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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
10 uggest that the SRL is crucial for anchoring EF-G on the ribosome during mRNA-tRNA translocation.
12 -ray coordinates of L11-23 S RNA complex and EF-G into the cryo-EM maps combined with molecular model
14 bacteria (known as eEF1A in eukaryotes) and EF-G (eEF2), which deliver aminoacyl-tRNAs to the riboso
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
19 ated tRNAs are bound to the 70S ribosome and EF-G-GTP is added, bases A1492 and A1493 again show subs
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
31 depends on competition between viomycin and EF-G for binding to the pretranslocation ribosome, and t
34 tance, we have characterized three S. aureus EF-G mutants with fast kinetics and crystal structures.
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
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
44 GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labele
48 s studies have suggested that ribosome-bound EF-G undergoes significant structural rearrangements.
55 , the rates of mRNA translocation induced by EF-G in the presence of GTP and a non-hydrolyzable analo
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
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
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
69 In every round of translation elongation, EF-G catalyzes translocation, the movement of tRNAs (and
73 ral rearrangements in both elongation factor EF-G and the ribosome occur during tRNA translocation.
75 plexes in conjunction with elongation factor EF-G, liberating ribosomes for further rounds of transla
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
85 These results suggest a novel function for EF-G and RRF in the post-stress return of PSRP1/pY-inact
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
93 the hairpin promotes dissociation of futile EF-G and thus causes multiple EF-G driven translocation
96 sidic acid (FA) targets elongation factor G (EF-G) and inhibits ribosomal peptide elongation and ribo
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
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
109 tion factor 2 (IF2) and elongation factor G (EF-G) induce similar changes in ribosome structure.
113 ocation, the binding of elongation factor G (EF-G) to the pretranslocational ribosome leads to a ratc
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
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
136 270A site in EF-Tu with sequence homologues, EF-G and EF-1alpha, suggests steric clashes that would p
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
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
148 ructures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with beta,gamma-imidoguanosine 5'
151 ubunit rotational movement in the absence of EF-G, fluctuating between two conformations correspondin
153 ing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling st
155 ion (k(trans)), and the apparent affinity of EF-G for the pretranslocation complex (i.e., increases K
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.
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
166 the P-site tRNA suggest that the binding of EF-G would trigger the removal of deacylated tRNA from t
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
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
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
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
189 us structural analysis of the interaction of EF-G with the ribosome used either model complexes conta
192 tream ap/P-tRNA is contacted by domain IV of EF-G and P-site elements within the 30S subunit body, wh
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
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
204 The physiological role of LepA, a paralog of EF-G found in all bacteria, has been a mystery for decad
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
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
213 Although the high-resolution structure of EF-G bound to the posttranslocation ribosome has been de
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
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
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
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
229 state, indicating that it traps the ribosome.EF-G complex in a preexisting conformation formed during
231 amount of 70S ribosomes increased, more RRF, EF-G and GTP were necessary to split 70S ribosomes.
234 inal domain of L11 is necessary to stabilize EF-G binding in the post-translocation state, and thiost
237 rganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the
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
246 insights into the conformational space that EF-G samples on the ribosome and reveal that tRNA transl
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
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
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
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(-)
275 t bacterial trGTPases, including IF2, EF-Tu, EF-G and RF3, play well-known roles in translation.
277 on of plastid-encoded proteins (e.g., EF-Tu, EF-G, and mRNA binding proteins) and thylakoid formation
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
282 e mutant ribosomes were affected in in vitro EF-G-dependent GTP hydrolysis but all showed resistance
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
288 somal conformational changes associated with EF-G dissociation upon unsuccessful translocation attemp
290 tion conformation of the ribosome bound with EF-G and A-site tRNA has evaded visualization owing to t
292 le for thiostrepton to compete directly with EF-G.GDP for binding to the L11-RNA complex, and provide
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
298 trom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiot
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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