ライフサイエンスコーパス: EF-G

1 EF-G binds to the ribosome in a GTP-bound form and subse

2 EF-G catalyzes translocation of mRNA and tRNAs within th

3 EF-G dependent translocation from the classical PRE comp

4 EF-G rearrangement would then provide directional contro

5 EF-G.GTP binding to the pretranslocation (PRE) complex a

6 ctors along with elongation factors G and 4 (EF-G and EF4).

7 In support of this model, an EF-G truncation variant that does not possess domains IV

8 uggest that the SRL is crucial for anchoring EF-G on the ribosome during mRNA-tRNA translocation.

9 ment of crystal structures of EF-G bound and EF-G unbound ribosomal subunits.

10 ormation of the more stable EF-G complex and EF-G-induced RRF dissociation.

11 bacteria (known as eEF1A in eukaryotes) and EF-G (eEF2), which deliver aminoacyl-tRNAs to the riboso

12 lyzed by RRF (ribosome recycling factor) and EF-G (elongation factor G).

13 high structural similarity between LepA and EF-G enabled us to derive a homology model for LepA boun

14 degree of sequence identity between LepA and EF-G is reflected in the structural similarity between t

15 he individual homologous domains of LepA and EF-G.

16 ated tRNAs are bound to the 70S ribosome and EF-G-GTP is added, bases A1492 and A1493 again show subs

17 undance of FusB-type protein, ribosomes, and EF-G.

18 RRF and EF-G (a) each form a binary complex on binding to a bare

19 eme that accounts quantitatively for RRF and EF-G interaction on the Escherichia coli ribosome.

20 ular basis for ribosome recycling by RRF and EF-G remains unclear.

21 into subunits by the joint action of RRF and EF-G.

22 or the splitting of 70S ribosomes by RRF and EF-G/GTP during the lag phase for activation of ribosome

23 ng and accommodation to the empty A site and EF-G action either leads to the slippage of the tRNAs in

24 m of deacylated tRNA into the 50S E site and EF-G binding to the ribosome both contribute to stabiliz

25 not critical for GTP hydrolysis on EF-Tu and EF-G.

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

27 ase factors elongation factor Tu (EF-Tu) and EF-G.

28 depends on competition between viomycin and EF-G for binding to the pretranslocation ribosome, and t

29 When apo-EF-G is bound to 70S ribosomes and GTP is added, substan

30 ndirect structural changes in this region as EF-G is bound and as GTP is hydrolyzed.

31 tance, we have characterized three S. aureus EF-G mutants with fast kinetics and crystal structures.

32 7.3-A cryo-EM structure of a complex between EF-G and the 70S ribosome.

33 the precise identity of the contacts between EF-G and ribosome components.

34 ved from it, showing the interaction between EF-G and RRF on the 50S subunit in the presence of the n

35 formed, by ultraviolet irradiation, between EF-G and a sarcin/ricin domain (SRD) oligoribonucleotide

36 pendent GTP hydrolysis is inhibited for both EF-G and EF4, with IC(50) values equivalent to the 70S r

37 e in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conf

38 x and one of the 50S subunit bound with both EF-G and RRF.

39 ously observed only in the presence of bound EF-G.

40 GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labele

41 We show that ribosome-bound EF-G adopts distinct conformations corresponding to the

42 Our data suggest that ribosome-bound EF-G may also occasionally sample at least one more comp

43 By contrast, ribosome-bound EF-G predominantly adopts an extended conformation regar

44 s studies have suggested that ribosome-bound EF-G undergoes significant structural rearrangements.

45 not increase the lability of ribosome-bound EF-G.

46 rmations in ribosome-free and ribosome-bound EF-G.

47 nd tRNAs within the ribosome is catalyzed by EF-G binding and GTP hydrolysis.

48 GTP hydrolysis catalyzed by EF-G does not affect the relative stability of the obser

49 of the ribosome-stimulated GTP hydrolysis by EF-G to tRNA/mRNA translocation remains debated.

50 promotes futile cycles of GTP hydrolysis by EF-G.

