ライフサイエンスコーパス: aminoacyl

1 and whether functional linkages between the aminoacyl (A) and E sites modulate the dynamics of prote

2 me footprint lengths can reveal the ribosome aminoacyl (A) and peptidyl (P) site locations.

3 ccupies the ribosomal decoding center at the aminoacyl (A) site in a manner resembling that of the tR

4 ith elongation factor-Tu and GTP, enters the aminoacyl (A) site of the ribosome via a multi-step, mRN

5 ariety of three-nucleotide codons within the aminoacyl (A) site, but how these endonucleases achieve

6 e adjacent GUA triplet coding for Val at the aminoacyl (A) site.

7 d AUA codons at both the peptidyl- (P-), and aminoacyl- (A-) sites of the ribosome.

8 is converted to EF-Tu.GDP, forms part of an aminoacyl(aa)-tRNA.EF-Tu.GTP ternary complex (TC) that a

9 cells, whereas the Bp1026b toxin cleaves the aminoacyl acceptor stems of tRNA molecules.

10 The aminoacyl-acceptor stem plays a major role in stopping R

11 ally encoded mismatched nucleotides in their aminoacyl-acceptor stem sequences.

12 it is processed releasing a non-hydrolyzable aminoacyl adenylate that inhibits an essential aminoacyl

13 nsfer editing, which hydrolyzes misactivated aminoacyl-adenylate intermediate via a nebulous mechanis

14 This selective rejection of a non-protein aminoacyl-adenylate is in addition to known kinetic disc

15 sult in a specificity switch toward aromatic aminoacyl-adenylate substrates.

16 lso able to detoxify several nonhydrolyzable aminoacyl adenylates but not processed McC.

17 e can specifically detoxify non-hydrolyzable aminoacyl adenylates differing in their aminoacyl moieti

18 nce to McC and various toxic nonhydrolyzable aminoacyl adenylates.

19 e enzymes may be used to avert various toxic aminoacyl-adenylates that accumulate during antibiotic b

20 ognate tRNA, IleRS exhibits a 10-fold faster aminoacyl-AMP hydrolysis and a 10-fold drop in amino aci

21 ds by acylation of cysteine with N-(Pg-alpha-aminoacyl)- and N-(Pg-alpha-dipeptidoyl)benzotriazoles (

22 lpha-hydroxycarboxylic acids with N-Pg(alpha-aminoacyl)benzotriazoles followed by deprotection produc

23 N-Pg(alpha-Aminoacyl)benzotriazoles reacted with alpha-hydroxycarbo

24 of steady-state kinetic parameters for both aminoacyl-beta-naphthylamide and unmodified dipeptide su

25 ds into chiral potential novel pharmacophore aminoacyl conjugates (33-53%).

26 S-(Pg-alpha-aminoacyl)cysteines 4a,b underwent native chemical ligat

27 ed alanyl-PG then revealed hydrolysis of the aminoacyl linkage, resulting in the formation of alanine

28 Surprisingly, the aminoacyl moieties of these tRNAs also exhibit exception

29 ves an amide bond connecting the peptidyl or aminoacyl moieties of, respectively, intact and processe

30 able aminoacyl adenylates differing in their aminoacyl moieties.

31 ce of H-bonding interactions between the two aminoacyl moieties.

32 trolling the stability and reactivity of the aminoacyl moiety and has important implications for the

33 The prediction of an interaction between an aminoacyl moiety and the adenine nucleobase was confirme

34 bstrates reveals the tRNA acceptor stem, the aminoacyl moiety, and the polar head group of PG as the

35 and YhhY protect bacteria from various toxic aminoacyl nucleotides, either exogenous or those generat

36 Aminoacyl-phosphatidylglycerol synthases (aaPGSs) are me

37 ove sequentially on the ribosome from the A (aminoacyl) site to the P (peptidyl) site to the E (exit)

38 fer was observed only with a slowly reacting aminoacyl-site nucleophile, proline.

