ライフサイエンスコーパス: eIF4A

1 eIF4A bound to an adjacent region within each repeat, su

2 eIF4A can physically interact with BAM in Drosophila S2

3 eIF4A exhibits dosage-specific interactions with bam in

4 eIF4A has been thought to unwind structures formed in th

5 eIF4A is a DEAD-box RNA-dependent ATPase thought to unwi

6 eIF4A is a highly conserved RNA-stimulated ATPase and he

7 eIF4A is dissected into two fragments, and each fragment

8 eIF4A is part of the 5'-7-methylguanosine cap-binding co

9 eIF4A mutants exhibit increased Dpp signalling and accum

10 eIF4A participates in the initiation of translation by u

11 eIF4A/eIF4G stimulated initiation only at low temperatur

12 The formation of a 1:1 eIF4A-Pdcd4 complex in solution is consistent with the r

13 eukaryotic translation initiation factor 4A (eIF4A) activity and binding to translation initiation fa

14 eukaryotic translation initiation factor 4A (eIF4A) and Ded1 promote translation by resolving mRNA se

15 ors such as eukaryotic initiation factor 4A (eIF4A) and eIF4E (translation initiation factors), eEF1B

16 of the two eukaryotic initiation factor 4A (eIF4A) genes present in the nuclear genome.

17 stimulating eukaryotic initiation factor 4A (eIF4A) helicase activity.

18 The eukaryotic initiation factor 4A (eIF4A) is a DEAD box helicase that unwinds RNA structure

19 The eukaryotic translation factor 4A (eIF4A) is a member of DEA(D/H)-box RNA helicase family,

20 of that of eukaryotic initiation factor 4A (eIF4A) on double-stranded substrates.

21 ered by the eukaryotic initiation factor 4A (eIF4A), a DEAD-box helicase.

22 ocA targets eukaryotic initiation factor 4A (eIF4A), an ATP-dependent DEAD-box RNA helicase; its mess

23 activity of eukaryotic initiation factor 4A (eIF4A), an ATP-dependent RNA helicase, as a target of BC

24 own to bind eukaryotic initiation factor 4A (eIF4A), inhibit translation initiation, and act as a tum

25 t binds to translation initiation factor 4A (eIF4A), sufficiently inhibited Sin1 translation, and thu

26 eukaryotic translation initiation factor 4A (eIF4A), which mediates activation-dependent degradation

27 eukaryotic translation initiation factor 4A (eIF4A).

28 tein is the eukaryotic initiation factor 4A (eIF4A).

29 eukaryotic translation initiation factor 4A (eIF4A).

30 ukaryotic translation initiation factors 4A (eIF4A) and 4G (eIF4G) are crucial for the assembly of th

31 9K,D414K), and Pdcd4(D253A,D418A)) lost >90% eIF4A-binding activity.

32 Mutations that abolish eIF4A binding negate both functions of the cMA3.

33 s that in addition to its helicase activity, eIF4A uses the free energy of ATP binding and hydrolysis

34 -initiation caused by the mutations altering eIF4A-binding site.

35 Using hippuristanol, an eIF4A inhibitor, we find that translation of dINR UTR co

36 Here we report an eIF4A RNA helicase-dependent mechanism of translational

37 These findings reveal an eIF4A-independent role for eIF4B in addition to its func

38 t surface is adjacent to the RNA-, ATP-, and eIF4A-NTD-interacting regions.

39 RAN translation initiates through a cap- and eIF4A-dependent mechanism that utilizes a CUG start codo

40 cap with the 43S pre-initiation complex, and eIF4A, which is a helicase necessary for initiation.

41 ed p70s6K activation, PDCD4 is degraded, and eIF4A activity is greatly enhanced.

42 Together with eIF3 and eIF4A/4B, eIF4G recruits ribosomal subunits to mRNAs and

43 BP but not the interaction between eIF4B and eIF4A or eIFiso4G, demonstrating that the effect of zinc

44 This resistance to inhibition of eIF4E and eIF4A indicates a conserved strategy to allow translatio

45 se proteins, through inhibition of eIF4E and eIF4A, respectively, impair cap-dependent translation.

46 of the other cap-complex factors, eIF4E and eIF4A.