51 , the rates of mRNA translocation induced by EF-G in the presence of GTP and a non-hydrolyzable analo

52 Energy liberated by EF-G's GTPase activity is necessary for EF-G to catalyze

53 ransfer RNA translocation on the ribosome by EF-G, translates a large-scale movement of EF-G's domain

54 se that the release of ribosome-bound RRF by EF-G is required for post-termination complex disassembl

55 The release of bound RRF by EF-G is stimulated by GTP analogues.

56 Cryo-EM reconstructions of certain EF-G-containing complexes led to the proposal that the m

57 the observed failure of FusB to bind E. coli EF-G, and its inability to confer resistance in E. coli.

58 e GTPase active site, resulting in a compact EF-G conformation that favors an intermediate state of r

59 onance energy transfer (smFRET) between (Cy5)EF-G and (Cy3)tRNALys, we studied the translational elon

60 rate that single-turnover ribosome-dependent EF-G GTPase proceeds according to a kinetic scheme in wh

61 We find that hairpin opening occurs during EF-G-catalyzed translocation and is driven by the forwar

62 rmational changes typically only seen during EF-G-mediated translocation of the mRNA-tRNA pairs.

63 idyl-tRNA in the small subunit P site during EF-G-catalyzed translocation.

64 to the A-site of the ribosome, whereas eEF2 (EF-G in bacteria) translocates the ribosome along the mR

65 l of translocation that begins with the eEF2/EF-G binding-induced ratcheting motion of the small ribo

66 A-site binding of either EF-G to the PRE complex or of aminoacyl-tRNAEF-Tu ternar

67 In every round of translation elongation, EF-G catalyzes translocation, the movement of tRNAs (and

68 of an elongation factor (eEF2 in eukaryotes, EF-G in bacteria).

69 Elongation factor EF-G (fusA [mhp083]) (P = 0.002), RNA polymerase beta ch

70 acterial post-TCs requires elongation factor EF-G and a ribosome recycling factor RRF.

71 me, a process catalyzed by elongation factor EF-G, is a crucial step in protein synthesis.

72 uence and structure to the elongation factor EF-G.

73 xchange within translation elongation factor EF-G.

74 The essential translation factor EF-G is an in vivo substrate of PrkC and this phosphoryl

75 es with the activity of translocation factor EF-G to unwind mRNA secondary structures using high-reso

76 y a universally conserved elongation factor (EF-G in prokaryotes and EF-2 in eukaryotes).

77 ical/open state and toward states that favor EF-G dissociation apparently allows the PRE complex to e

78 ve defined the steps leading to fully folded EF-G.

79 intact aminoacyl tRNAs as substrates and for EF-G catalyzed translocation.

80 ain stabilities, which is likely crucial for EF-G function, complicates the folding of this large mul

81 These results suggest a novel function for EF-G and RRF in the post-stress return of PSRP1/pY-inact

82 n and suggests a common GTPase mechanism for EF-G and elongation factor Tu.

83 d by EF-G's GTPase activity is necessary for EF-G to catalyze rapid and precise translocation.

84 other hand, the affinity of the ribosome for EF-G*GTP is increased when peptidyl-tRNA is in the A-sit

85 increased the maximal rate of both forward (EF-G dependent) and reverse (spontaneous) translocation.

86 movements of the tRNAs and mRNA or to foster EF-G dissociation from the ribosome after translocation

87 Free EF-G, not bound to the ribosome, adopts quite different

88 Our results indicate that ribosome-free EF-G predominantly adopts a compact conformation that ca

89 the hairpin promotes dissociation of futile EF-G and thus causes multiple EF-G driven translocation

90 recycling factor (RRF), elongation factor G (EF-G) and GTP split 70S ribosomes into subunits.

91 a reaction catalyzed by elongation factor G (EF-G) and guanosine triphosphate (GTP).

92 sidic acid (FA) targets elongation factor G (EF-G) and inhibits ribosomal peptide elongation and ribo

93 etween the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal s

94 two conserved proteins, elongation factor G (EF-G) and the ribosome recycling factor (RRF).

95 of G proteins, such as elongation factor G (EF-G) bound to the ribosome, as well as many biochemical

96 n synthesis by blocking elongation factor G (EF-G) catalyzed translocation of messenger RNA on the ri

97 triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent movement of mRNA and tRNA

98 rsally conserved GTPase elongation factor G (EF-G) catalyzes the translocation of tRNA and mRNA on th

99 ribosome is promoted by elongation factor G (EF-G) during the translation cycle.

