ライフサイエンスコーパス: aminoacyl-tRNA synthetase

1 otein using an engineered pair of yeast tRNA/aminoacyl tRNA synthetase.

2 inoacyl adenylate that inhibits an essential aminoacyl-tRNA synthetase.

3 lysine with the participation of a dedicated aminoacyl-tRNA synthetase.

4 e to tRNA(CUA) by PylS, an archaeal class II aminoacyl-tRNA synthetase.

5 thioesters of CoA as the ancestors of modern aminoacyl tRNA synthetases.

6 ished by aminoacylations of transfer RNAs by aminoacyl tRNA synthetases.

7 catalytic activity in the earliest Class II aminoacyl-tRNA synthetases.

8 H and KMSKS motifs characteristic of class I aminoacyl-tRNA synthetases.

9 is the 2(')(3(')) aminoacylation of tRNA by aminoacyl-tRNA synthetases.

10 ing a functionally relevant core in Class Ia aminoacyl-tRNA synthetases.

11 hat may prove to be common to other class II aminoacyl-tRNA synthetases.

12 -Tu*GTP can readily dissociate and rebind to aminoacyl-tRNA synthetases.

13 proposed on the basis of studies of related aminoacyl-tRNA synthetases.

14 ere shown to be substrates for their cognate aminoacyl-tRNA synthetases.

15 y direct aminoacylation of tRNA catalyzed by aminoacyl-tRNA synthetases.

16 ritable defects in the editing activities of aminoacyl-tRNA synthetases.

17 ein synthesis and its fidelity rely upon the aminoacyl-tRNA synthetases.

18 g of amino acids with tRNAs catalyzed by the aminoacyl-tRNA synthetases.

19 y role for Hints on LysRS and possibly other aminoacyl-tRNA synthetases.

20 hed in aminoacylation reactions catalyzed by aminoacyl-tRNA synthetases.

21 xed in aminoacylation reactions catalyzed by aminoacyl-tRNA synthetases.

22 tive pressures for maintenance of editing by aminoacyl-tRNA synthetases.

23 anslation is editing of misacylated tRNAs by aminoacyl-tRNA synthetases.

24 t comparison with other class I and class II aminoacyl-tRNA synthetases.

25 tion of selected amino acid transporters and aminoacyl-tRNA synthetases.

26 nts of the tRNA interaction network, such as aminoacyl-tRNA synthetases.

27 y determinants for aminoacylation by cognate aminoacyl-tRNA synthetases.

28 pparatus, including some bacterial and human aminoacyl-tRNA synthetases (AA-RS).

29 While a number of aminoacyl tRNA synthetase (aaRS):tRNA pairs have been en

30 proximity assay (SPA) technology to measure aminoacyl-tRNA synthetase (aaRS) activity and the use of

31 Ancient forms of aminoacyl-tRNA synthetase (aaRS) catalytic domains and a

32 While aminoacyl-tRNA synthetase (AARS) editing potentially pro

33 the specificity resides at the level of the aminoacyl-tRNA synthetase (AARS) enzymes that are respon

34 A mutant Escherichia coli aminoacyl-tRNA synthetase (aaRS) is first evolved in yea

35 ubstrate recognition properties of a natural aminoacyl-tRNA synthetase (aaRS) must be modified in ord

36 coli amber suppressor tRNA(CUA) and cognate aminoacyl-tRNA synthetase (aaRS) pair, and expression of

37 cy using an orthogonal amber suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.

38 te, representing a rare example of a class I aminoacyl-tRNA synthetase (aaRS) that does not proofread

39 ctures allowed the placement of PylRS in the aminoacyl-tRNA synthetase (aaRS) tree as the last known

40 The anti-codon-binding domain of an archeal aminoacyl-tRNA synthetase (aaRS) was discovered to posse

41 ondria of Saccharomyces cerevisiae, a single aminoacyl-tRNA synthetase (aaRS), MST1, aminoacylates tw

42 Aminoacyl-tRNA synthetases (AARS) are an essential famil

43 Aminoacyl-tRNA synthetases (aaRS) catalyze both chemical

44 Aminoacyl-tRNA synthetases (aaRS) join amino acids to th

45 The genetic code is implemented by aminoacyl-tRNA synthetases (aaRS).

46 The 20 aminoacyl tRNA synthetases (aaRSs) couple each amino aci

47 this question for an enzyme family, we chose aminoacyl tRNA synthetases (AARSs).