39 Here, we examine tRNA-aminoacyl synthetase (ARS) localization in protein synth

40 ains were progressively added to cytoplasmic aminoacyl transfer RNA (tRNA) synthetases during evoluti

41 an expanded translation machinery, including aminoacyl transfer RNA synthetases with specificities fo

42 Here, we perform simulations of large-scale aminoacyl-transfer RNA (aa-tRNA) rearrangements during a

43 Aminoacyl-transfer RNA (tRNA) synthetases (RS) are essen

44 Protein biosynthesis requires aminoacyl-transfer RNA (tRNA) synthetases to provide ami

45 lation are conserved in evolution, bacterial aminoacyl-transfer RNA synthetases are unable to acylate

46 of eukaryote-specific domains from bacterial aminoacyl-transfer RNA synthetases.

47 ring protein synthesis, the ribosome selects aminoacyl-transfer RNAs with anticodons matching the mes

48 ptide, a peptidoglycan precursor used by the aminoacyl-transferase FemXWv for synthesis of the bacter

49 It involves accurate selection of each aminoacyl tRNA as dictated by the mRNA codon, catalysis

50 being allosterically released when the next aminoacyl tRNA binds to the A site.

51 by mTORC1-S6K1 induces its release from the aminoacyl tRNA multisynthetase complex, which is require

52 We measured the rupture forces of aminoacyl tRNA or peptidyl tRNA mimic from the ribosome

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

68 ch reaction, the alpha-amine of the incoming aminoacyl tRNA versus the water molecule.

69 o acids on the surface of EF-Tu that contact aminoacyl-tRNA (aa-tRNA) are highly conserved among bact

70 Aminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternar

71 (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tRNA (aa-tRNA) into actively translating ribos

72 explain the high fidelity and efficiency of aminoacyl-tRNA (aa-tRNA) selection by the ribosome.

73 Aminoacyl-tRNA (aa-tRNA), in a ternary complex with elon

74 g the site that interacts with the 3'-end of aminoacyl-tRNA (aa-tRNA).

75 translation by modulating GTP hydrolysis by aminoacyl-tRNA * EF-Tu * GTP ternary complexes during th

76 uanosine-5'-triphosphate (GTP) hydrolysis by aminoacyl-tRNA * EF-Tu * GTP.

77 erase center of the ribosome interferes with aminoacyl-tRNA accommodation, suggesting that during can

78 Comparison of aminoacyl-tRNA analogs demonstrates that the T-box detec

79 t which acts as an analogue of the 3'-end of aminoacyl-tRNA and terminates protein synthesis by accep

80 ctor-1A and its ternary complex with GTP and aminoacyl-tRNA are common targets for the evolution of c

81 fects were observed using the same, natural, aminoacyl-tRNA at the A site and all rates of accommodat

82 vent stable binding and accommodation of the aminoacyl-tRNA at the A-site, leading to inhibition of p

83 in their elongation activity at the level of aminoacyl-tRNA binding in vitro.

84 f eubacterial IF1, by blocking the ribosomal aminoacyl-tRNA binding site (A site) at the initiation s

85 r tRNAs to the second codon presented in the aminoacyl-tRNA binding site (A site).

86 t closely resembles that seen upon EF-Tu-GTP-aminoacyl-tRNA binding to the 70S ribosome.

87 m, glycine, serine and threonine metabolism, aminoacyl-tRNA biosynthesis and taurine and hypotaurine

88 athways (pentose phosphate, carbon fixation, aminoacyl-tRNA biosynthesis, one-carbon-pool by folate)

89 olyamine, lysine, tryptophan metabolism, and aminoacyl-tRNA biosynthesis; and in CSF involved cortiso

90 etermined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GTP analog,

91 The crystal structure of dimeric D-aminoacyl-tRNA deacylase (DTD) from Plasmodium falciparu

92 al proofreading underlies the inability of D-aminoacyl-tRNA deacylase (DTD) to discriminate between D

93 This unexpected relationship between aminoacyl-tRNA decoding and translocation suggests that

94 The crucial process of aminoacyl-tRNA delivery to the ribosome is energized by

95 conditions, such as amino acid starvation or aminoacyl-tRNA depletion due to a high level of recombin

96 rossing attempt frequency was calculated for aminoacyl-tRNA elbow-accommodation.

97 steps in the accommodation process, wherein aminoacyl-tRNA enters the peptidyltransferase center of

98 Aminoacyl-tRNA enters the translating ribosome in a tern

99 Parallel analyses of adenylate and aminoacyl-tRNA formation reactions by wild-type and muta

100 ty control via two-step pathways for cognate aminoacyl-tRNA formation.