100 ycling factor (RRF) and elongation factor G (EF-G) in a guanosine 5'-triphosphate (GTP)-hydrolysis-de

101 osome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation factor 2 (EF-2) in e

102 ing from the binding of elongation factor G (EF-G) in various forms.

103 tion factor 2 (IF2) and elongation factor G (EF-G) induce similar changes in ribosome structure.

104 Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays

105 Elongation factor G (EF-G) is a universally conserved translational GTPase th

106 Binding of elongation factor G (EF-G) shifts this equilibrium toward the closed conforma

107 ntrast, the activity of elongation factor G (EF-G) was strongly impaired in alpha-sarcin-treated ribo

108 n factor Tu (EF-Tu) and elongation factor G (EF-G) with the ribosome during protein synthesis were un

109 otic protein synthesis, elongation factor G (EF-G), a guanosine triphosphatase (GTPase), binds to the

110 In elongation factor G (EF-G), a highly conserved protein composed of 5 domains,

111 recycling factor (RRF), elongation factor G (EF-G), and GTP to prepare the ribosome for a fresh round

112 or (RRF), together with elongation factor G (EF-G), disassembles this posttermination complex into mR

113 factor (RRF) and GTPase elongation factor G (EF-G), synergistically split 100S ribosomes in a GTP-dep

114 These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translation from FA-

115 a proper substrate for elongation factor G (EF-G), thus inhibiting translocation until the E-site tR

116 The elongation factor G (EF-G)-catalyzed translocation of mRNA and tRNA through t

117 ed significantly slower elongation factor G (EF-G)-catalyzed translocation through the slippery seque

118 onstructions of certain elongation factor G (EF-G)-containing complexes have led to the proposal that

119 triphosphatase (GTPase) elongation factor G (EF-G).

120 complex and catalyzed by elongtion factor G (EF-G).

121 n factor Tu (EF-Tu) and elongation factor G (EF-G).

122 ng with the function of elongation factor G (EF-G).

123 ycling factor (RRF) and elongation factor G (EF-G).

124 e ribosome catalyzed by elongation factor G (EF-G).

125 omain rearrangements of elongation factor G (EF-G).

126 eaction is catalyzed by elongation factor-G (EF-G) and is associated with ribosome-dependent hydrolys

127 ycling factor (RRF) and elongation factor-G (EF-G) are jointly essential for recycling bacterial ribo

128 ycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC

129 biotic thiostrepton and elongation factor-G (EF-G) rigorously localized the binding cleft of thiostre

130 ylococcus aureus, locks elongation factor-G (EF-G) to the ribosome after GTP hydrolysis.

131 ind to the drug target (Elongation factor G [EF-G]) and promote dissociation of EF-G from FA-stalled

132 n) can occur in the absence of EF-G and GTP, EF-G is essential for enforcing coupled movement of the

133 ns III and V have structural counterparts in EF-G and LepA.

134 lts suggest that the SRL is more critical in EF-G than ternary complex binding to the ribosome implic

135 ryptophan at position 127 in the G domain in EF-G and either one of two 5-iodouridine nucleotides in

136 shed light on the role of these elements in EF-G function.

137 tains a C-terminal domain (CTD) not found in EF-G that has a previously unobserved protein fold.

138 also for triggering interdomain movements in EF-G essential for its function, explaining functional d

139 our structural model, all known mutations in EF-G and RRF that relate to ribosome recycling have been

140 V in LepA differs from their orientations in EF-G.

141 Importantly, cleavage of SRL inhibited EF-G binding, and consequently GTP hydrolysis and mRNA-t

142 tion of any of these 16S rRNA bases inhibits EF-G-dependent translocation.

143 ructures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with beta,gamma-imidoguanosine 5'

144 tion of futile EF-G and thus causes multiple EF-G driven translocation attempts.

145 30S head domain) can occur in the absence of EF-G and GTP, EF-G is essential for enforcing coupled mo

146 ate translocation in vitro in the absence of EF-G and GTP.

147 mRNA and two tRNAs, formed in the absence of EF-G or GTP, provides insight into the respective roles

148 ubunit rotational movement in the absence of EF-G, fluctuating between two conformations correspondin

149 n interaction is disrupted in the absence of EF-G, resulting in slippage of the translational reading

150 agents promotes this event in the absence of EF-G.

