ライフサイエンスコーパス: EF-Tu

1 EF-Tu alternates between GTP- and GDP-bound conformation

2 EF-Tu delivers aa-tRNA to the ribosomal A site and parti

3 EF-Tu from the clinically relevant pathogen Pseudomonas

4 EF-Tu is a cytoplasmic protein but has been localized ex

5 EF-Tu is in its active conformation, the switch I loop i

6 EF-Tu is required to support this tRNase activity in vit

7 EF-Tu plays a critical role in mRNA decoding by increasi

8 EF-Tu.GTP.aa-tRNA ternary complex formation and decay ra

9 ribosomes, indicates that in all cases ~3.7 EF-Tu copies are bound on average to each translating 70

10 aaRS, EF-Tu, and the ribosome act as "chiral checkpoints" by p

11 in-ricin loop of the 50S subunit, activating EF-Tu for GTP hydrolysis and enabling accommodation of t

12 end of accommodation corridor passage after EF-Tu release can be reengaged by EF-Tu.GTP from solutio

13 An EF-Tu library was created in which codons specifying the

14 n mRNA codon impedes amino acid addition and EF-Tu GTPase activation.

15 Surprisingly, unlike in eEF1A and EF-Tu, the guanine nucleotide exchange does not cause a

16 eptor kinase (LRR-RK) family called FLS2 and EF-Tu receptor, respectively.

17 K1 is an LRR-RK coreceptor for both FLS2 and EF-Tu receptor.

18 teraction of two abundant proteins, MreB and EF-Tu, in Escherichia coli cells.

19 onformational changes occur in both PPHD and EF-Tu, including a >20-A movement of the EF-Tu switch I

20 single-step displacements from ribosome and EF-Tu diffusive trajectories before and after Onc112 tre

21 specific binding with both the ribosome and EF-Tu.

22 AtFtsZ2-2 assemble together with rpl12A and EF-Tu into a novel chloroplast membrane complex.

23 h the decoding center of the 30S subunit and EF-Tu at the factor binding site.

24 s P-site tRNA, RF2-dependent termination and EF-Tu-dependent decoding are largely unaffected in analo

25 ediate the release of aa-tRNA from EF-Tu and EF-Tu from the ribosome after GTP hydrolysis.

26 lants synthesized and accumulated three anti-EF-Tu cross-reacting polypeptides of similar molecular m

27 further increased in a second and apparently EF-Tu-independent step.

28 rchitecture to translational GTPases such as EF-Tu and the selenocysteine incorporation factor SelB.

29 s elongation factors (EFs) between bacterial EF-Tu and eukaryotic eEF1A.

30 R and FLS2, which are the PRRs for bacterial EF-Tu and flagellin, respectively.

31 Introduction of bacterial EF-Tu residues at these sites into eEF1A protein efficie

32 Our results indicate that ribosome-bound EF-Tu separates from the GAC prior to its full separatio

33 or near-cognate aminoacyl-tRNAs delivered by EF-Tu.

34 cts, and ion dependence of GTP hydrolysis by EF-Tu off and on the ribosome to dissect the reaction me

35 RNA(Lys) complex following GTP hydrolysis by EF-Tu.

36 lection and a proofreading step, mediated by EF-Tu, which forms a ternary complex with aminoacyl(aa)-

37 sage after EF-Tu release can be reengaged by EF-Tu.GTP from solution, coupled to GTP hydrolysis.

38 RNA(Gly) 'misediting paradox' is resolved by EF-Tu in the cell.

39 d by inefficient delivery to the ribosome by EF-Tu, not slow peptide bond formation on the ribosome.

40 ates after the delivery of aminoacyl-tRNA by EF-Tu*GTP.

41 s suggest that overexpression of chloroplast EF-Tu can be beneficial to wheat tolerance to heat stres

42 In vivo studies revealed that V. cholerae EF-Tu is highly sensitive to oxidative protein degradati

43 Here we report that wild-type E. coli EF-Tu and phenylalanyl-tRNA synthetase collaborate with

44 reases the rate of GTP hydrolysis by E. coli EF-Tu by fivefold.