101 e activity reduces the amount of the cognate aminoacyl-tRNA in a cell-free translation system resulti

102 nteraction strength between the ribosome and aminoacyl-tRNA in presence of viomycin.

103 otic binding should prevent the placement of aminoacyl-tRNA in the catalytic site, it is commonly ass

104 findings demonstrate an unexpected role for aminoacyl-tRNA in the formation of dehydroamino acids in

105 codon recognition by elongation factor-bound aminoacyl-tRNA is initiated by hydrogen bond interaction

106 S. pneumoniae depends in part upon MurM, an aminoacyl-tRNA ligase that attaches L-serine or L-alanin

107 SILAC experiments conducted in culture, the aminoacyl-tRNA precursor pool is near completely labeled

108 ent within intracellular free amino acid and aminoacyl-tRNA precursor pools in dividing and division-

109 re preferentially utilized as substrates for aminoacyl-tRNA precursors for protein synthesis.

110 Human DUE-B also retains the aminoacyl-tRNA proofreading function of its shorter orth

111 nce context plays a key role in near-cognate aminoacyl-tRNA selection during PTC suppression.

112 t rotated state with an exposed codon in the aminoacyl-tRNA site (A site).

113 racycline interfere with tRNA binding to the aminoacyl-tRNA site on the small 30S ribosomal subunit.

114 The mutually exclusive aminoacyl-tRNA substrate specificities of the WT and eng

115 hydrophobic lipid substrate PG and the polar aminoacyl-tRNA substrate to access the catalytic site fr

116 l-transfer RNA (tRNA) synthetases to provide aminoacyl-tRNA substrates for the ribosome.

117 s problem by fast kinetics using full-length aminoacyl-tRNA substrates with atomic substitutions that

118 rated fatty acids; decreases occurred in the aminoacyl-tRNA synthesis pathway.

119 Quality control during aminoacyl-tRNA synthesis reduces non-protein amino acid

120 During aminoacyl-tRNA synthesis, stringent substrate discrimina

121 but also by amino acid uptake, recycling and aminoacyl-tRNA synthesis.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

138 Aminoacyl-tRNA synthetase binding is RNase A sensitive,

139 Urzymes from both aminoacyl-tRNA synthetase classes possess sophisticated

140 3 to form a stable and conserved large multi-aminoacyl-tRNA synthetase complex (MARS), whose molecula

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

177 Aminoacyl-tRNA synthetases (aaRS) catalyze both chemical

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

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

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

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

182 Aminoacyl-tRNA synthetases (aaRSs) are housekeeping enzy

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

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

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

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

187 Aminoacyl-tRNA synthetases (aaRSs) ensure faithful trans

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

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

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

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

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

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

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

195 Aminoacyl-tRNA synthetases (ARSs) catalyze the attachmen

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

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

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

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

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

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

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

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

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

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

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

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

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

209 Aminoacyl-tRNA synthetases attach specific amino acids t

210 Aminoacyl-tRNA synthetases catalyze ATP-dependent covale

211 Aminoacyl-tRNA synthetases catalyze the covalent attachm

212 Aminoacyl-tRNA synthetases classically regulate protein

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

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

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

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

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

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

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

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

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

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

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

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

225 Aminoacyl-tRNA synthetases maintain the fidelity during

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

227 Aminoacyl-tRNA synthetases perform a critical step in tr

228 Many aminoacyl-tRNA synthetases prevent mistranslation by rel

229 Aminoacyl-tRNA synthetases recognize tRNA anticodon and

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

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

232 Aminoacyl-tRNA synthetases use a variety of mechanisms t

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

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

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

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

237 Aminoacyl-tRNA synthetases, essential components of the

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

254 secondary metabolic pathways by hijacking an aminoacyl-tRNA to the antibiotic biosynthetic pathway.

255 ies: while TET sterically hinders binding of aminoacyl-tRNA to the ribosome, NEG stabilizes its bindi

256 d by the TEF1 and TEF2 genes in yeast) is an aminoacyl-tRNA transferase needed during protein transla

257 diated by the base pairing of a near-cognate aminoacyl-tRNA with a PTC and subsequently, the amino ac

258 g the rate of ATP consumption to the rate of aminoacyl-tRNA(AA) formation demonstrated that pre-trans

259 as well as catalytic hydrolysis of mispaired aminoacyl-tRNA(Phe) species.

