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1                                              EF-G and the cryo-EM density map at 17 A resolution.
2                                              EF-G binds to the ribosome in a GTP-bound form and subse
3                                              EF-G catalyzes translocation of mRNA and tRNAs within th
4                                              EF-G dependent translocation from the classical PRE comp
5                                              EF-G rearrangement would then provide directional contro
6                                              EF-G.GTP binding to the pretranslocation (PRE) complex a
7 ctors along with elongation factors G and 4 (EF-G and EF4).
8 ed phosphatase and kinase activities against EF-G in vitro.
9                 In support of this model, an EF-G truncation variant that does not possess domains IV
10 uggest that the SRL is crucial for anchoring EF-G on the ribosome during mRNA-tRNA translocation.
11 ment of crystal structures of EF-G bound and EF-G unbound ribosomal subunits.
12 -ray coordinates of L11-23 S RNA complex and EF-G into the cryo-EM maps combined with molecular model
13 ormation of the more stable EF-G complex and EF-G-induced RRF dissociation.
14  bacteria (known as eEF1A in eukaryotes) and EF-G (eEF2), which deliver aminoacyl-tRNAs to the riboso
15 lyzed by RRF (ribosome recycling factor) and EF-G (elongation factor G).
16  high structural similarity between LepA and EF-G enabled us to derive a homology model for LepA boun
17 degree of sequence identity between LepA and EF-G is reflected in the structural similarity between t
18 he individual homologous domains of LepA and EF-G.
19 ated tRNAs are bound to the 70S ribosome and EF-G-GTP is added, bases A1492 and A1493 again show subs
20 undance of FusB-type protein, ribosomes, and EF-G.
21                                      RRF and EF-G (a) each form a binary complex on binding to a bare
22 NA, is accompanied by the release of RRF and EF-G from the ribosome.
23 eme that accounts quantitatively for RRF and EF-G interaction on the Escherichia coli ribosome.
24 into subunits by the joint action of RRF and EF-G.
25 or the splitting of 70S ribosomes by RRF and EF-G/GTP during the lag phase for activation of ribosome
26 ng and accommodation to the empty A site and EF-G action either leads to the slippage of the tRNAs in
27 m of deacylated tRNA into the 50S E site and EF-G binding to the ribosome both contribute to stabiliz
28 not critical for GTP hydrolysis on EF-Tu and EF-G.
29  located near the binding site for EF-Tu and EF-G.
30 ase factors elongation factor Tu (EF-Tu) and EF-G.
31  depends on competition between viomycin and EF-G for binding to the pretranslocation ribosome, and t
32                                     When apo-EF-G is bound to 70S ribosomes and GTP is added, substan
33 ndirect structural changes in this region as EF-G is bound and as GTP is hydrolyzed.
34 tance, we have characterized three S. aureus EF-G mutants with fast kinetics and crystal structures.
35 7.3-A cryo-EM structure of a complex between EF-G and the 70S ribosome.
36 the precise identity of the contacts between EF-G and ribosome components.
37 ved from it, showing the interaction between EF-G and RRF on the 50S subunit in the presence of the n
38  formed, by ultraviolet irradiation, between EF-G and a sarcin/ricin domain (SRD) oligoribonucleotide
39  a loss of the capacity of ribosomes to bind EF-G and by indirection the EF-Tu ternary complex.
40 pendent GTP hydrolysis is inhibited for both EF-G and EF4, with IC(50) values equivalent to the 70S r
41 e in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conf
42 arious functional states, and show that both EF-G binding and subsequent GTP hydrolysis lead to ratch
43 x and one of the 50S subunit bound with both EF-G and RRF.
44 GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labele
45                  We show that ribosome-bound EF-G adopts distinct conformations corresponding to the
46         Our data suggest that ribosome-bound EF-G may also occasionally sample at least one more comp
47                  By contrast, ribosome-bound EF-G predominantly adopts an extended conformation regar
48 s studies have suggested that ribosome-bound EF-G undergoes significant structural rearrangements.
49  not increase the lability of ribosome-bound EF-G.
50 rmations in ribosome-free and ribosome-bound EF-G.
51 nd tRNAs within the ribosome is catalyzed by EF-G binding and GTP hydrolysis.
52                  GTP hydrolysis catalyzed by EF-G does not affect the relative stability of the obser
53 of the ribosome-stimulated GTP hydrolysis by EF-G to tRNA/mRNA translocation remains debated.
54  promotes futile cycles of GTP hydrolysis by EF-G.