45 n of the H66A mutation into Escherichia coli EF-Tu, whereas Ala-tRNA(Ala) and Gly-tRNA(Gly) were unaf

46 ing of elongation factor Tu ternary complex (EF-Tu*GTP*tRNA) to the ribosome.

47 ribosome to wrap around the ternary complex, EF-Tu(GTP)aa-tRNA.

48 Highly conserved EF-Tu residues are responsible for both attracting aa-tR

49 In contrast, EF-Tu(Mg) 340-358 peptides exhibited minimal blocking ac

50 he CCA tail of the tRNA, weakens the crucial EF-Tu-tRNA interactions, which lowers tRNA binding affin

51 After successful decoding, EF-Tu hydrolyzes GTP, which triggers a conformational ch

52 e resulting closure of the 30S subunit docks EF-Tu at the sarcin-ricin loop of the 50S subunit, activ

53 In so doing, EF-Tu increases the rate and fidelity of the translation

54 ical and pathological significance of a DsbA/EF-Tu association is unknown, peptides derived from the

55 was used to identify a set of sites in eEF1A/EF-Tu associated with eEF1B binding in eukaryotes and an

56 ion, eukaryotic elongation factor 1A (eEF1A; EF-Tu in bacteria) delivers aminoacylated-tRNA to the A-

57 eam pathway with the FLS2/flagellin- and EFR/EF-Tu-mediated signaling pathways.

58 tein/protein docking studies to predict EftM/EF-Tu interactions.

59 p-tRNA synthetase (SepRS), and an engineered EF-Tu (EF-Sep).

60 findings demonstrate how, through evolution, EF-Tu has fine-tuned the structural and dynamic features

61 , reinforced the role of the surface-exposed EF-Tu carboxyl region in Fn binding.

62 evidence that switch I of EF-Tu facilitates EF-Tu's involvement during aa-tRNA selection.

63 ze bacterial flagellin and elongation factor EF-Tu (and their elicitor-active epitopes flg22 and elf1

64 urface-exposed translation elongation factor EF-Tu carrying a Lys-5 trimethylation, incorporated by t

65 A that is delivered by the elongation factor EF-Tu(1).

66 8 (a part of the bacterial elongation factor EF-Tu) but not chitin (a component of fungal cell walls)

67 n of a single protein, the elongation factor EF-Tu, was sufficient to rescue both the ts and bleach-s

68 the bacterial translation elongation factor EF-Tu.

69 tly described location of translation factor EF-Tu on the ribosome and the proposed involvement of h1

70 and can phosphorylate the translation factor EF-Tu, suggesting a persistence mechanism via cell stasi

71 rylation of the essential translation factor EF-Tu.

72 roplast protein synthesis elongation factor, EF-Tu, displays reduced thermal aggregation of leaf prot

73 hly conserved prokaryotic elongation factor, EF-Tu.

74 ly conserved translation elongation factors, EF-Tu in bacteria (known as eEF1A in eukaryotes) and EF-

75 e tRNA mutants with different affinities for EF-Tu to demonstrate that proofreading of aa-tRNAs occur

76 , mutant tRNAs with differing affinities for EF-Tu were assayed for decoding on Escherichia coli ribo

77 biotinyl-lysine, had a very low affinity for EF-Tu:GTP, while the small unnatural AAs on the same tRN

78 ially transit the accommodation corridor for EF-Tu.GDP to release.

79 ve previously identified the gene, eftM (for EF-Tu-modifying enzyme), responsible for this modificati

80 ons, combined with copy number estimates for EF-Tu and ribosomes, indicates that in all cases ~3.7 EF

81 the guanosine nucleotide exchange factor for EF-Tu, directly accelerates both the formation and disso

82 the guanosine nucleotide exchange factor for EF-Tu.

83 lls and uncover a surprising requirement for EF-Tu.

84 served and located near the binding site for EF-Tu and EF-G.

85 e to define the affinity of each aa-tRNA for EF-Tu, both off and on the ribosome.

86 Thus, the affinities of aa-tRNAs for EF-Tu are constrained to be uniform by their need to bin

87 assay of the affinities of the AA-tRNAs for EF-Tu during translation.