47 e yeast eIF4G2 mutations altering eIF4E- and eIF4A-binding sites increase re-initiation at GCN4 and i

48 F4A to type 1 IRESs, and together, eIF4G and eIF4A induce conformational changes at their 3' borders.

49 Studies with eIF4G and eIF4A variants suggest a model by which cp(C3) alters th

50 nning but does not absolutely need eIF4G and eIF4A: There was efficient reinitiation in a standard re

51 on factor 4F), composed of eIF4E, eIF4G, and eIF4A, binds to the m(7)G cap structure of mRNA and stim

52 Thus, Vhs, eIF4H, and eIF4A comprise a group of proteins, each of which is abl

53 interfering with translation initiation and eIF4A maintains self-renewal by inhibiting BAM function

54 yeast DEAD-box helicases Ded1p, Mss116p, and eIF4A.

55 binding to eIF4G (a scaffolding subunit) and eIF4A (an ATP-dependent RNA helicase) leads to assembly

56 the 7-repeats and NTD domains of yeIF4B and eIF4A in mRNA recruitment.

57 utant with a genomic copy of the Arabidopsis eIF4A-1 gene partially complemented the growth phenotype

58 rotein is N-terminally truncated and acts as eIF4A inhibitor.

59 ole for eIF4B in addition to its function as eIF4A cofactor in promoting PIC attachment or scanning o

60 drugs actually increase the affinity between eIF4A and RNA.

61 ormation of a stable ternary complex between eIF4A and eIF4B.

62 In particular, the interaction between eIF4A and eIF4G is destabilized, leading to a temporary

63 F correlated with the ability of Vhs to bind eIF4A but not eIF4H.

64 cancer cells was also inhibited by blocking eIF4A RNA helicase activity with silvestrol and CR-1-31-

65 Here we show that, albeit both eIF4A domains play a role in binding the middle domain o

66 minal eIF4A binding domain but not when both eIF4A binding domains are present, suggesting that the C

67 ciates with at least four cap complexes, but eIF4A is replaced by additional helicases in quiescent c

68 to the Yn-Xm-AUG motif, which is enhanced by eIF4A.

69 eIF4A, whereas others are suppressed only by eIF4A overexpression.

70 bit mRNA recruitment in a manner relieved by eIF4A, indicating that the factor does not act solely to

71 G to the J-K domains, which is stimulated by eIF4A.

72 y stimulates the rate of duplex unwinding by eIF4A on the IRES.

73 only provide evidence that mRNA unwinding by eIF4A stimulates start codon recognition, but also sugge

74 Here we show that S. cerevisiae eIF4A and Ded1p directly interact with each other and si

75 This artificially clamped eIF4A blocks 43S scanning, leading to premature, upstrea

76 vitro and in cells, RocA specifically clamps eIF4A onto polypurine sequences in an ATP-independent ma

77 lex to the 5' mRNA cap by the eIF4F complex (eIF4A, eIF4E, and eIF4G).

78 ap-dependent translation initiation complex, eIF4A has a novel function as a specific inhibitor of Dp

79 nant cells, define mRNA features that confer eIF4A dependence, and provide genetic support for Silves

80 cells demonstrates that this novel conserved eIF4A/eIF4G-like complex acts in pre-rRNA processing, ad

81 s from proliferating cultures mainly contain eIF4A, which associates with at least four cap complexes

82 s in the presence of a transcript containing eIF4A-interacting RNA aptamer resulted in the restoratio

83 In contrast, eIF4A on its own has little RNA substrate specificity.

84 ramework for the interactions between Ded1p, eIF4A, eIF4G, RNA and ATP, which indicates that eIF4A, w

85 Therefore, our results define eIF4A as a universal initiation factor in cap-dependent

86 specifically to the eIF4A N-terminal domain (eIF4A-NTD) using similar binding interfaces.

87 se 2B but did not phosphorylate eIF1, eIF1A, eIF4A, eIF4E, eIF4G, eIFiso4E, or eIFiso4G.

88 All of them require eIF2, eIF3, eIF4A, eIF4G, eIF4B, eIF1A, and a single ITAF, poly(C) b

89 eIF4B, eIF4A, and Ded1 mutations also preferentially impair tra

90 nding region, and binding domains for eIF4E, eIF4A, and eIF4B; (ii) eIF4G601-1488, which contains an

91 Interactions of eIF4G with eIF4E, eIF4A, eIF3, poly(A)-binding protein, and Mnk1/2 have be

92 +/- 30 nm), (ii) the helicase complex eIF4F-eIF4A-eIF4B-ATP increases 40S subunit binding (Kd = 120

93 part of eIF4F, the complex comprising eIF4G, eIF4A, and eIF4E.

