl-tRNA synthetase (LdTyrRS) namely, aminoacylation, and as a mimic of host CXC chemokine.

96 two sites lead to rigorous accuracy in tRNA aminoacylation, and both activities are essential to Leu

97 taB2 showed comparable kinetics for in vitro aminoacylation, and both enzymes complemented a defect i

98 own is not attributable to altered tRNA(Gly) aminoacylation, and cannot be rescued by Drosophila Gars

99 ctive site titration, amino acid activation, aminoacylation, and posttransfer editing (deacylation).

100 e for amino acid supply, transfer RNA (tRNA) aminoacylation, and protein folding.

101 structure and creates a better substrate for aminoacylation, and thus the UPD and TLS are functionall

102 exonucleases, CCA end addition, tRNA nuclear aminoacylation, and tRNA subcellular traffic.

103 formation but reduces the level of tRNA(Met) aminoacylation approximately 2-fold.

104 Recognition strategies for tRNA aminoacylation are ancient and highly conserved, having

105 lthough the nucleotides in tRNA required for aminoacylation are conserved in evolution, bacterial ami

106 nd its kinetic parameters were determined by aminoacylation assay.

107 functionally active in ATP-PPi exchange and aminoacylation assays, and showed similar Km for L-proli

108 ircular dichroism and NMR spectroscopies and aminoacylation assays, we have investigated the function

109 elopment of tRNA nucleotide determinants for aminoacylation being interdependent with those for ribos

110 evolution of amino acid specificity and tRNA aminoacylation, both essential for expanding the genetic

111 the leucine-specific domain is critical for aminoacylation but not required for editing activity.

112 ed with ATP, yet decreases the efficiency of aminoacylation by 10(3)-fold while significantly elevati

113 peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results f

114 ific G.U base pair (G3.U70) marks a tRNA for aminoacylation by alanyl-tRNA synthetase.

115 Accurate transfer RNA (tRNA) aminoacylation by aminoacyl-tRNA synthetases controls tr

116 Critical recognition elements for aminoacylation by bacterial ProRS include acceptor stem

117 RS improves the catalytic efficiency of tRNA aminoacylation by both LysRS and ProRS.

118 The addition of G(-1) did not improve aminoacylation by C. crescentus HisRS.

119 acity of this protein to enhance the rate of aminoacylation by class I synthetases.

120 tRNA are important identity determinants for aminoacylation by cognate aminoacyl-tRNA synthetases.

121 These activities clear errors of aminoacylation by deacylation of mischarged tRNAs.

122 heir ability to correct occasional errors of aminoacylation by editing reactions.

123 an essential identity determinant for proper aminoacylation by isoleucyl tRNA synthetase (IleRS) and

124 No significant changes in aminoacylation by LeuRS or ProRS were observed upon the

125 The steady-state kinetics of aminoacylation by LysRS indicated that LeuRS specificall

126 structural requirements of the anticodon for aminoacylation by methionyl tRNA synthetase and IleRS.

127 pathways work in concert to ensure accurate aminoacylation by ProRS.

128 to translational fidelity by enhancing tRNA aminoacylation by ProRS.

129 d MCP2, that binds tRNAs and increases their aminoacylation by the complex.

130 on of tRNA(ala)(GAC) at a site that prevents aminoacylation by the dicot alanyl-tRNA synthetase, indi

131 Catalysis of tRNA(Tyr) aminoacylation by tyrosyl-tRNA synthetase can be divided

132 th EF-1alpha, suggesting that the product of aminoacylation can be directly handed off to EF-1alpha f

133 he 2'-hydroxyl of A66, are also critical for aminoacylation catalytic efficiency by human ProRS.

134 ayed a refolding defect resulting in reduced aminoacylation compared to wild type after renaturation.

135 s within the RDW peptide are critical to the aminoacylation complex, but impacted amino acid editing

136 nfluence productive tRNA interactions in the aminoacylation complex.

137 Here we identify a new pathway for lipid aminoacylation, conserved in many Actinobacteria, which

138 tRNA acceptor stem end between the canonical aminoacylation core and a separate domain called CP1 tha

139 ta-strands, which link the CP1 domain to the aminoacylation core of LeuRS, are required for editing o

140 ucts are translocated 30A from the canonical aminoacylation core to a hydrolytic editing-active site

141 n bacterial and mammalian systems, errors of aminoacylation could be mutagenic and lead to disease.

142 pic functions in protein synthesis including aminoacylation, decoding and translocation.