55 , the rates of mRNA translocation induced by EF-G in the presence of GTP and a non-hydrolyzable analo
56                          Energy liberated by EF-G's GTPase activity is necessary for EF-G to catalyze
57 ransfer RNA translocation on the ribosome by EF-G, translates a large-scale movement of EF-G's domain
58 se that the release of ribosome-bound RRF by EF-G is required for post-termination complex disassembl
59                  The release of bound RRF by EF-G is stimulated by GTP analogues.
60           Cryo-EM reconstructions of certain EF-G-containing complexes led to the proposal that the m
61 the observed failure of FusB to bind E. coli EF-G, and its inability to confer resistance in E. coli.
62 e GTPase active site, resulting in a compact EF-G conformation that favors an intermediate state of r
63 onance energy transfer (smFRET) between (Cy5)EF-G and (Cy3)tRNALys, we studied the translational elon
64 rate that single-turnover ribosome-dependent EF-G GTPase proceeds according to a kinetic scheme in wh
65 idyl-tRNA in the small subunit P site during EF-G-catalyzed translocation.
66 to the A-site of the ribosome, whereas eEF2 (EF-G in bacteria) translocates the ribosome along the mR
67 l of translocation that begins with the eEF2/EF-G binding-induced ratcheting motion of the small ribo
68                     A-site binding of either EF-G to the PRE complex or of aminoacyl-tRNAEF-Tu ternar
69    In every round of translation elongation, EF-G catalyzes translocation, the movement of tRNAs (and
70 of an elongation factor (eEF2 in eukaryotes, EF-G in bacteria).
71                            Elongation factor EF-G (fusA [mhp083]) (P = 0.002), RNA polymerase beta ch
72 acterial post-TCs requires elongation factor EF-G and a ribosome recycling factor RRF.
73 ral rearrangements in both elongation factor EF-G and the ribosome occur during tRNA translocation.
74 me, a process catalyzed by elongation factor EF-G, is a crucial step in protein synthesis.
75 plexes in conjunction with elongation factor EF-G, liberating ribosomes for further rounds of transla
76 xchange within translation elongation factor EF-G.
77 ant sequence similarity to elongation factor EF-G.
78 uence and structure to the elongation factor EF-G.
79             The essential translation factor EF-G is an in vivo substrate of PrkC and this phosphoryl
80 y a universally conserved elongation factor (EF-G in prokaryotes and EF-2 in eukaryotes).
81 ical/open state and toward states that favor EF-G dissociation apparently allows the PRE complex to e
82 rast, fusidic acid and a GTP analog that fix EF-G to the ribosome, allowing one round of tRNA translo
83  molecular modeling, reveals that, following EF-G-dependent GTP hydrolysis, domain V of EF-G intrudes
84 intact aminoacyl tRNAs as substrates and for EF-G catalyzed translocation.
85   These results suggest a novel function for EF-G and RRF in the post-stress return of PSRP1/pY-inact
86 n and suggests a common GTPase mechanism for EF-G and elongation factor Tu.
87 d by EF-G's GTPase activity is necessary for EF-G to catalyze rapid and precise translocation.
88 other hand, the affinity of the ribosome for EF-G*GTP is increased when peptidyl-tRNA is in the A-sit
89  increased the maximal rate of both forward (EF-G dependent) and reverse (spontaneous) translocation.
90 movements of the tRNAs and mRNA or to foster EF-G dissociation from the ribosome after translocation
91                                         Free EF-G, not bound to the ribosome, adopts quite different
92      Our results indicate that ribosome-free EF-G predominantly adopts a compact conformation that ca
93  the hairpin promotes dissociation of futile EF-G and thus causes multiple EF-G driven translocation
94 recycling factor (RRF), elongation factor G (EF-G) and GTP split 70S ribosomes into subunits.
95 a reaction catalyzed by elongation factor G (EF-G) and guanosine triphosphate (GTP).
96 sidic acid (FA) targets elongation factor G (EF-G) and inhibits ribosomal peptide elongation and ribo
97                         Elongation factor G (EF-G) and ribosome recycling factor (RRF) disassemble po
98 etween the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal s
99 peptide-bond formation, elongation factor G (EF-G) binds to the ribosome, triggering the translocatio
100  of G proteins, such as elongation factor G (EF-G) bound to the ribosome, as well as many biochemical
101 n synthesis by blocking elongation factor G (EF-G) catalyzed translocation of messenger RNA on the ri
102 triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent movement of mRNA and tRNA
103 rsally conserved GTPase elongation factor G (EF-G) catalyzes the translocation of tRNA and mRNA on th
104 tor (RRF) together with elongation factor G (EF-G) disassembles the post- termination ribosomal compl
105 ribosome is promoted by elongation factor G (EF-G) during the translation cycle.
