ライフサイエンスコーパス: EF-Tu

1 EF-Tu from the clinically relevant pathogen Pseudomonas

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

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

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

5 EF-Tu(mt) L338Q functions as effectively as wild-type EF

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

7 , a plant unable to perceive EF-Tu, acquires EF-Tu binding sites and responsiveness upon transient ex

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

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

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

11 Here, we show that flagellin and EF-Tu activate a common set of signaling events and defe

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

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

14 50S subunit in a manner similar to EF-G and EF-Tu.

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

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

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

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

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

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

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

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

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

24 t defense responses induced by PAMPs such as EF-Tu reduce transformation by Agrobacterium.

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

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

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

28 ains of bacterial flagellin and of bacterial EF-Tu.

29 Both EF-Tu orthologs discriminate against these misacylated t

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

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

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

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

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

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

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

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

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

39 ell-killing mechanism in which a few cleaved EF-Tu proteins are able block translating ribosomes from

40 reated at the equivalent position in E. coli EF-Tu (Q290L).

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

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

43 E. coli EF-Tu Q290L is more active in poly(U)-directed polymeriz

44 Surprisingly, while E. coli EF-Tu Q290L is more active in polymerization with mitoch

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

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

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

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

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

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

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

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

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

59 table ternary complex with elongation factor EF-Tu preventing any participation in chain elongation.

60 8 (a part of the bacterial elongation factor EF-Tu) but not chitin (a component of fungal cell walls)

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

62 the bacterial translation elongation factor EF-Tu.

63 ooperation with the GTPase elongation factor EF-Tu.

64 ifically cleaves the host translation factor EF-Tu (elongation factor Tu) after it has formed a weak

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

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

67 ite-specifically the host translation factor EF-Tu, ultimately leading to cell death.

68 rylation of the essential translation factor EF-Tu.

69 astidal protein synthesis elongation factor (EF-Tu), which, compared to non-transgenic plants, displa

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

71 The protein synthesis elongation factor, EF-Tu, is a protein that carries aminoacyl-tRNA to the A

72 hly conserved prokaryotic elongation factor, EF-Tu.

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

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

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

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

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

78 minimal threshold of binding free energy for EF-Tu is required for suppression to occur.

79 to identify a receptor kinase essential for EF-Tu perception, which we called EFR.

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

81 the guanosine nucleotide exchange factor for EF-Tu.

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

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

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

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

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

87 sidering the crystal structures of both free EF-Tu.GTP and the ternary complex and allowing for small

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 xpression of plastid-encoded proteins (e.g., EF-Tu, EF-G, and mRNA binding proteins) and thylakoid fo

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

95 through stabilization of the ternary Lit.Gol.EF-Tu complex.

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

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

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

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

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

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

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

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

110 t work, Leu338 was mutated to Gln (L338Q) in EF-Tu(mt).

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

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

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

114 re-accommodation intermediates with inactive EF-Tu.

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

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

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

118 d that the isolated protein was indeed maize EF-Tu.

119 effect of the recombinant precursor of maize EF-Tu (pre-EF-Tu) on thermal aggregation and inactivatio

120 this study support the hypothesis that maize EF-Tu plays a role in heat tolerance by acting as a mole

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

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

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

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

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

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

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

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

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

130 ass I enzymes correlates with the ability of EF-Tu to form a ternary complex with class I but not cla

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

132 Given the abundance of EF-Tu in the cell, this finding is consistent with a cel

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 ractions confirmed the stable association of EF-Tu within the mycoplasma membrane.

138 d to calculate the free energy of binding of EF-Tu to any misacylated E. coli tRNA, and the values ag

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

140 esults also demonstrate that the capacity of EF-Tu to discriminate against both of these aminoacyl-tR

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

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

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

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

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

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

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

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

149 The primary sequence of domain II of EF-Tu is highly conserved.

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

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

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

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

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

155 y(Phe) synthesis is prevented by omission of EF-Tu, or in studies on vacant ribosomes.

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

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

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

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

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

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

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

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

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

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

166 ith the previously determined specificity of EF-Tu for the tRNA body, these experiments further demon

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

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

169 cture strikingly similar to the structure of EF-Tu*GTP.

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

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

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

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

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

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

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

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

178 iana benthamiana, a plant unable to perceive EF-Tu, acquires EF-Tu binding sites and responsiveness u

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

180 nstration of the introduction of a plastidal EF-Tu in plants that leads to protection against heat in

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

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

183 chaperone activity by a plant/eukaryotic pre-EF-Tu protein.

184 Importantly, the recombinant maize pre-EF-Tu displayed chaperone activity.

185 The recombinant pre-EF-Tu was purified from Escherichia coli expressing this

186 he recombinant precursor of maize EF-Tu (pre-EF-Tu) on thermal aggregation and inactivation of the he

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

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

189 affect the function of the encoded protein, EF-Tu.

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

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

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

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

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

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

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

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

200 the preaccommodated state of the tmRNA.SmpB.EF-Tu.70S ribosome complex with much improved definition

201 The results support the concept that EF-Tu ameliorates negative effects of heat stress by act

202 , these experiments further demonstrate that EF-Tu uses thermodynamic compensation to bind cognate am

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

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

205 tolerance, and it has been hypothesized that EF-Tu confers heat tolerance by acting as a molecular ch

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

207 P) bound to yeast Phe-tRNA(Phe) reveals that EF-Tu interacts with the tRNA body primarily through con

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 These results demonstrate that EFR is the EF-Tu receptor and that plant defense responses induced

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

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

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

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

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

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

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

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

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

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

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

227 have demonstrated that Thermus thermophilus EF-Tu does not bind Asp-tRNA (Asn) and predicted a simil

228 e tRNA binding cleft of Thermus Thermophilus EF-Tu were each mutated to structurally conservative alt

229 th Escherichia coli and Thermus thermophilus EF-Tu.

230 e propose that a 1:1:1 complex of SmpB.tmRNA.EF-Tu(GTP) recognizes and binds a stalled ribosome to in

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

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

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

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

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

236 52, G53, and U54 contribute significantly to EF-Tu binding energies.

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

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

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

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

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

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

243 uanosine 5'- [beta,gamma-imido]triphosphate (EF-Tu.GDPNP) bound to yeast Phe-tRNA(Phe) reveals that E

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

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

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

247 , beginning with formation of aminoacyl-tRNA.EF-Tu.GTP ternary complexs and culminating with transloc

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

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

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

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

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

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

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

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

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

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

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

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

260 Elongation factor Tu (EF-Tu) binds and loads elongating aminoacyl-tRNAs (aa-tR

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

262 Elongation factor Tu (EF-Tu) is responsible for the delivery of the aminoacyl-

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

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

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

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

267 o Thermus thermophilus elongation factor Tu (EF-Tu) were determined.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

282 r Thermus thermophilus elongation factor Tu (EF-Tu).GTP were determined using a ribonuclease protecti

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

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

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

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

287 L338Q functions as effectively as wild-type EF-Tu(mt) in poly(U)-directed polymerization with both p

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

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

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

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

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

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

294 ein synthesis through their association with EF-Tu.

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

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

297 Asp-tRNA (Asn), will not form a complex with EF-Tu.

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

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

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

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