151 ing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling st

152 Addition of EF-G to the ribosome-RRF complex induces rapid RRF disso

153 ion (k(trans)), and the apparent affinity of EF-G for the pretranslocation complex (i.e., increases K

154 he ribosomal ratchet motion, with the aid of EF-G, drives tRNA translocation.

155 in this model and a comparative analysis of EF-G structures in various nucleotide- and ribosome-boun

156 hibition while inducing a closer approach of EF-G to the GAC than is seen during normal turnover.

157 ibition is to abrogate the stable binding of EF-G and EF4 to the 70S ribosome.

158 attributed to neither the initial binding of EF-G nor the subsequent GTP hydrolysis step.

159 We demonstrate that binding of EF-G shifts the equilibrium toward the ratcheted state.

160 plexes, we have proposed that the binding of EF-G to an RRF-containing posttermination ribosome trigg

161 Furthermore, binding of EF-G to the PoTC.RRF complex reverts the ribosome from r

162 Binding of EF-G to the ribosome in the presence of the non-hydrolyz

163 the P-site tRNA suggest that the binding of EF-G would trigger the removal of deacylated tRNA from t

164 weed antiviral protein and on the binding of EF-G*GTP were assessed.

165 ed thiostrepton slows the initial binding of EF-G, and prevents both formation of the more stable EF-

166 nal change in the SRD that favors binding of EF-G.

167 To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue nea

168 ist for essentially only one conformation of EF-G in complex with the ribosome.

169 observe a previously unseen conformation of EF-G in the pretranslocation complex, which is independe

170 ted, translocation-competent conformation of EF-G while GTP hydrolysis triggers EF-G release from the

171 factor G [EF-G]) and promote dissociation of EF-G from FA-stalled ribosome complexes.

172 rgy transfer (FRET) between the G' domain of EF-G and the N-terminal domain of ribosomal protein L11

173 cid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with thr

174 bosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that

175 y interaction with the C-terminal domains of EF-G.

176 omain may be triggered by various domains of EF-G.

177 However, the structural dynamics of EF-G bound to the ribosome have not yet been described d

178 by affecting the conformational dynamics of EF-G on the ribosome.

179 changes in the conformational flexibility of EF-G in response to FusB binding and show that these cha

180 structure and conformational flexibility of EF-G, but which of these changes drives FA resistance wa

181 SRL to the supposedly catalytic histidine of EF-G (His87), we probed this interaction by an atomic mu

182 f domain IV of EF-G relative to domain II of EF-G using ensemble and single-molecule Forster resonanc

183 ed by a larger rotation within domain III of EF-G before its dissociation from the ribosome.

184 We find that the central domain III of EF-G is highly dynamic and does not fold upon emerging f

185 cant change in the dynamics of domain III of EF-G(C3) that leads to an increase in a minor, more diso

186 d a kinetic model for viomycin inhibition of EF-G catalyzed translocation, allowing for testable pred

187 t FA functions rather as a slow inhibitor of EF-G.GTPase, permitting a number of GTPase turnovers pri

188 The interaction of EF-G with ribosomal elements implicated in stimulating c

189 us structural analysis of the interaction of EF-G with the ribosome used either model complexes conta

190 g process, domain II of RRF and domain IV of EF-G adopt hitherto unknown conformations.

191 etween the observed movement of domain IV of EF-G and GTP hydrolysis.

192 tream ap/P-tRNA is contacted by domain IV of EF-G and P-site elements within the 30S subunit body, wh

193 Domain IV of EF-G is positioned in the cleft between the body and hea

194 , upon ribosomal translocation, domain IV of EF-G moves toward the A site of the small ribosomal subu

195 ndings suggest a model in which domain IV of EF-G promotes the translocation of tRNA from the A to th

196 Here, we follow the movement of domain IV of EF-G relative to domain II of EF-G using ensemble and si

197 talk and the L11 region, and of domain IV of EF-G with the tRNA at the peptidyl-tRNA binding site (P

198 Here, we follow the movement of domain IV of EF-G, which is critical for the catalysis of translocati

199 Here, we report the rotational motions of EF-G domains during normal translocation detected by sin

200 ecedes P(i) release, paralleling movement of EF-G following its binding to the ribosome, and in both

201 y EF-G, translates a large-scale movement of EF-G's domain IV, induced by GTP hydrolysis, into the do

202 The physiological role of LepA, a paralog of EF-G found in all bacteria, has been a mystery for decad

203 LepA is a paralog of EF-G found in all bacteria.

204 ism on the folding of the C-terminal part of EF-G.