94 ance of eIF4F core components (eIF4E, eIF4G, eIF4A) and the eIF4F-associated factor poly(A) binding p

95 essential for translation initiation, eIF4G-eIF4A, and we demonstrate that Gle1(InsP6) and eIF4G bot

96 eIF4G/eIF4A then restructure the region of ribosomal attachmen

97 ability of mutant type 1 IRESs to bind eIF4G/eIF4A correlated with their translational activity.

98 nhibit protein synthesis by displacing eIF4G/eIF4A from uncapped > capped RNAs.

99 ), and starts with specific binding of eIF4G/eIF4A to d11.

100 nce, initiation starts with binding of eIF4G/eIF4A.

101 OR signaling, likely resulting from enhanced eIF4A-dependent unwinding of G-quadruplexes in the 5' un

102 cogenes with complex 5'UTRs require enhanced eIF4A RNA helicase activity for translation.

103 For example, eIF4A promotes T-cell acute lymphoblastic leukaemia deve

104 inhibitor not only enhances PDCD4 expression/eIF4A binding but also blocks HA-CD44-mediated tumor cel

105 1 production, and increases PDCD4 expression/eIF4A binding.

106 of eukaryotic translation initiation factor eIF4A and pixie mutant clones in wing discs suggests tha

107 ication of the translation initiation factor eIF4A for its essential role in self-renewal by directly

108 rexpression of translation initiation factor eIF4A, a helicase, enhances production of Hac1 from an m

109 ine-339 of the translation initiation factor eIF4A, abolishing its helicase activity and inhibiting t

110 ) inhibits the translation initiation factor eIF4A, an RNA helicase that catalyzes the unwinding of s

111 y blocking the translation initiation factor eIF4A.

112 expression of translation initiation factors eIF4A and eIF4GI, and reduced expression of the eIF4A in

113 of the human translation initiation factors eIF4A, a two-domain DEAD-Box helicase, the HEAT-1 domain

114 shown that Vhs binds the translation factors eIF4A and eIF4H.

115 th mRNA as well as other initiation factors (eIF4A, eIF4G, PABP, and eIF3).

116 lex, an amalgam of three initiation factors, eIF4A, eIF4G, and eIF4E, by the chemical inhibitor 4E1RC

117 itiation factor 4B (eIF4B) is a cofactor for eIF4A but also might function independently of eIF4A.

118 ns in that there are interaction domains for eIF4A and PABP and we identify, for the first time, the

119 strate that the MA-3 domain is important for eIF4A binding and explain the ability of Pdcd4 or eIF4Gc

120 of mRNAs shows a heightened requirement for eIF4A, dependence on eIF4A is correlated with requiremen

121 ompete with the eIF4G MA3 domain and RNA for eIF4A binding.

122 ber and cell size, consistent with roles for eIF4A in both cell division and cell growth.

123 Free eIF4A is a poor helicase and requires the accessory prot

124 initiation by displacing eIF4G and RNA from eIF4A.

125 Furthermore, eIF4A physically associates with Mad and Medea, and prom

126 -binding subunit eIF4E and the mRNA helicase eIF4A and is also required for re-initiation in mammals.

127 initiation complex, namely, the RNA helicase eIF4A and the scaffolding protein eIF4G.

128 f the cap-binding eIF4E and the RNA helicase eIF4A assembled onto an eIF4G platform, remains obscure.

129 The two-domain RNA helicase eIF4A is a very weak helicase by itself, but the activit

130 The RNA helicase eIF4A plays a key role in unwinding of mRNA and scanning

131 by interacting tightly with the RNA helicase eIF4A via its tandem MA-3 domains.

132 the cap-binding protein eIF4E, the helicase eIF4A, and the central scaffold eIF4G, is a convergence

133 nits eIF4G and eIF4E and often the helicase, eIF4A.

134 N obviates the requirement for the helicase, eIF4A.

135 DEAD-box RNA helicases eIF4A and Ded1 are believed to promote translation initi

136 volves two conserved DEAD-box RNA helicases, eIF4A and Ded1p.