106 ycling factor (RRF) and elongation factor G (EF-G) in a guanosine 5'-triphosphate (GTP)-hydrolysis-de
107 osome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation factor 2 (EF-2) in e
108 ing from the binding of elongation factor G (EF-G) in various forms.
109 tion factor 2 (IF2) and elongation factor G (EF-G) induce similar changes in ribosome structure.
110                         Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays
111                         Elongation factor G (EF-G) is a universally conserved translational GTPase th
112              Binding of elongation factor G (EF-G) shifts this equilibrium toward the closed conforma
113 ocation, the binding of elongation factor G (EF-G) to the pretranslocational ribosome leads to a ratc
114                         Elongation factor G (EF-G) was identified as one possible target of the PrpC
115 ntrast, the activity of elongation factor G (EF-G) was strongly impaired in alpha-sarcin-treated ribo
116 n factor Tu (EF-Tu) and elongation factor G (EF-G) with the ribosome during protein synthesis were un
117 otic protein synthesis, elongation factor G (EF-G), a guanosine triphosphatase (GTPase), binds to the
118 recycling factor (RRF), elongation factor G (EF-G), and GTP to prepare the ribosome for a fresh round
119 or (RRF), together with elongation factor G (EF-G), disassembles this posttermination complex into mR
120  These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translation from FA-
121  a proper substrate for elongation factor G (EF-G), thus inhibiting translocation until the E-site tR
122 ed significantly slower elongation factor G (EF-G)-catalyzed translocation through the slippery seque
123 onstructions of certain elongation factor G (EF-G)-containing complexes have led to the proposal that
124 n factor Tu (EF-Tu) and elongation factor G (EF-G).
125 ng with the function of elongation factor G (EF-G).
126 ycling factor (RRF) and elongation factor G (EF-G).
127 e ribosome catalyzed by elongation factor G (EF-G).
128 omain rearrangements of elongation factor G (EF-G).
129 triphosphatase (GTPase) elongation factor G (EF-G).
130 complex and catalyzed by elongtion factor G (EF-G).
131 eaction is catalyzed by elongation factor-G (EF-G) and is associated with ribosome-dependent hydrolys
132 ycling factor (RRF) and elongation factor-G (EF-G) are jointly essential for recycling bacterial ribo
133 ycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC
134 biotic thiostrepton and elongation factor-G (EF-G) rigorously localized the binding cleft of thiostre
135 ylococcus aureus, locks elongation factor-G (EF-G) to the ribosome after GTP hydrolysis.
136 270A site in EF-Tu with sequence homologues, EF-G and EF-1alpha, suggests steric clashes that would p
137 ns III and V have structural counterparts in EF-G and LepA.
138 lts suggest that the SRL is more critical in EF-G than ternary complex binding to the ribosome implic
139 ryptophan at position 127 in the G domain in EF-G and either one of two 5-iodouridine nucleotides in
140  shed light on the role of these elements in EF-G function.
141 tains a C-terminal domain (CTD) not found in EF-G that has a previously unobserved protein fold.
142 also for triggering interdomain movements in EF-G essential for its function, explaining functional d
143 our structural model, all known mutations in EF-G and RRF that relate to ribosome recycling have been
144 V in LepA differs from their orientations in EF-G.
145       Importantly, cleavage of SRL inhibited EF-G binding, and consequently GTP hydrolysis and mRNA-t
146 tion of any of these 16S rRNA bases inhibits EF-G-dependent translocation.
147 change on the 70S ribosome, mainly involving EF-G's domains III, IV, and V.
148 ructures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with beta,gamma-imidoguanosine 5'
149 tion of futile EF-G and thus causes multiple EF-G driven translocation attempts.
150 ate translocation in vitro in the absence of EF-G and GTP.
151 ubunit rotational movement in the absence of EF-G, fluctuating between two conformations correspondin
152 agents promotes this event in the absence of EF-G.
153 ing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling st
154                                  Addition of EF-G to the ribosome-RRF complex induces rapid RRF disso
155 ion (k(trans)), and the apparent affinity of EF-G for the pretranslocation complex (i.e., increases K
156 he ribosomal ratchet motion, with the aid of EF-G, drives tRNA translocation.