88 rary to current models--the reaction in free EF-Tu follows a pathway that does not involve the critic

89 with the velocity of tRNA dissociation from EF-Tu-GDP on the ribosome, which ensure uniform incorpor

90 ry complex but weakly enough to release from EF-Tu during decoding.

91 led at the step of BOP-Lys-tRNA release from EF-Tu into the ribosome.

92 tide bond formation due to slow release from EF-Tu*GDP.

93 nts that mediate the release of aa-tRNA from EF-Tu and EF-Tu from the ribosome after GTP hydrolysis.

94 tely results in the release of the tRNA from EF-Tu.

95 strate that surface-associated M. genitalium EF-Tu (EF-Tu(Mg)), in spite of sharing 96% identity with

96 in the context of translationally active GTP.EF-Tu.tRNA ternary complexes.

97 ally cleaves substrate in the context of GTP.EF-Tu.aa-tRNA complexes.

98 ose that EF-Ts promotes the formation of GTP.EF-Tu.tRNA ternary complexes, thereby accelerating subst

99 rvations suggest that the toxin remodels GTP.EF-Tu.aa-tRNA complexes to free the 3'-end of aa-tRNA fo

100 the toxin domain onto previously solved GTP.EF-Tu.aa-tRNA structures reveals potential steric clashe

101 on of the genetic code depends on the GTPase EF-Tu delivering correctly charged aminoacyl-tRNAs to th

102 lus adhesion and penetration protein [Hap]), EF-Tu, LDH, PD, and P6 exhibited interactions with lamin

103 phases could be made dominant by using high EF-Tu concentrations and/or lower reaction temperature,

104 The structural mechanism of how EF-Tu is involved in proofreading remains to be fully re

105 kinetic model of accommodation and show how EF-Tu can contribute to efficient and accurate proofread

106 Most bacterial trGTPases, including IF2, EF-Tu, EF-G and RF3, play well-known roles in translatio

107 methylation of EF-Tu by EftM does not impact EF-Tu's canonical function in translation.

108 prior to the major conformational change in EF-Tu that follows GTP hydrolysis, or irreversible disso

109 t, rate-determining conformational change in EF-Tu.

110 A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathwa

111 ations reveal that conformational changes in EF-Tu coordinate the rate-limiting passage of aa-tRNA th

112 the toxin induces conformational changes in EF-Tu, displacing a beta-hairpin loop that forms a criti

113 ed to target specific structural elements in EF-Tu to redesign the thermodynamic landscape.

114 tor (EF) Ts-catalyzed nucleotide exchange in EF-Tu in bacteria and particularly in clinically relevan

115 yses identify the coevolution of residues in EF-Tu and aa-tRNAs at the binding interface.

116 The trend in EF-Tu.Cys-tRNA(Cys) binding energies observed as the res

117 site) of an open 30S subunit, while inactive EF-Tu is separated from the 50S subunit.

118 re-accommodation intermediates with inactive EF-Tu.

119 ation factor subfamily of GTPases, including EF-Tu, EF-G, and LepA.

120 stress-responsive toxin HipA, which inhibits EF-Tu, also rescues bacterial growth and protein folding

121 stal structure of PPHD complexed with intact EF-Tu reveals that major conformational changes occur in

122 characterization of two different mesophilic EF-Tu orthologs, one from Escherichia coli, a bacterium

123 s corresponding to this region of EF-Tu(Mp) (EF-Tu(Mp) 340-358) blocked both recombinant EF-Tu(Mp) an

124 The single-molecule tracking of MreB, EF-Tu and MreB-EF-Tu pairs reveals intriguing localizati

125 le-molecule tracking of MreB, EF-Tu and MreB-EF-Tu pairs reveals intriguing localization-dependent he

126 ibution and domain sizes of interacting MreB-EF-Tu pairs as a subpopulation of total EF-Tu.

127 insights to understanding the roles of MreB-EF-Tu interactions.

128 The toxin binds exclusively to domain 2 of EF-Tu, partially overlapping the site that interacts wit

129 t EftM exclusively methylates at lysine 5 of EF-Tu in a distributive manner.