48 hrough metadynamics simulations on a class I aminoacyl-tRNA synthetase (aaRSs), the largest group in

49 These modes involve distinct classes of aminoacyl-tRNA synthetases (aaRSs I and II) with recogni

50 us enzyme) derived from Class I and Class II aminoacyl-tRNA synthetases (aaRSs) acylate tRNA far fast

51 ynthesis of cognate amino acid:tRNA pairs by aminoacyl-tRNA synthetases (aaRSs) and accurate selectio

52 nate amino acid:transfer RNA (tRNA) pairs by aminoacyl-tRNA synthetases (aaRSs) and inaccurate select

53 ecific attachment of amino acids to tRNAs by aminoacyl-tRNA synthetases (aaRSs) and the subsequent de

54 Aminoacyl-tRNA synthetases (AARSs) are a superfamily of

55 Aminoacyl-tRNA synthetases (aaRSs) are housekeeping enzy

56 In mammalian cells, aminoacyl-tRNA synthetases (aaRSs) are organized into a

57 Aminoacyl-tRNA synthetases (AARSs) are required for tran

58 Aminoacyl-tRNA synthetases (aaRSs) are responsible for a

59 The aminoacyl-tRNA synthetases (AARSs) attach amino acids to

60 Aminoacyl-tRNA synthetases (AARSs) catalyze an early ste

61 Aminoacyl-tRNA synthetases (aaRSs) charge tRNAs with the

62 Many aminoacyl-tRNA synthetases (aaRSs) contain two active si

63 To prevent mistranslation, aminoacyl-tRNA synthetases (AARSs) discriminate against

64 Some aminoacyl-tRNA synthetases (AARSs) employ an editing mec

65 To ensure translational fidelity, aminoacyl-tRNA synthetases (aaRSs) employ pre-transfer a

66 Aminoacyl-tRNA synthetases (aaRSs) ensure faithful trans

67 Aminoacyl-tRNA synthetases (aaRSs) join amino acids to 1

68 Aminoacyl-tRNA synthetases (aaRSs) play a key role in de

69 Accurate aminoacylation of tRNAs by the aminoacyl-tRNA synthetases (aaRSs) plays a critical role

70 Aminoacyl-tRNA synthetases (aaRSs) that use tRNA anticod

71 Aminoacyl-tRNA synthetases (aaRSs) translate the genetic

72 ytoplasmic and potentially all mitochondrial aminoacyl-tRNA synthetases (aaRSs) were identified, and

73 curring can result from mechanisms involving aminoacyl-tRNA synthetases (aaRSs) with inactivated hydr

74 We evolved chromosomal aminoacyl-tRNA synthetases (aaRSs) with up to 25-fold in

75 mitochondrial translation machinery, such as aminoacyl-tRNA synthetases (aaRSs), can also lead to dis

76 For several class I aminoacyl-tRNA synthetases (aaRSs), the rate-determining

77 Key players in this process are aminoacyl-tRNA synthetases (aaRSs), which not only catal

78 amino group) of amino acids into tRNA using aminoacyl-tRNA synthetases (aaRSs).

79 o show experimentally that a minimal class I aminoacyl-tRNA synthetase active site might have functio

80 complex composed of eight proteins that have aminoacyl-tRNA synthetase activities as well as three no

81 ning procedure for the identification of new aminoacyl-tRNA synthetase activity based on the cell sur

82 ular proteins often requires engineering new aminoacyl-tRNA synthetase activity into the cell.

83 an be facilitated by the introduction of new aminoacyl-tRNA synthetase activity into the expression h

84 The resulting aminoacyl-tRNA synthetases aminoacylate an amber suppres

85 nvolved evolution of the first non-canonical aminoacyl-tRNA synthetase and cognate tRNA to be describ

86 Several aminoacyl-tRNA synthetases and Mcm2-7 proteins were iden

87 However, when CP1 domains from different aminoacyl-tRNA synthetases and origins were fused to thi

88 ion using a pure translation system in which aminoacyl-tRNA synthetases and other competitors are del

89 -box riboswitches regulate the expression of aminoacyl-tRNA synthetases and other proteins in respons

90 WHEP domains exist in certain eukaryotic aminoacyl-tRNA synthetases and play roles in tRNA or pro

91 icient and specific substrates of eukaryotic aminoacyl-tRNA synthetases and ribosomes.