157  in this model and a comparative analysis of EF-G structures in various nucleotide- and ribosome-boun
158 hibition while inducing a closer approach of EF-G to the GAC than is seen during normal turnover.
159 ibition is to abrogate the stable binding of EF-G and EF4 to the 70S ribosome.
160 attributed to neither the initial binding of EF-G nor the subsequent GTP hydrolysis step.
161               We demonstrate that binding of EF-G shifts the equilibrium toward the ratcheted state.
162 plexes, we have proposed that the binding of EF-G to an RRF-containing posttermination ribosome trigg
163 logs of C2658 and G2663 decreased binding of EF-G to SRD oligoribonucleotides; the same mutations in
164                      Furthermore, binding of EF-G to the PoTC.RRF complex reverts the ribosome from r
165                                   Binding of EF-G to the ribosome in the presence of the non-hydrolyz
166  the P-site tRNA suggest that the binding of EF-G would trigger the removal of deacylated tRNA from t
167 weed antiviral protein and on the binding of EF-G*GTP were assessed.
168 ed thiostrepton slows the initial binding of EF-G, and prevents both formation of the more stable EF-
169  in protein synthesis, and in the binding of EF-G, was associated with a C2658G x G2663C mutation; it
170 nal change in the SRD that favors binding of EF-G.
171                 To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue nea
172 ist for essentially only one conformation of EF-G in complex with the ribosome.
173  observe a previously unseen conformation of EF-G in the pretranslocation complex, which is independe
174 ted, translocation-competent conformation of EF-G while GTP hydrolysis triggers EF-G release from the
175 rgy transfer (FRET) between the G' domain of EF-G and the N-terminal domain of ribosomal protein L11
176 cid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with thr
177 bosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that
178 he arc-like connection with the G' domain of EF-G.
179 y interaction with the C-terminal domains of EF-G.
180 omain may be triggered by various domains of EF-G.
181          However, the structural dynamics of EF-G bound to the ribosome have not yet been described d
182  by affecting the conformational dynamics of EF-G on the ribosome.
183 SRL to the supposedly catalytic histidine of EF-G (His87), we probed this interaction by an atomic mu
184 f domain IV of EF-G relative to domain II of EF-G using ensemble and single-molecule Forster resonanc
185 ed by a larger rotation within domain III of EF-G before its dissociation from the ribosome.
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  provide a new insight into the mechanism of EF-G-dependent translocation.
200    Here, we report the rotational motions of EF-G domains during normal translocation detected by sin
201 ecedes P(i) release, paralleling movement of EF-G following its binding to the ribosome, and in both
202 y EF-G, translates a large-scale movement of EF-G's domain IV, induced by GTP hydrolysis, into the do
203                                   Mutants of EF-G that are impaired for translocation fail to disasse
204 The physiological role of LepA, a paralog of EF-G found in all bacteria, has been a mystery for decad
205                         LepA is a paralog of EF-G found in all bacteria.
206 sed states, respectively, in the presence of EF-G before translocation, in contrast with DeltaSL-prog
207 conditions, including 1), in the presence of EF-G; 2), spontaneously; 3), in different buffers, and 4
208       Hence, the structural rearrangement of EF-G makes a considerable energetic contribution to prom
209                         The rearrangement of EF-G's structurally preserved regions, mediated and guid
210 cus on the distance between the G' region of EF-G and the N-terminal region of L11 (L11-NTD), located
211 formational change in the Switch I region of EF-G, suggesting that a conformational signal transducti
212  translocation (III), just before release of EF-G from the post-translocation ribosome.
213    Although the high-resolution structure of EF-G bound to the posttranslocation ribosome has been de
214 tified by alignment of crystal structures of EF-G bound and EF-G unbound ribosomal subunits.
215 four atomic-resolution crystal structures of EF-G bound to the ribosome programmed in the pre- and po
216 strom resolution x-ray crystal structures of EF-G complexed with a nonhydrolyzable guanosine 5'-triph
217                                Structures of EF-G on the ribosome have been visualized at various int
218 anslocation and to prolong the dwell time of EF-G on the ribosome.
219 e MMB-GUI to create a possible trajectory of EF-G mediated gate-passing translocation in the ribosome
220 is facilitated by a structural transition of EF-G from a compact to an elongated conformation, which
221 g EF-G-dependent GTP hydrolysis, domain V of EF-G intrudes into the cleft between the 23 S ribosomal
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 nti-association activity of IF3, and the RRF/EF-G/GTP-dependent splitting of 70S ribosomes.