130 rase that directly trimethylates lysine 5 of EF-Tu in P. aeruginosa.

131 ol, constant viability count, the absence of EF-Tu and SecA in the culture medium, and the lack of ef

132 le placement of the first 5-6 amino acids of EF-Tu into a conserved peptide-binding channel in EftM.

133 ing to identify the essential amino acids of EF-Tu(Mp) that mediate Fn interactions by generating mod

134 The GTPase activity of EF-Tu is triggered by ribosome-induced conformational ch

135 ion impairs the essential GTPase activity of EF-Tu, thereby preventing its release from the ribosome.

136 Notably, EF-Ts attenuates the affinity of EF-Tu for GTP and destabilizes ternary complex in the pr

137 nt to significantly reduce the Fn binding of EF-Tu(Mp).

138 r and the guanosine triphosphatase center of EF-Tu.

139 ons, we studied the conformational change of EF-Tu from the guanosine triphosphate to guanine diphosp

140 is the existence of a quaternary complex of EF-Tu/Ts.GTP.aa-tRNA(aa).

141 We find that the steric composition of EF-Tu can reduce the free-energy barrier associated with

142 GDP binding to the apo conformation of EF-Tu is both enthalpically and entropically favored, a

143 e switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to domains D2 and D3 and leads

144 employing fluorescent labeled derivatives of EF-Tu, tRNA, and the ribosome to measure changes in eith

145 -molecule tracking study of the diffusion of EF-Tu in E. coli growing with doubling times in the rang

146 Then, following dissociation of EF-Tu.GDP from the ribosome, the accuracy is further inc

147 GTP hydrolysis enables the GTPase domain of EF-Tu to extend away, releasing EF-Tu from tRNA.

148 tively little is known about the dynamics of EF-Tu interaction with either the ribosome or aa-tRNA.

149 Also, our observed effects of EF-Tu concentration on the fraction of the fast phase of

150 Here, we describe the engineering of EF-Tu for improved selenoprotein synthesis.

151 Here, we provide evidence that switch I of EF-Tu facilitates EF-Tu's involvement during aa-tRNA sel

152 Switch I of EF-Tu rapidly converts from an alpha-helix into a beta-h

153 process of translation through impairment of EF-Tu function.

154 This leads to higher observable levels of EF-Tu trimethylation at the lower temperature.

155 ting the hypothesis that increased levels of EF-Tu will lead to a non-specific protection of leaf pro

156 ween the nucleotide and the switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to do

157 p of EF-Tu, and between the effector loop of EF-Tu and a conserved region of the 16S rRNA.

158 ween the sarcin-ricin loop and the P loop of EF-Tu, and between the effector loop of EF-Tu and a cons

159 ivo temperature dependence of methylation of EF-Tu, preincubation of EftM at 37 degrees C abolished m

160 in the backbone hydrogen bonding network of EF-Tu.

161 Such binding, placing a portion of EF-Tu in contact with the GTPase Associated Center (GAC)

162 The diffusive properties of EF-Tu remain quantitatively indistinguishable across all

163 uce the energetics of the GTPase reaction of EF-Tu with and without the ribosome and with several key

164 ion, the ribosome induces a rearrangement of EF-Tu that renders GTP hydrolysis sensitive to mutations

165 tic peptides corresponding to this region of EF-Tu(Mp) (EF-Tu(Mp) 340-358) blocked both recombinant E

166 ronectin (Fn) through the carboxyl region of EF-Tu.

167 with both aa-tRNA and the switch I region of EF-Tu.

168 es in the conserved GTPase switch regions of EF-Tu that trigger hydrolysis of GTP, along with key int

169 of EF-Ts was paralleled by up-regulation of EF-Tu and induction of genes involved in mitochondrial b

170 To this end, we probe the role of EF-Tu during aa-tRNA accommodation (the proofreading ste

171 g in bacteria, highlight the pivotal role of EF-Tu for fast and accurate protein synthesis, and illus

172 critical in establishing the specificity of EF-Tu for different esterified amino acids.