92 e manifests itself in the interaction of the aminoacyl-tRNA synthetases and their cognate tRNAs.

93 lasmids enables the bulk purification of the aminoacyl-tRNA synthetases and translation factors neces

94 and specialization (neofunctionalization) of aminoacyl-tRNA synthetases and tRNAs from common ancestr

95 duced the current set of mutually orthogonal aminoacyl-tRNA synthetases and tRNAs that direct natural

96 level of structural similarity to class IIa aminoacyl tRNA synthetases, and forms a dimer in the cry

97 RNA's including an initiator methionyl-tRNA, aminoacyl tRNA synthetases, and other protein factors.

98 er RNAs with their cognate amino acid by the aminoacyl-tRNA synthetases, and the selection of cognate

99 Aminoacyl-tRNA synthetases are a family of enzymes that

100 Aminoacyl-tRNA synthetases are an ancient class of enzym

101 In animal cells, nine aminoacyl-tRNA synthetases are associated with the three

102 In mammals, many aminoacyl-tRNA synthetases are bound together in a multi

103 Aminoacyl-tRNA synthetases are divided into two classes

104 The aminoacyl-tRNA synthetases are divided into two unrelate

105 Aminoacyl-tRNA synthetases are key enzymes in the transl

106 Mutations in genes encoding aminoacyl-tRNA synthetases are known to cause leukodystr

107 Aminoacyl-tRNA synthetases are modular enzymes composed

108 Aminoacyl-tRNA synthetases are multidomain enzymes that

109 Aminoacyl-tRNA synthetases are multidomain proteins resp

110 Aminoacyl-tRNA synthetases are multidomain proteins that

111 Aminoacyl-tRNA synthetases are normally found in one of

112 Aminoacyl-tRNA synthetases are responsible for attaching

113 Aminoacyl tRNA synthetases (ARS) catalyze the ligation o

114 JTV1/AIMP2, a structural subunit of a multi-aminoacyl-tRNA synthetase (ARS) complex, has also been r

115 Here we explore the potential of the aminoacyl-tRNA synthetase (ARS) family as a source of an

116 to amino acid (AA) limitation of the entire aminoacyl-tRNA synthetase (ARS) gene family revealed tha

117 Mutations in several aminoacyl-tRNA synthetase (ARS) genes have been implicat

118 Aminoacyl-tRNA synthetases (ARSs) are responsible for ch

119 Aminoacyl-tRNA synthetases (ARSs) catalyze the attachmen

120 Mutations in three genes encoding aminoacyl-tRNA synthetases (ARSs) have been implicated i

121 Aminoacyl-tRNA synthetases (ARSs) join amino acids to th

122 DNA polymerases and aminoacyl-tRNA synthetases (ARSs) represent large enzyme

123 d that mutations in a tRNA gene, aspT, in an aminoacyl tRNA synthetase, AspRS, and in a translation f

124 Aminoacyl-tRNA synthetases attach specific amino acids t

125 ibits aminoacylation, a unique example of an aminoacyl-tRNA synthetase being inhibited by a toxin enc

126 problem is compounded as the 20 contemporary aminoacyl-tRNA synthetases belong to two quite distinct

127 Aminoacyl-tRNA synthetase binding is RNase A sensitive,

128 Once released by aminoacyl-tRNA synthetases, both cognate and near-cognat

129 consensus motifs characteristic of a class I aminoacyl-tRNA synthetase but lacks the Zn(2+) binding m

130 ns such as the ribosome, or proteins such as aminoacyl-tRNA synthetases, but is unprecedented for a c

131 een conserved motifs 2 and 3 of the Class II aminoacyl-tRNA synthetase catalytic core.