234 inal domain of L11 is necessary to stabilize EF-G binding in the post-translocation state, and thiost
235 d prevents both formation of the more stable EF-G complex and EF-G-induced RRF dissociation.
236           Purified FusB bound staphylococcal EF-G, the target of fusidic acid.
237 rganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the
238 in from a natural mRNA template, and support EF-G-dependent translocation at wild-type rates.
239 acid resistance protein and the drug target (EF-G) it acts to protect.
240                                   FA targets EF-G at an early stage in the translocation process (I),
241      Collectively, our data demonstrate that EF-G and the L1 stalk allosterically collaborate to dire
242 lts provide primary, real-time evidence that EF-G induces direct or indirect structural changes in th
243                   The structures reveal that EF-G binding to the ribosome stabilizes switch regions i
244                           Here, we show that EF-G releases RRF from 70 S ribosomal and model post-ter
245                         Our study shows that EF-G has a small ( approximately 10 degrees ) global rot
246  insights into the conformational space that EF-G samples on the ribosome and reveal that tRNA transl
247                These structures suggest that EF-G controls the translocation reaction by cycles of co
248  other translocation modulators suggest that EF-G-dependent GTP hydrolysis is more important for INT
249 P with much weaker affinity, suggesting that EF-G may move RRF to this position during the release of
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 hat the pretranslocation conformation of the EF-G-ribosome complex is significantly less stable than
259 ce that the SRD is in close proximity to the EF-G catalytic center.
260                     RRF was shown to bind to EF-G-ribosome complexes in the presence of GTP with much
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 induces conformational and dynamic changes in the l
265 cture influence coupling of tRNA movement to EF-G.GTP-induced conformational changes.
266 on, similar in shape and binding position to EF-G.
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 ined to refine the structure of translocase (EF-G) in the ribosome-bound form against data from cryoe
272 nd to the ribosome and induce translocation, EF-G*GDP in complex with phosphate group analogs BeF3(-)
273                           Fusidic acid traps EF-G in a conformation intermediate between the guanosin
274 mation of EF-G while GTP hydrolysis triggers EF-G release from the ribosome.
275 t bacterial trGTPases, including IF2, EF-Tu, EF-G and RF3, play well-known roles in translation.
276 actor subfamily of GTPases, including EF-Tu, EF-G, and LepA.
277 on of plastid-encoded proteins (e.g., EF-Tu, EF-G, and mRNA binding proteins) and thylakoid formation
278 fusidic acid (FA) inhibits multiple-turnover EF-G.GTPase.
279  examine such changes during single-turnover EF-G-dependent GTPase on vacant ribosomes and to elucida
280  with the mRNA stimulatory elements uncouple EF-G catalysed translocation from normal ribosomal subun
281                                         Upon EF-G binding, both RRF and tRNA are driven towards the t
282 e mutant ribosomes were affected in in vitro EF-G-dependent GTP hydrolysis but all showed resistance
283                                         When EF-G-GTP is bound to 70S ribosomes, bases A1492 and A149
284  from the POST to PRE state is observed when EF-G is depleted from ribosomes in the POST state or whe
285 NA or only a single tRNA, or complexes where EF-G was directly bound to ribosomes in the posttransloc
286                     Here, we show that while EF-G*GDP does not stably bind to the ribosome and induce
287 nslation factor family of GTPases along with EF-G and LepA.
288 somal conformational changes associated with EF-G dissociation upon unsuccessful translocation attemp
289 ng the coordinated movements associated with EF-G-driven GTP hydrolysis.
290 tion conformation of the ribosome bound with EF-G and A-site tRNA has evaded visualization owing to t
291 ts, we demonstrate that EF4 can compete with EF-G for binding to the PRE complex.
292 le for thiostrepton to compete directly with EF-G.GDP for binding to the L11-RNA complex, and provide
293  mRNA release but partially takes place with EF-G alone.
294 n the A/P and P/E states, respectively, with EF-G.GTP causes reversal of the FRET changes.
295 rmine the structure of the 70S ribosome with EF-G, which is trapped in the pretranslocation state usi
296 c) each bind to two sites per ribosome, with EF-G having considerably higher second-site affinity tha
297            Although sequence similarity with EF-G suggests Snu114p functions as a molecular motor, ou
298 trom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiot
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

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