173 ing activity, reinforcing the specificity of EF-Tu-Fn interactions as mediators of microbial coloniza

174 we have determined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GT

175 as been as laboratory tools for the study of EF-Tu and the ribosome, as their poor pharmacokinetic pr

176 While the amino acids on the surface of EF-Tu that contact aminoacyl-tRNA (aa-tRNA) are highly c

177 amino acid changes corresponding to those of EF-Tu(Mg).

178 ith eftM and conclude that trimethylation of EF-Tu by EftM does not impact EF-Tu's canonical function

179 derstanding of EftM's mechanism of action on EF-Tu.

180 chaperones and proteases acting directly on EF-Tu to modulate the intracellular rate of protein synt

181 he SRL is not critical for GTP hydrolysis on EF-Tu and EF-G.

182 Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism

183 a proofreading step after GTP hydrolysis on EF-Tu.

184 erial pathogen-associated molecular patterns EF-Tu and flagellin, respectively.

185 As a consequence, phosphorylated EF-Tu has a dominant-negative effect in elongation, resu

186 proved by modulating expression of plastidal EF-Tu and/or by selection of genotypes with increased en

187 we determined that binding of M. pneumoniae EF-Tu to Fn is primarily mediated by the EF-Tu carboxyl

188 the classically defined cytoplasmic protein EF-Tu relative to cellular function, compartmentalizatio

189 The G-protein EF-Tu, which undergoes a major conformational change whe

190 The Arabidopsis PRR EF-Tu receptor (EFR) recognizes the bacterial PAMP elong

191 sites, in contrast with the related receptor EF-Tu receptor that can be rendered nonfunctional by dis

192 e molecular mechanism by which it recognizes EF-Tu.

193 (EF-Tu(Mp) 340-358) blocked both recombinant EF-Tu(Mp) and radiolabeled M. pneumoniae cell binding to

194 eractions by generating modified recombinant EF-Tu proteins with amino acid changes corresponding to

195 ing the genetic code rested on reengineering EF-Tu to relax its quality-control function and permit S

196 se domain of EF-Tu to extend away, releasing EF-Tu from tRNA.

197 d Sec incorporation into hAGT; the resulting EF-Tu variants contained highly conserved amino acid cha

198 ese pathways correspond to either reversible EF-Tu.GDP dissociation from the ribosome prior to the ma

199 ar dynamics simulations of the full ribosome-EF-Tu complex.

200 eta-galactosidase, gamma-secretase, ribosome-EF-Tu complex, 20S proteasome and RNA polymerase III, we

201 lows down the rearrangements in the ribosome-EF-Tu-GDP-Pi-Lys-tRNA(Lys) complex following GTP hydroly

202 At saturating EF-Tu concentrations, weaker-binding aa-tRNAs decode the

203 ftM cannot methylate the isolated N-terminal EF-Tu peptide and that binding-induced conformational ch

204 . aeruginosa physiology, we demonstrate that EF-Tu is the only observable substrate for EftM.

205 Here, we provide evidence that EF-Tu is not a target of HipA.

206 the results also support the hypothesis that EF-Tu contributes to heat tolerance by acting as a molec

207 ion in the absence of Hsp33, indicating that EF-Tu is a vital chaperone substrate of Hsp33 in V. chol

208 ll separation from aa-tRNA, and suggest that EF-Tu.GDP dissociates from the ribosome by two different

209 -tRNA is not essential for survival, and the EF-Tu barrier against misacylated aa-tRNA is not absolut

210 s on the structural dynamics of tRNA and the EF-Tu.Cys-tRNA(Cys) interface.

211 iae EF-Tu to Fn is primarily mediated by the EF-Tu carboxyl region.

212 sults support the following conclusions: the EF-Tu ternary complex binds to the A-site whenever it is

213 iation is unknown, peptides derived from the EF-Tu switch I region bound to AbDsbA with submicromolar

214 n of structure activity relationships in the EF-Tu targeting class of thiazolyl peptides.

215 itting reasonably accurate prediction of the EF-Tu binding affinity for all E. coli tRNAs.

216 emonstrated the surface accessibility of the EF-Tu carboxyl region.

217 and EF-Tu, including a >20-A movement of the EF-Tu switch I loop.