132 Aminoacyl-tRNA synthetases catalyze ATP-dependent covale

133 Aminoacyl-tRNA synthetases catalyze the attachment of am

134 Aminoacyl-tRNA synthetases catalyze the attachment of am

135 Aminoacyl-tRNA synthetases catalyze the attachment of co

136 Aminoacyl-tRNA synthetases catalyze the covalent attachm

137 ion and tRNA esterification are corrected by aminoacyl-tRNA synthetase-catalyzed editing reactions, a

138 nds on a cytosolic complex (AME) made of two aminoacyl-tRNA synthetases (cERS and cMRS) attached to a

139 YajL substrates included ribosomal proteins, aminoacyl-tRNA synthetases, chaperones, catalases, perox

140 rther, we tested the hypothesis that the two aminoacyl tRNA synthetase classes have originated from a

141 Urzymes from both aminoacyl-tRNA synthetase classes possess sophisticated

142 Within the two unrelated aminoacyl-tRNA synthetase classes, lysyl-tRNA synthetase

143 Aminoacyl-tRNA synthetases classically regulate protein

144 tal sRNA pool after met-tRNAi was charged by aminoacyl tRNA synthetase, co-eluted with sRNA by size e

145 Here we show that only the aminoacyl-tRNA synthetase cofactor p38 is upregulated in

146 ide II (EMAP II), one component of the multi-aminoacyl tRNA synthetase complex, plays multiple roles

147 he accumulation of parkin substrates, AIMP2 (aminoacyl tRNA synthetase complex-interacting multifunct

148 -tRNA synthetase, a polypeptide of the multi-aminoacyl tRNA synthetase complex.

149 3 to form a stable and conserved large multi-aminoacyl-tRNA synthetase complex (MARS), whose molecula

150 sequestered in a high-molecular-weight multi-aminoacyl-tRNA synthetase complex (MSC), restricting the

151 LysRS is normally sequestered in a multi-aminoacyl-tRNA synthetase complex (MSC).

152 gradation of two substrates, synphilin-1 and aminoacyl-tRNA synthetase complex cofactor, p38.

153 sgenic overexpression of a parkin substrate, aminoacyl-tRNA synthetase complex interacting multifunct

154 The long form is a component of the multiple aminoacyl-tRNA synthetase complex, and the other is an N

155 ar proteins, in the case of a heterotrimeric aminoacyl-tRNA synthetase complex, the aggregated protei

156 Aminoacyl-tRNA synthetase-containing complexes have been

157 curate transfer RNA (tRNA) aminoacylation by aminoacyl-tRNA synthetases controls translational fideli

158 In all organisms, aminoacyl tRNA synthetases covalently attach amino acids

159 The aminoacyl-tRNA synthetases covalently link transfer RNAs

160 The aminoacyl-tRNA synthetases covalently link transfer RNAs

161 In higher organisms, aminoacyl-tRNA synthetases developed receptor-mediated e

162 y is unusually severe in comparison to other aminoacyl-tRNA synthetase disorders.

163 Strains releasing asynchronously the two aminoacyl-tRNA synthetases display aberrant expression o

164 ming the amino-acid substrate specificity of aminoacyl-tRNA synthetase enzymes that are orthogonal in

165 Aminoacyl tRNA synthetases--enzymes that catalyze the fi

166 forms of a number of proteins, including the aminoacyl-tRNA synthetase EPRS.

167 Aminoacyl-tRNA synthetases, essential components of the

168 Aminoacyl-tRNA synthetases establish the genetic code by

169 of tRNAs with their cognate amino acids, by aminoacyl-tRNA synthetases, establishes the genetic code

170 a GlnRS and provides a paradigm for studying aminoacyl-tRNA synthetase evolution using directed engin

171 zymes, this would favor a scenario where the aminoacyl-tRNA synthetases evolved in the context of pre

172 Purified aminoacyl-tRNA synthetases exhibit a fidelity of one err

173 We show that PylS is a specialized aminoacyl-tRNA synthetase for charging pyrrolysine to tR

174 The specificity of most aminoacyl-tRNA synthetases for an amino acid and cognate

175 these libraries can be expanded using mutant aminoacyl-tRNA synthetases for the incorporation of addi

176 terest for amino acid activation by class Ic aminoacyl-tRNA synthetases, for which there is substanti