205 sed states, respectively, in the presence of EF-G before translocation, in contrast with DeltaSL-prog

206 conditions, including 1), in the presence of EF-G; 2), spontaneously; 3), in different buffers, and 4

207 Hence, the structural rearrangement of EF-G makes a considerable energetic contribution to prom

208 cus on the distance between the G' region of EF-G and the N-terminal region of L11 (L11-NTD), located

209 formational change in the Switch I region of EF-G, suggesting that a conformational signal transducti

210 translocation (III), just before release of EF-G from the post-translocation ribosome.

211 within EF-G by which FA prevents release of EF-G from the ribosome.

212 rovides insight into the respective roles of EF-G and the ribosome in translocation.

213 ncrease in a minor, more disordered state of EF-G domain III.

214 Although the high-resolution structure of EF-G bound to the posttranslocation ribosome has been de

215 tified by alignment of crystal structures of EF-G bound and EF-G unbound ribosomal subunits.

216 four atomic-resolution crystal structures of EF-G bound to the ribosome programmed in the pre- and po

217 strom resolution x-ray crystal structures of EF-G complexed with a nonhydrolyzable guanosine 5'-triph

218 Structures of EF-G on the ribosome have been visualized at various int

219 anslocation and to prolong the dwell time of EF-G on the ribosome.

220 e MMB-GUI to create a possible trajectory of EF-G mediated gate-passing translocation in the ribosome

221 is facilitated by a structural transition of EF-G from a compact to an elongated conformation, which

222 mpatible with efficient GTPase activation on EF-G.

223 says to study the effects of thiostrepton on EF-G and a newly described translation factor, elongatio

224 aging from multiple structural perspectives, EF-G is shown to accelerate structural and kinetic pathw

225 Thus, FA-resistant EF-G mutations causing fitness loss and compensation ope

226 In contrast, the complexes of ribosome, EF-G and thiostrepton could bind RRF, although with lowe

227 upon binding to a pretranslocation ribosome, EF-G moves from a compact to a more extended conformatio

228 n a manner that interferes with the ribosome-EF-G interaction.

229 state, indicating that it traps the ribosome.EF-G complex in a preexisting conformation formed during

230 nt centrifugation (SDGC) without IF3 if RRF, EF-G and GTP were present in the SDGC buffer.

231 amount of 70S ribosomes increased, more RRF, EF-G and GTP were necessary to split 70S ribosomes.

232 Overlapping binding sites of RRF, EF-G, and the P-site tRNA suggest that the binding of EF

233 The bacterial RRF/EF-G pair was previously known to target only the post-t

234 We found that although HflX and the RRF/EF-G pair are functionally interchangeable, HflX is expr

235 nti-association activity of IF3, and the RRF/EF-G/GTP-dependent splitting of 70S ribosomes.

236 inal domain of L11 is necessary to stabilize EF-G binding in the post-translocation state, and thiost

237 d prevents both formation of the more stable EF-G complex and EF-G-induced RRF dissociation.

238 Purified FusB bound staphylococcal EF-G, the target of fusidic acid.

239 rganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the

240 in from a natural mRNA template, and support EF-G-dependent translocation at wild-type rates.

241 acid resistance protein and the drug target (EF-G) it acts to protect.

242 FA targets EF-G at an early stage in the translocation process (I),

243 Collectively, our data demonstrate that EF-G and the L1 stalk allosterically collaborate to dire

244 lts provide primary, real-time evidence that EF-G induces direct or indirect structural changes in th

245 The structures reveal that EF-G binding to the ribosome stabilizes switch regions i

246 Our study shows that EF-G has a small ( approximately 10 degrees ) global rot

247 insights into the conformational space that EF-G samples on the ribosome and reveal that tRNA transl

248 These structures suggest that EF-G controls the translocation reaction by cycles of co

249 other translocation modulators suggest that EF-G-dependent GTP hydrolysis is more important for INT

250 complexes with fusidic acid, suggesting that EF-G stabilized by fusidic acid does not represent the n

251 Despite numerous studies suggesting that EF-G undergoes extensive conformational rearrangements d

252 The EF-G-bound ribosome remains highly dynamic in nature, wh

253 The EF-G-dependent release occurs in the presence of fusidic

254 the most significant difference between the EF-G.GTPase activities of vacant and translocating ribos

255 ameshift promoting signals mostly impair the EF-G-catalyzed translocation step of the two tRNALys and

256 the same orientation, while domain II in the EF-G-containing 50S subunit is extensively rotated (appr

257 pery sequence also helps dissociation of the EF-G by providing alternative base-pairing options.