143 translational fidelity both by enhancing the aminoacylation efficiencies of the three aaRSs in the co

144 iant enzyme displayed significantly improved aminoacylation efficiency for the G34A mutant, suggestin

145 rminal fragment in trans did not improve the aminoacylation efficiency of the N-terminal fragment to

146 fluence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in eith

147 ssociation in the MARS complex enhances tRNA-aminoacylation efficiency, which is in part dependent on

148 Aminoacylation errors lead to genetic code ambiguity and

149 tions with the ribosome, with PoxA-catalyzed aminoacylation evolving later as a secondary mechanism t

150 Aminoacylation experiments in vitro showed that air oxid

151 -tRNA synthetase (hs mt LeuRS) achieves high aminoacylation fidelity without a functional editing act

152 editing mechanisms evolved to maintain tRNA aminoacylation fidelity.

153 The same selection also showed that RNA aminoacylation from adenylate is simpler than from CoA t

154 to improve the anticodon specificity of tRNA aminoacylation from bacteria to humans, possibly to acco

155 emoval of 3'-primer before reaction selected aminoacylation from PheAMP in three cycles, yielding act

156 hetases and is independent of its well-known aminoacylation function in protein synthesis.

157 ynthetase (TyrRS) is known for its essential aminoacylation function in protein synthesis.

158 th (CMT) neuropathy, suggesting that altered aminoacylation function underlies the disease.

159 many aaRS CMT mutants result in loss of tRNA aminoacylation function, animal genetics studies demonst

160 enotype is not caused by a loss of the GlyRS aminoacylation function.

161 ants were pleiotropic, exhibiting defects in aminoacylation, global structure, and elongation-factor

162 tRNA 3' end to the other protein subunit for aminoacylation in a conformation-dependent manner.

163 It is hypothesized that KARS variants affect aminoacylation in inner-ear cells by interfering with bi

164 anticodon confusion and subsequent erroneous aminoacylation in the ancestral coding system.

165 ailability of nutrients to cells and by tRNA aminoacylation in the nucleus.

166 and L570 in E. coli LeuRS) strongly impacts aminoacylation in two ways: it affects both amino acid d

167 The accuracy of tRNA aminoacylation in vivo is uncertain, however, and might

168 ilar stability and exhibit similar levels of aminoacylation in vivo.

169 two functions of the enzyme in splicing and aminoacylation in vivo.

170 affect reaction with tRNA, so that efficient aminoacylation is achieved.

171 functional changes that impact how accurate aminoacylation is achieved.

172 In addition, tRNA recognition and aminoacylation is affected.

173 deacylated tRNA, which accumulates when tRNA aminoacylation is limited by lack of substrates or inhib

174 eir specific role in the elementary steps of aminoacylation is poorly understood.

175 mechanism suggested by these data to promote aminoacylation is reminiscent of the NAD(+)-dependent me

176 etases (aaRSs), the rate-determining step in aminoacylation is the dissociation of charged tRNA from

177 The catalytic efficiency of steady-state aminoacylation (k(cat)/K(M)) with lysine by LysRS1 varia

178 stacking interactions with U34 and U35, and aminoacylation kinetics also identified direct interacti

179 Comparative aminoacylation kinetics by M. mazei CysRS and SepRS reve

180 Comparative pre-steady-state aminoacylation kinetics of native tRNA1(Gln), synthetic

181 te and noncognate reactions by ATP/PP(i) and aminoacylation kinetics strongly suggests that SepRS is

182 tain bacterial and eukaryotic tRNAs enhances aminoacylation kinetics, assists proper codon-anticodon

183 obal translation in this organism; that tRNA aminoacylation levels exert, at most, weak control over

184 gest codon dwell times could be explained by aminoacylation levels or high codon usage relative to tR

185 eins in response to fluctuating transfer RNA aminoacylation levels under various nutritional states.

186 nd LysRS2 do not drastically impact cellular aminoacylation levels, focusing attention on the mechani

187 glycine codons through the reduction of tRNA aminoacylation levels.

188 84 traps the enzyme-tRNA complex in a novel 'aminoacylation-like' conformation, forming novel interac

189 Steady-state kinetic parameters for aminoacylation measured under these conditions reveal th

190 talytic importance of the A76 2'-OH group in aminoacylation mirrors a similar role for this moiety th

191 splicing, as well as tRNA nuclear export and aminoacylation, occur efficiently when the SEN complex i

192 The absence of PAP I led to improved aminoacylation of 5'-immature tRNAs.

193 ant improvement compared to the wild type in aminoacylation of a tRNALysUUG mutant.