177 Aminoacyl-tRNA synthetases form complexes with tRNA to c

178 Thus, this aminoacyl-tRNA synthetase fragment contributes to standa

179 Here we investigate thirty-one aminoacyl-tRNA synthetases from infectious disease organ

180 class of natural product inhibitors affects aminoacyl-tRNA synthetase function, providing potentiall

181 ncluding an inducible copy of the respective aminoacyl-tRNA synthetase gene on each incorporation pla

182 nscripts of many amino acid biosynthetic and aminoacyl tRNA synthetase genes contain 5' untranslated

183 s study provides insights into how auxiliary aminoacyl-tRNA synthetase genes are regulated in bacteri

184 ded expression of amino acid transporter and aminoacyl-tRNA synthetase genes downstream of the stress

185 pression of many amino acid biosynthetic and aminoacyl-tRNA synthetase genes.

186 synthesis demonstrates that the misacylating aminoacyl-tRNA synthetase (GluRS(ND)) and the tRNA-depen

187 Many aminoacyl-tRNA synthetases have an editing activity that

188 Mutations in genes encoding aminoacyl-tRNA synthetases have been implicated in perip

189 cause of this important biological function, aminoacyl-tRNA synthetases have been the focus of anti-i

190 Engineered aminoacyl-tRNA synthetases have been used to enable the

191 Some aminoacyl-tRNA synthetases have editing activities to cl

192 teins, DUE-B was previously classified as an aminoacyl-tRNA synthetase; however, the human protein is

193 Aminoacyl-tRNA synthetases hydrolyze aminoacyl adenylate

194 Like some other aminoacyl-tRNA synthetases, IleRS can mischarge tRNA(Ile

195 While having multiple aminoacyl-tRNA synthetases implicated in Charcot-Marie-T

196 l, including characterization of the evolved aminoacyl-tRNA synthetase in S. cerevisiae, can be compl

197 ysyl-tRNA synthetase (PylRS), a polyspecific aminoacyl-tRNA synthetase in wide use, has facilitated i

198 e existence of a functional complex of three aminoacyl-tRNA synthetases in archaea in which LeuRS imp

199 To investigate interactions involving aminoacyl-tRNA synthetases in Archaea, we undertook a ye

200 cyl-tRNA synthetase (IleRS) is unusual among aminoacyl-tRNA synthetases in having a tRNA-dependent pr

201 m for understanding the role of mutations in aminoacyl-tRNA synthetases in neurological diseases.

202 is predominately dictated by the accuracy of aminoacyl-tRNA synthetases in pairing amino acids with c

203 The role of aminoacyl-tRNA synthetases in translation is to define t

204 nt with pyrophosphate being an inhibitor for aminoacyl-tRNA synthetase, incubations in the presence o

205 s the editing site as a bona fide target for aminoacyl-tRNA synthetase inhibitors.

206 nt of Parkinson disease pathology along with aminoacyl-tRNA synthetase interacting multifunctional pr

207 ding protein 1 is known to be degraded in an aminoacyl-tRNA synthetase interacting multifunctional pr

208 ation, accumulation of the parkin substrates aminoacyl-tRNA synthetase-interacting multifunctional pr

209 Aminoacyl-tRNA synthetase-interacting multifunctional pr

210 enzyme specificity, a library of orthogonal aminoacyl-tRNA synthetase is generated and genetic selec

211 ling of cognate amino acids and tRNAs by the aminoacyl-tRNA synthetases is achieved through a combina

212 The selection of tRNAs by their cognate aminoacyl-tRNA synthetases is critical for ensuring the

213 Although high fidelity of aminoacyl-tRNA synthetases is often thought to be essent

214 uctural plasticity that is observed in these aminoacyl-tRNA synthetases is rarely found in other muta

215 Aminoacylation of tRNA by aminoacyl-tRNA synthetases is the essential reaction tha

216 e, which exhibits some similarity to class 2 aminoacyl tRNA synthetases, is functional.

217 Aminoacyl-tRNA synthetases maintain the fidelity during

218 along with the identification of its cognate aminoacyl-tRNA synthetase makes it possible to map trans

219 The multiple aminoacyl-tRNA synthetase (MARS) complex contained at le

220 ent sporulation and suggests that editing by aminoacyl-tRNA synthetases may be important for survival

221 Using the in vivo suppressor tRNA/aminoacyl-tRNA synthetase method, Y730NH2Y-alpha2 and Y7

222 oth of which are aminoacylated by Class I mt-aminoacyl-tRNA synthetases (mt-aaRSs).