260 ngation factor-1A ternary complex (eEF1A.GTP.aminoacyl-tRNA) as a specific target and demonstrate com

261 ognate deacyl-tRNA binds to the ribosomal A (aminoacyl-tRNA) site.

262 Using a simple method to prepare homogeneous aminoacyl-tRNA, we show that the Bacillus subtilis glyQS

263 and near-cognate tRNA anticodons explore the aminoacyl-tRNA-binding site (A site) of an open 30S subu

264 About 10 years ago, an aminoacyl-tRNA-dependent enzyme involved in the biosynth

265 y the description of an increasing number of aminoacyl-tRNA-dependent enzymes involved in secondary m

266 This review describes the three groups of aminoacyl-tRNA-dependent enzymes involved in the synthes

267 experimentally because of the instability of aminoacyl-tRNA.

268 e to capture the chiral centre of incoming D-aminoacyl-tRNA.

269 unit that are essential for accommodation of aminoacyl-tRNA.

270 hydrolysis and enabling accommodation of the aminoacyl-tRNA.

271 nascent-chain C terminus or at the incoming aminoacyl-tRNA.

272 beta-alanine; valine, leucine, iso-leucine; aminoacyl-tRNA; and alanine, aspartate, glutamate.

273 ing intermediates of translation elongation (aminoacyl-tRNAeEF1A), termination (eRF1eRF3), and riboso

274 ding of either EF-G to the PRE complex or of aminoacyl-tRNAEF-Tu ternary complex to the POST complex

275 ryotic elongation factor 1A (eEF1A) delivers aminoacyl tRNAs to the A-site of the translating 80S rib

276 Aminoacyl-tRNAs (aa-tRNAs) are selected by the messenger

277 ynthetases (aaRSs) and accurate selection of aminoacyl-tRNAs (aa-tRNAs) by the ribosome.

278 To better understand why aminoacyl-tRNAs (aa-tRNAs) have evolved to bind bacteria

279 ) are enzymes that transfer amino acids from aminoacyl-tRNAs (aa-tRNAs) to phosphatidylglycerol (PG)

280 zes proteins using exclusively L- or achiral aminoacyl-tRNAs (aa-tRNAs), despite the presence of D-am

281 noacylation site and hydrolysis of misformed aminoacyl-tRNAs at the editing site.

282 The selection of aminoacyl-tRNAs by the ribosome is a fundamental step in

283 thetases (aaRSs) and inaccurate selection of aminoacyl-tRNAs by the ribosome.

284 es of ribosomes with cognate or near-cognate aminoacyl-tRNAs delivered by EF-Tu.

285 omes decode mRNA codons by selecting cognate aminoacyl-tRNAs delivered by elongation factor Tu (EF-Tu

286 explains how the enriched cellular pool of L-aminoacyl-tRNAs escapes this proofreading step.

287 mponents to study initial codon selection of aminoacyl-tRNAs in ternary complex with elongation facto

288 talling motifs, peptidyl transfer to certain aminoacyl-tRNAs is inhibited.

289 eEF1A is responsible for the delivery of all aminoacyl-tRNAs to the ribosome, aside from initiator an

290 EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in

291 The affinities of eight aminoacyl-tRNAs were differentially destabilized by the

292 Aminoacyl-tRNAs were long thought to be involved solely

293 different pattern of binding of 10 different aminoacyl-tRNAs, clearly showing that this position is c

294 ontrol mechanism, the editing of misacylated aminoacyl-tRNAs, provides a critical checkpoint both for

295 d by the inevitable interaction with cognate aminoacyl-tRNAs.

296 mited by the intracellular concentrations of aminoacyl-tRNAs.

297 oper decoding of mRNAs by the ribosome using aminoacyl-tRNAs.

298 rt, by proofreading of the newly synthesized aminoacyl-tRNAs.

299 s for the reactivity and stability of normal aminoacyl-tRNAs.

300 o related transferases recognizing different aminoacyl-tRNAs.