218 te has peptidyl-tRNA; and association of the EF-Tu ternary complex is prevented, simply by steric hin

219 s both the formation and dissociation of the EF-Tu-GTP-Phe-tRNA(Phe) ternary complex.

220 he nucleotide into the binding pocket of the EF-Tu.EF-Ts binary complex, followed by displacement of

221 mulations to investigate the dynamics of the EF-Tu.guanosine 5'-triphosphate.aa-tRNA(Cys) complex and

222 s in the elucidation of the structure of the EF-Tu/ribosome complex provide the rare opportunity of g

223 structure of this complex revealed that the EF-Tu switch I region binds to the non-catalytic surface

224 Further characterization confirmed that the EF-Tu- and DsbB-derived peptides bind at two distinct si

225 Thus, the EF-Tu modification by EftM may represent a target to pre

226 odon loop through h44 and protein S12 to the EF-Tu-binding CCA end of aa-tRNA, proposed to signal cog

227 th Escherichia coli and Thermus thermophilus EF-Tu.

228 body had essentially the same affinities to EF-Tu:GTP as natural AAs on this tRNA, but still 2-fold

229 linearly with increasing aa-tRNA affinity to EF-Tu.

230 ing on the observation that EftM can bind to EF-Tu lacking its N-terminal peptide (encompassing the L

231 that balance the strength of tRNA binding to EF-Tu-GTP with the velocity of tRNA dissociation from EF

232 be responsible for tuning aa-tRNA binding to EF-Tu.

233 tional change when EF-Tu.GTP is converted to EF-Tu.GDP, forms part of an aminoacyl(aa)-tRNA.EF-Tu.GTP

234 In contrast, binding of GTP to EF-Tu is entropically driven by the liberation of bound

235 rily account for tRNA binding specificity to EF-Tu.

236 t predicts the DeltaG degrees of any tRNA to EF-Tu using the sequence of its three T-stem base pairs.

237 ave a characteristic DeltaG degrees value to EF-Tu, but different T-stem sequences are used to achiev

238 number of aa-tRNAs that bind more weakly to EF-Tu than expected and thus are candidates for acting a

239 MreB-EF-Tu pairs as a subpopulation of total EF-Tu.

240 presence of SAM, EftM directly trimethylates EF-Tu.

241 odulating GTP hydrolysis by aminoacyl-tRNA * EF-Tu * GTP ternary complexes during the elongation phas

242 osphate (GTP) hydrolysis by aminoacyl-tRNA * EF-Tu * GTP.

243 -Tu.GDP, forms part of an aminoacyl(aa)-tRNA.EF-Tu.GTP ternary complex (TC) that accelerates the bind

244 criminating against these misacylated tRNAS, EF-Tu plays a direct role in preventing misincorporation

245 that surface-associated M. genitalium EF-Tu (EF-Tu(Mg)), in spite of sharing 96% identity with EF-Tu(

246 ocalized M. pneumoniae elongation factor Tu (EF-Tu(Mp)) mediates binding to the extracellular matrix

247 al MAMPs flagellin and elongation factor Tu (EF-Tu) activate distinct, phylogenetically related cell

248 res the GTPase factors elongation factor Tu (EF-Tu) and EF-G.

249 uential association of elongation factor Tu (EF-Tu) and elongation factor G (EF-G) with the ribosome

250 ring GTP hydrolysis on elongation factor Tu (EF-Tu) and elongation factor G (EF-G).

251 n ternary complex with elongation factor Tu (EF-Tu) and GTP and then, again, in a proofreading step a

252 a ternary complex with elongation factor Tu (EF-Tu) and GTP.

253 lex with the G-protein elongation factor Tu (EF-Tu) and GTP.

254 zes the bacterial PAMP elongation factor Tu (EF-Tu) and its derived peptide elf18.

255 We identify elongation factor Tu (EF-Tu) as a PPHD substrate, which undergoes prolyl-4-hyd

256 Elongation factor Tu (EF-Tu) binds to all standard aminoacyl transfer RNAs (aa

257 e translational GTPase elongation factor Tu (EF-Tu) delivers a transfer RNA (tRNA) to the ribosome.