137 to examine the roles of two yeast helicases, eIF4A and Ded1, previously implicated in translation ini

138 However, eIF4A overexpression suppressed the impaired AUG recogni

139 This study identifies eIF4A as a novel dose-dependent regulator of stem elonga

140 ng of mutants lacking eIF4B or with impaired eIF4A or Ded1 activity revealed that eliminating eIF4B r

141 These changes in eIF4A affinity for its partner proteins upon binding to

142 er, either eliminating eIF4B or inactivating eIF4A preferentially impacts mRNAs with longer, more str

143 ymatic activities of eIF4A, yet it inhibited eIF4A-eIF4G association and promoted the formation of a

144 In addition, directly inhibiting eIF4A with silvestrol significantly suppressed Sin1 tran

145 PDCD4 inhibits eIF4A, and PDCD4 knockout mice have a high penetrance fo

146 by a re-localization mechanism that involves eIF4A.

147 lutionarily conserved patch that matches key eIF4A-interacting residues of eIF4G when superimposed on

148 exes containing eIF4G and yeIF4B but lacking eIF4A.

149 unit of heterodimer eIF4F (plant eIF4F lacks eIF4A), and 3'-BTE-5'-UTR interaction.

150 f the HEAT domain in scanning beyond loading eIF4A onto the pre-initiation complex.

151 eIF4A, but the extent to which they modulate eIF4A activity is poorly understood.

152 Notably, among the most eIF4A-dependent and silvestrol-sensitive transcripts are

153 the translation initiation of natural mRNAs, eIF4A, eIF4B, and eIF4F.

154 the mTOR signaling pathway, including mTOR, eIF4A, and eIF4E, are downregulated by mf, suggesting th

155 s in vivo, and the rescue of specific mutant eIF4A.eIF4G complexes by yeIF4B was reconstituted in vit

156 as correlated with the restoration of native eIF4A.eIF4G complexes in vivo, and the rescue of specifi

157 sertions increase dependence on Ded1 but not eIF4A for efficient translation.

158 hanced the intrinsic enzymatic activities of eIF4A, yet it inhibited eIF4A-eIF4G association and prom

159 y and ATP-dependent RNA helicase activity of eIF4A and eIF4F during translation initiation.

160 y and ATP-dependent RNA helicase activity of eIF4A and eIF4F during translation initiation.

161 blocks the RNA duplex unwinding activity of eIF4A but, at the same time, stimulates its ATPase activ

162 both stimulate the RNA helicase activity of eIF4A, a component of the mRNA cap-binding complex eIF4F

163 F4H enhance the duplex unwinding activity of eIF4A, but the extent to which they modulate eIF4A activ

164 hat crowding enhances the ATPase activity of eIF4A, which correlates with a shift to a more compact s

165 ly activate the duplex unwinding activity of eIF4A.

166 cts on the RNA-stimulated ATPase activity of eIF4A.

167 dent, but unwinding-independent, activity of eIF4A.

168 accessory proteins modulate the affinity of eIF4A for ATP by interacting simultaneously with both he

169 in functions to stabilize the association of eIF4A with eIFiso4G in the presence of eIF4B or PABP.

170 Association of eIF4A with WT eIF4G in vivo also was enhanced by yeIF4B

171 ation phases of mRNA translation: binding of eIF4A to eIF4G, reduction in PDCD4 expression and inhibi

172 eIF4G stabilizes the active conformation of eIF4A required for its RNA helicase activity.

173 scribe the transcriptome-wide consequence of eIF4A inhibition in malignant cells, define mRNA feature

174 The helicase complex, consisting of eIF4A, eIF4B, and ATP, stimulated BTE binding with eIF4G

175 at eIF4B couples the ATP hydrolysis cycle of eIF4A with strand separation, thereby minimizing nonprod

176 nd to interact with the N-terminal domain of eIF4A through a conserved surface region encompassing th

177 4G-m interacts with the C-terminal domain of eIF4A.

178 However, the individual domains of eIF4A, or the eIF4G-HEAT-1 domain alone show little stru

179 sing, adding to the established functions of eIF4A/eIF4G in translation initiation and of eIF4AIII as

180 me footprinting to identify the hallmarks of eIF4A-dependent transcripts.