258 formational transitions that are part of the EF-G functional cycle during ribosome translocation.

259 hat the pretranslocation conformation of the EF-G-ribosome complex is significantly less stable than

260 ce that the SRD is in close proximity to the EF-G catalytic center.

261 On the other hand, RRF did not bind to EF-G-ribosome complexes with fusidic acid, suggesting th

262 By binding to EF-G on the ribosome, FusB-type proteins promote the dis

263 with a tRNA in the hybrid P/E state bound to EF-G with a GTP analog.

264 Binding of FusB to EF-G causes a significant change in the dynamics of doma

265 Binding of FusB to EF-G induces conformational and dynamic changes in the l

266 cture influence coupling of tRNA movement to EF-G.GTP-induced conformational changes.

267 er of the 50S subunit in a manner similar to EF-G and EF-Tu.

268 , EF4 showed chemical protections similar to EF-G and stabilized a ratcheted state of the 70S ribosom

269 ough structurally similar to the translocase EF-G, promotes back-translocation of tRNAs on the riboso

270 uite similar structurally to the translocase EF-G.

271 nd to the ribosome and induce translocation, EF-G*GDP in complex with phosphate group analogs BeF3(-)

272 Fusidic acid traps EF-G in a conformation intermediate between the guanosin

273 mation of EF-G while GTP hydrolysis triggers EF-G release from the ribosome.

274 t bacterial trGTPases, including IF2, EF-Tu, EF-G and RF3, play well-known roles in translation.

275 actor subfamily of GTPases, including EF-Tu, EF-G, and LepA.

276 on of plastid-encoded proteins (e.g., EF-Tu, EF-G, and mRNA binding proteins) and thylakoid formation

277 fusidic acid (FA) inhibits multiple-turnover EF-G.GTPase.

278 examine such changes during single-turnover EF-G-dependent GTPase on vacant ribosomes and to elucida

279 with the mRNA stimulatory elements uncouple EF-G catalysed translocation from normal ribosomal subun

280 Upon EF-G binding, both RRF and tRNA are driven towards the t

281 e mutant ribosomes were affected in in vitro EF-G-dependent GTP hydrolysis but all showed resistance

282 When EF-G-GTP is bound to 70S ribosomes, bases A1492 and A149

283 from the POST to PRE state is observed when EF-G is depleted from ribosomes in the POST state or whe

284 NA or only a single tRNA, or complexes where EF-G was directly bound to ribosomes in the posttransloc

285 Here, we show that while EF-G*GDP does not stably bind to the ribosome and induce

286 nslation factor family of GTPases along with EF-G and LepA.

287 somal conformational changes associated with EF-G dissociation upon unsuccessful translocation attemp

288 ng the coordinated movements associated with EF-G-driven GTP hydrolysis.

289 tion conformation of the ribosome bound with EF-G and A-site tRNA has evaded visualization owing to t

290 ts, we demonstrate that EF4 can compete with EF-G for binding to the PRE complex.

291 mus thermophilus 70S ribosome complexed with EF-G, RRF and two transfer RNAs at a resolution of 3.5 a

292 le for thiostrepton to compete directly with EF-G.GDP for binding to the L11-RNA complex, and provide

293 n the A/P and P/E states, respectively, with EF-G.GTP causes reversal of the FRET changes.

294 rmine the structure of the 70S ribosome with EF-G, which is trapped in the pretranslocation state usi

295 c) each bind to two sites per ribosome, with EF-G having considerably higher second-site affinity tha

296 Although sequence similarity with EF-G suggests Snu114p functions as a molecular motor, ou

297 trom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiot

298 ransmission of conformational changes within EF-G by which FA prevents release of EF-G from the ribos

299 es of the PoTC.RRF complex, with and without EF-G.

300 0.5) cryo-electron microscopy map of a 50S x EF-G x guanosine 5'-[(betagamma)-imido]triphosphate x RR