194 This bypass mechanism also rescues aminoacylation of an editing site mutation that hydrolyz

195 nsfer RNA synthetases through their accurate aminoacylation of cognate tRNAs and their ability to cor

196 x and by coupling two stages of translation: aminoacylation of cognate tRNAs and their subsequent cha

197 An effective method for aminoacylation of indoles and pyrroles has been achieved

198 resistance to antimicrobial peptides through aminoacylation of lipopolysaccharide (LPS), expected to

199 nyl-S-PCP intermediate; (ii) we confirm that aminoacylation of LnmP by LnmQ in trans is the result of

200 Aminoacylation of membrane lipids alters the biochemical

201 Moreover, a one-pot formal aminoacylation of olefins is described through a sequent

202 Aminoacylation of PG is used by bacteria to decrease the

203 Aminoacylation of RNA minihelices is speculated to be a

204 that very few nucleotides are needed for the aminoacylation of specific tRNAs.

205 expression of AtKRS in carrot cells promotes aminoacylation of such tRNAs in vivo and translational r

206 ino acid by the 5'-end of the pacRNA, and 3'-aminoacylation of the pacRNA.

207 Specific aminoacylation of the phospholipid phosphatidylglycerol

208 Aminoacylation of the polar head group of the phospholip

209 an be considered allosteric enzymes in which aminoacylation of the tRNA acceptor stem is enhanced upo

210 the unnatural base pair into mRNA and tRNA, aminoacylation of the tRNA with a non-canonical amino ac

211 y defect in this mutation was an inefficient aminoacylation of the tRNA(Leu(UUR)).

212 even though they had a drastic effect on the aminoacylation of the tRNAs.

213 This TLS not only acts like a tRNA to drive aminoacylation of the viral genomic (g)RNA, but also int

214 otein enzymes are solely responsible for the aminoacylation of transfer RNA.

215 ombined accuracy of two basic processes: the aminoacylation of transfer RNAs with their cognate amino

216 Aminoacylation of tRNA by aminoacyl-tRNA synthetases is

217 ep in protein biosynthesis is the 2(')(3(')) aminoacylation of tRNA by aminoacyl-tRNA synthetases.

218 t t(6)A is a strong positive determinant for aminoacylation of tRNA by bacterial-type but not by euka

219 Efficient aminoacylation of tRNA by Escherichia coli cysteinyl-tRN

220 Most aa-tRNAs are formed by direct aminoacylation of tRNA catalyzed by aminoacyl-tRNA synth

221 Aminoacylation of tRNA is the first step of protein synt

222 reas the anticodon sequence is essential for aminoacylation of tRNA(2Thr).

223 denylate, inhibits translation by preventing aminoacylation of tRNA(Asp) by aspartyl-tRNA synthetase

224 This G(-1) residue is required for aminoacylation of tRNA(His) by histidyl-tRNA synthetase,

225 ing that G(-1) is a critical determinant for aminoacylation of tRNA(His) in vivo.

226 ), which serves as a crucial determinant for aminoacylation of tRNA(His).

227 A(i)(Met) and other tRNA precursors, and the aminoacylation of tRNA(i)(Met) are also strongly impaire

228 yl-tRNA synthetase (hLysRS) is essential for aminoacylation of tRNA(Lys) Higher eukaryotic LysRSs pos

229 he RNA elements required for recognition and aminoacylation of tRNA(Pyl) in vivo by using the Pyl ana

230 cificity for tryptophan versus tyrosine, and aminoacylation of tRNA(Trp).

231 Single turnover kinetics for the aminoacylation of tRNA(Tyr) by D-tyrosine were monitored

232 y of tyrosyl-tRNA synthetase to catalyze the aminoacylation of tRNA(Tyr), we have expressed each of t

233 l domain of Escherichia coli LeuRS abolished aminoacylation of tRNALeu and also amino acid editing of

234 Accurate aminoacylation of tRNAs by the aminoacyl-tRNA synthetase

235 ility of essential amino acids (EAAs) limits aminoacylation of tRNAs by their cognate EAAs and activa

236 proofreading activity of this enzyme during aminoacylation of tRNAs.

237 on general features, such as the position of aminoacylation on the 3'-terminal tRNA ribose, and the t

238 variant had a minimal effect on activation, aminoacylation or misaminoacylation activities relative

239 We identified components of an indirect aminoacylation pathway for Gln-tRNA(Gln) biosynthesis in

240 trate a potential role for the indirect tRNA aminoacylation pathway in regulating translational fidel

241 picoplast proceeds via an essential indirect aminoacylation pathway that is reminiscent of bacteria a

242 te Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glu

243 The activation and aminoacylation properties of D. hafniense PylRS and the

244 The loss of aminoacylation quality control in the ileS(T233P) strain

245 As seen in other species defective for aminoacylation quality control, the growth rate of the i

246 However, the aminoacylation reaction can be diverted to produce diade

247 thanocaldococcus jannaschii tRNA(Cys) in the aminoacylation reaction for the two Methanococcus maripa

248 oduction by a tRNA synthetase is through the aminoacylation reaction intermediate aminoacyl-AMP, thus

249 c aminoacyl-adenylates as substrates in tRNA aminoacylation reaction may provide a way for incorporat

250 xpense of a significantly slower rate in the aminoacylation reaction, suggesting a previously unrecog

251 were otherwise completely inactive in direct aminoacylation reaction, thus bypassing the natural mech

252 cus is able to perform the first step of the aminoacylation reaction, which involves the activation o

253 reading activities at multiple stages of the aminoacylation reaction.