181 We highlight physiological implications of eIF4A inhibition, providing mechanistic insight into eIF

182 of many more genes than does inactivation of eIF4A, despite comparable reductions in bulk translation

183 ulates the ribosomal scanning independent of eIF4A.

184 te that eIF4G binds to eIF3 independently of eIF4A binding to the middle region of eIF4G.

185 F4A but also might function independently of eIF4A.

186 Accordingly, inhibition of eIF4A with silvestrol has powerful therapeutic effects a

187 itosis strongly enhanced the interactions of eIF4A with HEAT domain 2 of eIF4G and decreased associat

188 was confirmed, and we show that the level of eIF4A protein is strongly reduced in the mutant.

189 st DLBCLs are derived, have higher levels of eIF4A cap-binding activity and protein translation than

190 onal repeats are required at lower levels of eIF4A or when the NTD is missing.

191 late treatment may not phenocopy the loss of eIF4A activity, as these drugs actually increase the aff

192 Loss of eIF4A-1 reduces the proportion of mitotic cells in the r

193 ted presence in vivo of only one molecule of eIF4A in the eIF4F complex.

194 nditions Pdcd4 binds to a single molecule of eIF4A, which involves contacts with both Pdcd4 MA-3 doma

195 Omission of eIF4A or disruption of eIF4E-eIF4G-eIF3 interactions con

196 bilize the closed interdomain orientation of eIF4A.

197 Overexpression of eIF4A decreases Dpp signalling and causes loss of Mad an

198 ooperativity between all binding partners of eIF4A (eIF4G, RNA, ATP) and stimulation of eIF4A activit

199 eIF4G promotes recruitment of eIF4A to type 1 IRESs, and together, eIF4G and eIF4A ind

200 Here, we investigated the role of eIF4A in porcine sapovirus VPg-dependent translation.

201 complex and the mechanisms of stimulation of eIF4A activity have remained elusive.

202 f eIF4A (eIF4G, RNA, ATP) and stimulation of eIF4A activity in the eIF4F complex.

203 phoma progression, and specific targeting of eIF4A may be an attractive therapeutic approach in the m

204 ghtened requirement for eIF4A, dependence on eIF4A is correlated with requirements for Ded1 and 5' UT

205 Cdk1:cyclin B and its inhibitory effects on eIF4A helicase activity in the mitotic translation initi

206 nhibitor, we identify 284 genes that rely on eIF4A for efficient translation.

207 untranslated regions that depend strongly on eIF4A-mediated unwinding.

208 nt on the Ded1/Dbp1 type of helicase than on eIF4A or eIF4B.

209 translation initiation complex assembly, or eIF4A function.

210 compared the effects of mutations in Ded1 or eIF4A on global translational efficiencies (TEs) in budd

211 as eukaryotic initiation factor 3 (eIF3) or eIF4A, or the processing body (PB) markers, such as mRNA

212 the canonical cap-binding factor, eIF4G, or eIF4A or with proteins expressed late in oogenesis, incl

213 initiation factor 2alpha phosphorylation or eIF4A inhibition, but are still SG-competent when challe

214 uppressed by overexpressing either yeIF4B or eIF4A, whereas others are suppressed only by eIF4A overe

215 terization of the stoichiometry of the Pdcd4-eIF4A complex suggests that under physiological conditio

216 Plant eIF4A is very loosely associated with the plant cap-bind

217 hich bind and activate the DEAD-box proteins eIF4A and Dbp5.

218 A T-DNA mutant eif4a1 line, with reduced eIF4A protein levels, displays slow growth, reduced late

219 ocA does not repress translation by reducing eIF4A availability.

220 m transcripts for the translation regulators eIF4A and Pabp, which are also translationally-induced d

221 The resultant eIF4A protein is N-terminally truncated and acts as eIF4

222 expression from transcripts bearing the RocA-eIF4A target sequence.

223 Using Silvestrol, a selective eIF4A inhibitor, we identify 284 genes that rely on eIF4

224 reas inactivation of a temperature-sensitive eIF4A variant encoded by tif1-A79V (in a strain lacking

225 ammed cell death 4 (PDCD4), which sequesters eIF4A from the eIF4E.eIF4G complex, resulting in repress

226 domain to modulate its ability to stimulate eIF4A helicase activity.