223 These include the engineered tRNA/aminoacyl-tRNA synthetase pair and the nonsense mutant o

224 with an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase pair in Escherichia coli.

225 roduced a Methanocaldococcus jannaschii tRNA:aminoacyl-tRNA synthetase pair into the chromosome of a

226 omplished by coexpressing an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatura

227 Expression in yeast harboring a cognate tRNA/aminoacyl-tRNA synthetase pair specifically evolved to i

228 o add a new building block are a unique tRNA/aminoacyl-tRNA synthetase pair, a source of the amino ac

229 Using E. coli cells with a special tRNA/aminoacyl-tRNA synthetase pair, two PPARalpha variants w

230 nd efficiency by means of an orthogonal tRNA/aminoacyl-tRNA synthetase pair.

231 ense codon and corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair.

232 ense codon and corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair.

233 Recently, tRNA aminoacyl-tRNA synthetase pairs have been evolved that a

234 Two polyspecific tRNA/aminoacyl-tRNA synthetase pairs were inserted into this

235 Various domains of an aminoacyl-tRNA synthetase perform their specific functio

236 Aminoacyl-tRNA synthetases perform a critical step in tr

237 Many aminoacyl-tRNA synthetases prevent mistranslation by rel

238 te kinase (adk [mhp208]) (P = 0.001), prolyl aminoacyl tRNA synthetase (proS [mhp397]) (P = 0.009), a

239 In the first step of protein synthesis, aminoacyl-tRNA synthetases react with amino acid and ATP

240 d tRNA thermostability, and may have altered aminoacyl-tRNA synthetase recognition sites.

241 Aminoacyl-tRNA synthetases recognize tRNA anticodon and

242 expands the genetic and clinical spectrum of aminoacyl-tRNA synthetase-related human disease.

243 aspects of tRNA recognition from the parent aminoacyl-tRNA synthetase, relaxed tRNA specificity lead

244 Many aminoacyl-tRNA synthetases require an additional domain

245 n of rrt-1, and of most other genes encoding aminoacyl-tRNA synthetases, rescued animals from hypoxia

246 GARS is a member of the family of aminoacyl-tRNA synthetases responsible for charging tRNA

247 tion are also substrates, including multiple aminoacyl tRNA synthetases, ribosomal proteins, protein

248 Using the suppressor tRNA/aminoacyl-tRNA synthetase (RS) methodology, 3-aminotyros

249 sed as a sense codon, and an orthogonal tRNA/aminoacyl-tRNA synthetase (RS) pair is used to generate

250 using evolved Methanocaldococcus jannaschii aminoacyl-tRNA synthetase(s) (aaRS)/suppressor tRNA pair

251 translation system components, in particular aminoacyl-tRNA synthetases, shows that, at a stage of ev

252 nts required for this process, an orthogonal aminoacyl-tRNA synthetase specific for sulfotyrosine and

253 usually corrected by the editing activity of aminoacyl-tRNA synthetases such as phenylalanyl-tRNA syn

254 Aminoacyl-tRNA synthetase/suppressor tRNA (aaRS/tRNA(CUA

255 he amino acid and the generation of a mutant aminoacyl tRNA synthetase that can selectively charge th

256 mics, including the discovery of the elusive aminoacyl-tRNA synthetase that is involved in both the b

257 trate-bound Methanococcus jannaschii tyrosyl aminoacyl-tRNA synthetases that charge the unnatural ami

258 ploying mutants in tRNA(His) and its cognate aminoacyl-tRNA synthetase, the role of tRNA identity in

259 s substrates and catalytically interact with aminoacyl-tRNA synthetases, the significant differences

260 ugh LGTs were common in the evolution of the aminoacyl-tRNA synthetases, they were not sufficient to

261 rchers in the scientific community requested aminoacyl-tRNA synthetases to be targeted in the Seattle

262 ced fit of tRNA and protein employed by some aminoacyl-tRNA synthetases to increase specificity.