254 The genetic code is established in aminoacylation reactions catalyzed by aminoacyl-tRNA syn

255 The genetic code is fixed in aminoacylation reactions catalyzed by aminoacyl-tRNA syn

256 We first tested the canonical aminoacylation role of LdTyrRS.

257 tuberculosis that explains tRNA decoding and aminoacylation sensing by this riboregulator.

258 he adjacent linker form a tightly interwoven aminoacylation sensing module.

259 rable contacts from the linker region in the aminoacylation sensing module.

260 Overall, the T-box consists of decoding and aminoacylation sensing modules bridged by a rigid pseudo

261 ive activation of cognate amino acids at the aminoacylation site and hydrolysis of misformed aminoacy

262 usion, we propose that the plasticity of the aminoacylation site in MST1 allows binding of Ser-AMP an

263 ing a structural motif unrelated to that for aminoacylation so that, remarkably, two motifs (one for

264 tRNA bases have long been known to determine aminoacylation specificity.

265 aRS)-tRNA pairs that are orthogonal in their aminoacylation specificity.

266 conditions are met, tRNA is secured, and its aminoacylation state is sensed.

267 To improve the aminoacylation state of the mutant tRNA, we modified the

268 scriminator' structure, and interrogates its aminoacylation state using a steric filter fashioned fro

269 T-boxes directly bind tRNAs, assess their aminoacylation state, and regulate the transcription or

270 directly to a specific tRNA and sensing its aminoacylation state.

271 with the tRNA acceptor end and evaluates its aminoacylation state.

272 Related elements respond to the aminoacylation status of a specific tRNA or to a physica

273 rvation by binding, decoding and reading the aminoacylation status of specific transfer RNAs.

274 ession of downstream genes by monitoring the aminoacylation status of the cognate tRNA.

275 new transcription, and is independent of the aminoacylation status of tRNA.

276 NA Extension (tREX)-to determine the in vivo aminoacylation status of tRNAs.

277 don of tRNA, while a 3' domain evaluates its aminoacylation status, overcoming an otherwise stable tr

278 ted the impact of hmt-tRNA(Phe) mutations on aminoacylation, structure, and translation elongation-fa

279 Thus, borrelidin competes with all three aminoacylation substrates, providing a potent and redund

280 helices seriously reduces the efficiency of aminoacylation, suggesting that communication requires c

281 ancestral proto-anti-codon RNA (pacRNA) auto-aminoacylation system and show that pacRNAs would natura

282 ere, we used an in vitro reconstituted lipid aminoacylation system to investigate the two phylogeneti

283 with a nonprotein, nonribozyme, RNA-directed aminoacylation system.

284 We hypothesize ribozyme-based aminoacylation systems using aminoacyl thioesters of CoA

285 etic code before the evolution of the modern aminoacylation systems.

286 In the absence of aminoacylation, T-boxes clutch tRNAs and form a continuo

287 mation transitions in various stages of tRNA aminoacylation that are associated with catalysis.

288 ed': one face closely mimics tRNA and drives aminoacylation, the other face diverges from tRNA and en

289 role in the evolution of AlaRSs by coupling aminoacylation to editing to prevent mistranslation.

290 contribution affects steps ranging from tRNA aminoacylation to peptide bond formation.

291 anslocation process that moves tRNA from the aminoacylation to the editing complex.

292 We showed that the alteration of aminoacylation tRNA(Leu(UUR)) caused by the A3243G mutat

293 taneous induction of T2, which is active for aminoacylation under low zinc.

294 her, competition among tRNA isoacceptors for aminoacylation underlies the robustness of protein synth

295 RNA synthetase, the role of tRNA identity in aminoacylation was investigated.

296 hanges in the steady-state kinetics of LeuRS aminoacylation were observed upon the addition of ProRS.

297 codon usage and several tRNAs showed reduced aminoacylation, which was conserved in fasted mice.

298 A synthetic active site catalyzes tRNA aminoacylation, while an editing active site hydrolyzes

299 Previous work showed chiral preference of aminoacylation with a nonprotein, nonribozyme, RNA-direc

300 the specificity helix, accelerates tRNA(Trp) aminoacylation with approximately 10-fold specificity to