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 the only known valine cytoplasmic-localized aminoacyl-tRNA synthetase.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

35 l assays, we sought to determine whether any aminoacyl-tRNA synthetase (aaRS) utilizes BMAA as a subs

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

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

38 s into proteins is the scalable discovery of aminoacyl-tRNA synthetase (aaRS)-tRNA pairs that are ort

39 ed-fit adaption to the cognate mitochondrial aminoacyl-tRNA synthetase (aaRS).

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

41 Aminoacyl-tRNA synthetases (aaRS) catalyze both chemical

42 of the genetic code is maintained in part by aminoacyl-tRNA synthetases (aaRS) proofreading mechanism

43 In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthet

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

45 Among these, we identified the aminoacyl tRNA synthetases (aaRSs) as essential mediator

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 ancient enzymes t

56 Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes

57 Aminoacyl-tRNA synthetases (aaRSs) are housekeeping enzy

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

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

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

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

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

63 in pairing tRNAs with correct amino acids by aminoacyl-tRNA synthetases (aaRSs) dictates the fidelity

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

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

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

67 Aminoacyl-tRNA synthetases (aaRSs) ensure faithful trans

68 Aminoacyl-tRNA synthetases (aaRSs) have long been viewed

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

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

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

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

73 Aminoacyl-tRNA synthetases (aaRSs) translate the genetic

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

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

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

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

78 major factors involved in this exclusion are aminoacyl-tRNA synthetases (aaRSs), elongation factor th

79 Aminoacyl-tRNA synthetases (aaRSs), the enzymes responsi

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

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

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

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

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

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

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

87 The resulting aminoacyl-tRNA synthetases aminoacylate an amber suppres

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

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

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

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

92 lecting the substrate specificity of natural aminoacyl-tRNA synthetases and ribosomes.

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

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

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

96 the translation apparatus, including tRNAs, aminoacyl-tRNA synthetases and translation factors.

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

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

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

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

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

102 Aminoacyl-tRNA synthetases are a family of enzymes that

103 Aminoacyl-tRNA synthetases are an ancient class of enzym

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

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

106 Aminoacyl-tRNA synthetases are divided into two classes

107 The aminoacyl-tRNA synthetases are divided into two unrelate

108 Aminoacyl-tRNA synthetases are key enzymes in the transl

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

110 Aminoacyl-tRNA synthetases are multidomain proteins resp

111 Aminoacyl-tRNA synthetases are multidomain proteins that

112 Aminoacyl-tRNA synthetases are normally found in one of

113 Aminoacyl-tRNA synthetases are predominantly cytoplasmic

114 Aminoacyl-tRNA synthetases are ubiquitous and essential

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

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

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

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

119 Aminoacyl-tRNA synthetases (ARS) are ubiquitously expres

120 Aminoacyl tRNA synthetases (ARSs) link specific amino ac

121 Aminoacyl-tRNA synthetases (ARSs) are critical for prote

122 Aminoacyl-tRNA synthetases (ARSs) are essential enzymes

123 Aminoacyl-tRNA synthetases (ARSs) are essential enzymes

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

125 Aminoacyl-tRNA synthetases (ARSs) are ubiquitous, ancien

126 Aminoacyl-tRNA synthetases (ARSs) are universal enzymes

127 Aminoacyl-tRNA synthetases (ARSs) catalyze the attachmen

128 Aminoacyl-tRNA synthetases (ARSs) catalyze the attachmen

129 Aminoacyl-tRNA synthetases (ARSs) function to transfer a

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

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

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

133 A primer selection is facilitated by cognate aminoacyl-tRNA synthetases (ARSs), which bind tRNAs and

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

135 Aminoacyl-tRNA synthetases attach specific amino acids t

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

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

138 Aminoacyl-tRNA synthetase binding is RNase A sensitive,

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

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

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

142 Aminoacyl-tRNA synthetases catalyze ATP-dependent covale

143 Aminoacyl-tRNA synthetases catalyze the attachment of am

144 Aminoacyl-tRNA synthetases catalyze the attachment of am

145 Aminoacyl-tRNA synthetases catalyze the attachment of co

146 Aminoacyl-tRNA synthetases catalyze the attachment of co

147 Aminoacyl-tRNA synthetases catalyze the covalent attachm

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

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

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

151 Urzymes from both aminoacyl-tRNA synthetase classes possess sophisticated

152 Aminoacyl-tRNA synthetases classically regulate protein

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

154 strate protein (zinc finger protein 746) and aminoacyl tRNA synthetase complex interacting multifunct

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

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

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

158 3 to form a stable and conserved large multi-aminoacyl-tRNA synthetase complex (MARS), whose molecula

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

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

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

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

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

164 The aminoacyl-tRNA synthetases constitute the largest protei

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

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

167 The aminoacyl-tRNA synthetases covalently link transfer RNAs

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

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

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

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

172 Aminoacyl tRNA synthetases--enzymes that catalyze the fi

173 Aminoacyl-tRNA synthetases, essential components of the

174 Aminoacyl-tRNA synthetases establish the genetic code by

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

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

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

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

179 r 2 receptor alpha-subunit), MARS (methionyl aminoacyl-tRNA synthetase), FARSB (phenylalanine-tRNA sy

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

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

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

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

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

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

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

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

188 ring stationary phase by phosphorylating the aminoacyl-tRNA synthetases GltX and TrpS.

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

190 Many aminoacyl-tRNA synthetases have an editing activity that

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

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

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

194 Some aminoacyl-tRNA synthetases have editing activities to cl

195 a critical identity element for the histidyl aminoacyl tRNA synthetase (HisRS).

196 Aminoacyl-tRNA synthetases hydrolyze aminoacyl adenylate

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

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

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

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

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

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

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

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

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

206 cted dual-localized proteins, including many aminoacyl-tRNA synthetases, in which a leaky AUG start c

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

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

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

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

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

212 Aminoacyl-tRNA synthetase-interacting multifunctional pr

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

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

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

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

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

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

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

220 Aminoacyl-tRNA synthetases maintain the fidelity during

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

222 tantial evidence implicating the multienzyme aminoacyl-tRNA synthetase (mARS) complex and its AIMp1 s

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

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

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

226 Mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs) are essential comp

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

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

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

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

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

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

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

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

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

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

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

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

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

240 Aminoacyl-tRNA synthetases perform a critical step in tr

241 Many aminoacyl-tRNA synthetases prevent mistranslation by rel

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

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

244 Aminoacyl-tRNA synthetases recognize tRNA anticodon and

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

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

247 Bacterial aminoacyl-tRNA synthetases represent attractive and vali

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

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

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

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

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

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

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

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

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

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

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

259 Here we present newly developed aminoacyl-tRNA synthetases that enable genetic encoding

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

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

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

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

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

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

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

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

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

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

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

271 412d directly in E. coli with an orthogonal aminoacyl-tRNA synthetase/tRNA pair specific for sulfoty

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

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

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

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

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

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

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

279 It relies on mutually orthogonal engineered aminoacyl-tRNA synthetase/tRNA pairs that suppress diffe

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

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

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

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

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

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

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

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

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

289 Aminoacyl-tRNA synthetases use a variety of mechanisms t

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

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

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

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

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

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

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