ライフサイエンスコーパス: aminoacyl

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

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

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

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

5 ite nucleotides that monitor the mRNA in the aminoacyl(A) site adopt different orientations depending

6 Selection of correct aminoacyl (aa)-tRNA at the ribosomal A site is fundament

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

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

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

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

11 ureus seryl-tRNA synthetases in complex with aminoacyl adenylate analogues and applied a structure-ba

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

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

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

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

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

17 nce to McC and various toxic nonhydrolyzable aminoacyl adenylates.

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

19 tional accuracy despite differences in their aminoacyl attachments and anticodon nucleotide sequences

20 in food analysis, as well as non-proteolytic aminoacyl derivatives, which are well-known taste-active

21 A modeled aminoacyl disrupts tRNA-T-box stacking, severing the cen

22 For the treatment of HSV infections the aminoacyl esters of acyclovir were designed, and valacyc

23 selenylation products containing an adjacent aminoacyl group in a fast and efficient way, with high a

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

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

26 able aminoacyl adenylates differing in their aminoacyl moieties.

27 In vitro, AtaT2 acetylates the aminoacyl moiety of isoaccepting glycyl tRNAs, thus prec

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

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

30 Finally, we discover aminoacyl-PGs not only in Gram-positive bacteria but als

31 Aminoacyl-phosphatidylglycerol synthases (aaPGSs) are me

32 no acids, such as 5(4 H)-oxazolones, to form aminoacyl-RNA.

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

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

35 recently been reported that abnormalities in aminoacyl t-RNA synthetase (ARS) genes are linked to var

36 It is known that certain aminoacyl t-RNA synthetase have multiple non-canonical r

37 Aminoacyl t-RNA synthetase proteins are fundamentally kn

38 However, a robust mechanism for aminoacyl thioester formation has not been demonstrated(

39 thereby blocking accommodation of the first aminoacyl transfer RNA (tRNA) into the A site.

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 hat these ribosomes exhibit perturbations in aminoacyl-transfer RNA (aa-tRNA) selection and altered p

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

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

46 r RNA synthetase (Ec ProRS), a member of the aminoacyl-transfer RNA synthetase family, has been inves

47 equires the discovery of multiple orthogonal aminoacyl-transfer RNA synthetase/tRNA pairs.

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

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

50 consisting of elongation factor Tu (EF-Tu), aminoacyl tRNA and GTP, and locks the otherwise dynamica

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

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

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

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

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

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

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

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

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

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

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

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

63 Aminoacyl tRNA synthetases (ARSs) link specific amino ac

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

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

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

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

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

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

70 ary complex of elongation factor Tu (EF-Tu), aminoacyl-tRNA (aa-tRNA), and GTP.

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

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

73 of a bacterial ribosome in complex with a D-aminoacyl-tRNA analog bound to the A site.

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

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

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

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

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

79 e presence of a properly delivered initiator aminoacyl-tRNA at the P site to the distant GTPase cente

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

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

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

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

84 l muscle and lung had significant changes in aminoacyl-tRNA biosynthesis, as analyzed by pathway anal

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

86 al 33 ribosomal states after the delivery of aminoacyl-tRNA by EF-Tu*GTP.

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

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

89 thermo-unstable (EF-Tu), the ribosome, and d-aminoacyl-tRNA deacylase (DTD).

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

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

92 ecognition of a start codon by the initiator aminoacyl-tRNA determines the reading frame of messenger

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

94 Aminoacyl-tRNA enters the translating ribosome in a tern

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

110 se monomers to transfer RNAs (tRNAs) to make aminoacyl-tRNA substrates is a bottleneck.

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

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

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

114 During aminoacyl-tRNA synthesis, stringent substrate discrimina

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

132 Aminoacyl-tRNA synthetase binding is RNase A sensitive,

133 Urzymes from both aminoacyl-tRNA synthetase classes possess sophisticated

134 3 to form a stable and conserved large multi-aminoacyl-tRNA synthetase complex (MARS), whose molecula

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

168 Aminoacyl-tRNA synthetases (aaRS) catalyze both chemical

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

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

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

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

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

174 Aminoacyl-tRNA synthetases (aaRSs) are ancient enzymes t

175 Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes

176 Aminoacyl-tRNA synthetases (aaRSs) are housekeeping enzy

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

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

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

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

181 Aminoacyl-tRNA synthetases (aaRSs) ensure faithful trans

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

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

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

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

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

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

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

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

190 Aminoacyl-tRNA synthetases (ARS) are ubiquitously expres

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

192 Aminoacyl-tRNA synthetases (ARSs) are essential enzymes

193 Aminoacyl-tRNA synthetases (ARSs) are essential enzymes

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

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

196 Aminoacyl-tRNA synthetases (ARSs) are universal enzymes

197 Aminoacyl-tRNA synthetases (ARSs) catalyze the attachmen

198 Aminoacyl-tRNA synthetases (ARSs) catalyze the attachmen

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

214 Aminoacyl-tRNA synthetases are predominantly cytoplasmic

215 Aminoacyl-tRNA synthetases are ubiquitous and essential

216 Aminoacyl-tRNA synthetases catalyze ATP-dependent covale

217 Aminoacyl-tRNA synthetases catalyze the attachment of co

218 Aminoacyl-tRNA synthetases catalyze the covalent attachm

219 Aminoacyl-tRNA synthetases classically regulate protein

220 The aminoacyl-tRNA synthetases constitute the largest protei

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

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

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

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

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

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

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

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

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

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

231 Aminoacyl-tRNA synthetases maintain the fidelity during

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

233 Aminoacyl-tRNA synthetases recognize tRNA anticodon and

234 Bacterial aminoacyl-tRNA synthetases represent attractive and vali

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

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

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

238 Aminoacyl-tRNA synthetases use a variety of mechanisms t

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

254 accurately decode mRNA by proofreading each aminoacyl-tRNA that is delivered by the elongation facto

255 esis by regulating the delivery of the first aminoacyl-tRNA to messenger RNAs (mRNAs).

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

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

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

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 igured decoding center clashes with incoming aminoacyl-tRNA, thereby precluding elongation.

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

264 g the ribosomal A site for the next incoming aminoacyl-tRNA, while precisely maintaining the translat

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

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

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

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

269 hydrolysis and enabling accommodation of the aminoacyl-tRNA.

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

271 experimentally because of the instability of aminoacyl-tRNA.

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

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

274 tions between translation elongation rates, (aminoacyl-) tRNA levels, and codon usage in mammals.

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

276 compete with the RNA degradosome, protecting aminoacyl tRNAs from decay.

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

278 ecificaly target other if not all individual aminoacyl tRNAs.

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

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

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

282 anslation elongation to accommodate incoming aminoacyl-tRNAs and translocate along the mRNA template.

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

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

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

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

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

288 ll conditions, facilitating rapid testing of aminoacyl-tRNAs for a codon match.

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

290 gnate (8-oxoG*C) and near-cognate (8-oxoG*A) aminoacyl-tRNAs increased.

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

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

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

294 Aminoacyl-tRNAs were long thought to be involved solely

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

296 preferentially binding to l-amino acids or l-aminoacyl-tRNAs, thereby excluding d-amino acids.

297 o related transferases recognizing different aminoacyl-tRNAs.

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

299 mited by the intracellular concentrations of aminoacyl-tRNAs.

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