263 les that transfer activated amino acids from aminoacyl-tRNA synthetases to the ribosome, where they a

264 in living cells relies on an engineered tRNA/aminoacyl-tRNA synthetase (tRNA/aaRS) pair, orthogonal t

265 By creating mutually orthogonal aminoacyl-tRNA synthetase-tRNA pairs and combining them

266 require blank codons and mutually orthogonal aminoacyl-tRNA synthetase-tRNA pairs that recognize unna

267 be a rapid approach for directly discovering aminoacyl-tRNA synthetase-tRNA pairs that selectively in

268 nd enables the direct, scalable discovery of aminoacyl-tRNA synthetase-tRNA pairs with mutually ortho

269 Here, we report the selection of an aminoacyl-tRNA synthetase/tRNA pair for the cotranslatio

270 412d directly in E. coli with an orthogonal aminoacyl-tRNA synthetase/tRNA pair specific for sulfoty

271 ves modifying cells to express an orthogonal aminoacyl-tRNA synthetase/tRNA pair to enable the incorp

272 all number of naturally occurring orthogonal aminoacyl-tRNA synthetase/tRNA pairs do not place an int

273 We have discovered aminoacyl-tRNA synthetase/tRNA pairs for the efficient s

274 The development of new orthogonal aminoacyl-tRNA synthetase/tRNA pairs has led to the addi

275 Orthogonal aminoacyl-tRNA synthetase/tRNA pairs have been used toge

276 ning ribo-X, orthogonal mRNAs and orthogonal aminoacyl-tRNA synthetase/tRNA pairs in Escherichia coli

277 ) by introducing orthogonal amber suppressor aminoacyl-tRNA synthetase/tRNA pairs into a thiocillin p

278 The code is enforced by aminoacyl-tRNA synthetase/tRNA pairs, which direct the u

279 d into proteins using established orthogonal aminoacyl-tRNA synthetase/tRNA systems.

280 alian cells was achieved using an orthogonal aminoacyl-tRNA synthetase/tRNA(CUA) pair (CpKRS/MbtRNA(C

281 genetically encoded Tet-v2.0 with an evolved aminoacyl-tRNA synthetase/tRNA(CUA) pair.

282 Orthogonal aminoacyl-tRNA synthetase/tRNA(CUA) pairs, together with

283 one using a plasmid containing an orthogonal aminoacyl-tRNA synthetase/tRNA(CUA) that incorporates L-

284 on 166 using an evolved orthogonal nitro-Tyr-aminoacyl-tRNA synthetase/tRNACUA pair for functional st

285 We have evolved orthogonal aminoacyl-tRNA synthetase/tRNACUA pairs that genetically

286 At present, engineered unnatural aminoacyl-tRNA synthetases (UaaRS) are evaluated on thei

287 Aminoacyl-tRNA synthetases use a variety of mechanisms t

288 ntibiotic activity by specifically targeting aminoacyl-tRNA synthetases, validating these enzymes as

289 , the evolution of the genes encoding the 20 aminoacyl-tRNA synthetases was examined.

290 F-P by PoxA evolved from tRNA recognition by aminoacyl-tRNA synthetases, we compared the roles of EF-

291 from nucleic acid to protein is mediated by aminoacyl-tRNA synthetases, which catalyze the specific

292 from a common ancestor related to glutaminyl aminoacyl-tRNA synthetases, which may have been one of t

293 rallel with those between the two classes of aminoacyl-tRNA synthetases, which use distinct active si

294 o acids and deacylated tRNAs is catalyzed by aminoacyl-tRNA synthetases, which use quality control pa

295 nt to the CCA of mature tRNA is performed by aminoacyl-tRNA synthetases, which, like the preceding pr

296 uence of the fact that ND-GluRS is a class I aminoacyl-tRNA synthetase, while ND-AspRS belongs to the

297 Isoleucyl-tRNA synthetase (IleRS) is an aminoacyl-tRNA synthetase whose essential function is to

298 Isoacceptor-specific aminoacyl-tRNA synthetases will enable the reassignment

299 In this study, we identified two class-I aminoacyl-tRNA synthetases with high similarities to con

300 GlyRS) provides a unique case among class II aminoacyl tRNA synthetases, with two clearly widespread