258 In translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-pro

259 o Thermus thermophilus elongation factor Tu (EF-Tu) revealed that much of the specificity for tRNA oc

260 ly conserved His-66 of elongation factor Tu (EF-Tu) stacks on the side chain of the esterified Phe of

261 lar PGH motif found in elongation factor Tu (EF-Tu) that is required for GTP hydrolysis on interactio

262 diA-CT(EC869) binds to elongation factor Tu (EF-Tu) with high affinity and this interaction is critic

263 lved to bind bacterial elongation factor Tu (EF-Tu) with uniform affinities, mutant tRNAs with differ

264 GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-t

265 lex (TC) consisting of elongation factor Tu (EF-Tu), aminoacyl tRNA and GTP, and locks the otherwise

266 s a ternary complex of elongation factor Tu (EF-Tu), aminoacyl-tRNA (aa-tRNA), and GTP.

267 By analogy to elongation factor Tu (EF-Tu), SelB is expected to control the delivery and rel

268 by its poor binding to elongation factor Tu (EF-Tu), the yield of incorporation into peptide is addit

269 se) factors, including elongation factor Tu (EF-Tu), which delivers aminoacyl-transfer RNAs (tRNAs) t

270 red to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) an

271 for production of the elongation factor Tu (EF-Tu)-targeting 29-member thiazolyl peptide GE37468 fro

272 g protein, translation elongation factor Tu (EF-Tu).

273 universally conserved elongation factor Tu (EF-Tu).

274 s Sec depending on the elongation factor Tu (EF-Tu).

275 GTPase reaction of the elongation factor Tu (EF-Tu).

276 lizing the translation elongation factor Tu (EF-Tu).

277 cyl-tRNAs delivered by elongation factor Tu (EF-Tu).

278 e immunity protein and elongation factor Tu (EF-Tu).

279 sociated M. pneumoniae elongation factor Tu (EF-Tu, also called MPN665) serves as a fibronectin (Fn)-

280 specifically binds to elongation factor-Tu (EF-Tu) and targets it for degradation by the protease Lo

281 ing protein synthesis, elongation factor-Tu (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tR

282 ase EftM trimethylates elongation factor-Tu (EF-Tu) on lysine 5 to form a post-translational modifica

283 otein (RasGAP) and the elongation factor-Tu (EF-Tu) with a 1 W mechanism is still valid for the 2 W p

284 of Onc112 on ribosome, elongation factor-Tu (EF-Tu), and DNA spatial distributions and diffusive prop

285 timulates elongation factor thermo unstable (EF-Tu)-dependent GTP hydrolysis in vitro.

286 ethylates elongation factor-thermo-unstable (EF-Tu) on lysine 5.

287 dentified elongation factor thermo-unstable (EF-Tu), l-lactate dehydrogenase (LDH), protein D (PD), a

288 (aaRSs), elongation factor thermo-unstable (EF-Tu), the ribosome, and d-aminoacyl-tRNA deacylase (DT

289 mation most closely resembles that seen upon EF-Tu-GTP-aminoacyl-tRNA binding to the 70S ribosome.

290 d threonine, Thr-382, which was blocked when EF-Tu was treated with the antibiotic kirromycin.

291 undergoes a major conformational change when EF-Tu.GTP is converted to EF-Tu.GDP, forms part of an am

292 t, at intersubunit bridge B8, close to where EF-Tu engages the ribosome.

293 ein synthesis through their association with EF-Tu.

294 nto yeast tRNA Phe resulted in chimeras with EF-Tu binding affinities similar to those for the donor

295 that aminoacyl-tRNAs in ternary complex with EF-Tu*GTP can readily dissociate and rebind to aminoacyl

296 ilization of the EF-Ts variants complex with EF-Tu, in agreement with the dramatic steady-state level

297 First, aa-tRNAs in ternary complex with EF-Tu.GDP are selected in a step where the accuracy incr

298 tal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolu

299 (Mg)), in spite of sharing 96% identity with EF-Tu(Mp), does not bind Fn.

300 ctron microscopy map of the aminoacyl-tRNA x EF-Tu x GDP x kirromycin-bound Escherichia coli ribosome