227 autoinhibition, enabling eIF4G to stimulate eIF4A helicase activity.

228 Mammalian eIF4B also stimulates eIF4A activity, but this function appears to be lacking

229 binding truncation of eIF4G that stimulates eIF4A duplex unwinding independently of eIF4E.

230 eIF4H is much less efficient at stimulating eIF4A unwinding activity than eIF4B, implying that eIF4H

231 anslation initiation to yield free subunits (eIF4A, eIF4E, and eIF4G) is presented.

232 ited Sin1 translation is through suppressing eIF4A, and functionally important for suppression of mTO

233 Surprisingly, eIF4A accelerated the rate of recruitment of all mRNAs t

234 the central A-rich domains of BC RNAs target eIF4A, specifically inhibiting its RNA helicase activity

235 he primate-specific BC1 counterpart, targets eIF4A activity in identical fashion, as a result decoupl

236 ng eIFiso4G in the absence of the C-terminal eIF4A binding domain but not when both eIF4A binding dom

237 veal an important function of the C-terminal eIF4A binding domain in maintaining the interaction of m

238 are present, suggesting that the C-terminal eIF4A interaction domain functions to stabilize the asso

239 488, which contains an additional C-terminal eIF4A-binding domain; and (iii) eIF4G742-1196, which lac

240 does differ, however, in that the N-terminal eIF4A binding domain overlaps with the eIF4B and PABP bi

241 Our findings that eIF4A functionally interacts with the PIC and plays impo

242 Using a single-molecule assay, we found that eIF4A functions instead as an adenosine triphosphate-dep

243 and dominant-negative mutants, we found that eIF4A is required for viral translation and infectivity,

244 4A, eIF4G, RNA and ATP, which indicates that eIF4A, with and without eIF4G, acts as a modulator for a

245 ants could not be recovered, indicating that eIF4A function is essential for plant growth and develop

246 re is consistent with a recent proposal that eIF4A modulates the conformation of the 40S ribosomal su

247 Finally, we show that eIF4A acts synergistically with, but independently of, t

248 Importantly, our results show that eIF4A inhibition alters translation of an mRNA subset di

249 We show that eIF4A's ATPase activity is markedly stimulated in the pr

250 Our results show that eIF4A, especially in the presence of its "cofactor" eIF4

251 Our results suggest that eIF4A-mediated enhancement of oncogene translation may b

252 The eIF4A mechanism places BC RNAs in a central position to

253 the PI3Kshort right arrowAKT pathway and the eIF4A RNA helicase, and that this response promotes EGFR

254 d on BCR activation and is attenuated by the eIF4A inhibitor Silvestrol.

255 nes harbour a targetable requirement for the eIF4A RNA helicase.

256 It is also not clear if the eIF4A helicase plays a role in stabilizing the interacti

257 inding sites for one or more isoforms of the eIF4A family of ATP-dependent DEAD-box RNA helicases tha

258 /MA3 proteins, interacts with members of the eIF4A family of helicases.

259 ma signaling promotes the degradation of the eIF4A inhibitor programmed cell death protein 4, which f

260 4A and eIF4GI, and reduced expression of the eIF4A inhibitor, PDCD4.

261 death protein 4 (PDCD4), an inhibitor of the eIF4A RNA helicase, and contributes to the induction of

262 Here we report the topology of the eIF4A/4G/4H helicase complex, which is built from multip

263 n superimposed on the X-ray structure of the eIF4A/eIF4G complex.

264 m(7)G cap and eIF4E dependent, requires the eIF4A helicase, and is strongly influenced by repeat len

265 he findings also indicate that targeting the eIF4A RNA helicase is a novel approach for blocking MUC1

266 6 but not eIF4G601-1488, suggesting that the eIF4A binding domains may serve a regulatory role, with

267 codon recognition, but also suggest that the eIF4A-binding site on eIF4G made of the HEAT domain stim

268 ly very similar and bind specifically to the eIF4A N-terminal domain (eIF4A-NTD) using similar bindin

269 wth factor-stimulated MCF-10A cells with the eIF4A RNA helicase inhibitors, silvestrol and CR-1-31-B,

270 Thus eIF4A can act to separate only a limited number of base-

271 D253A,D418A), a mutant that does not bind to eIF4A, failed to inhibit Sin1 translation, and consequen

272 or eIF4Gc but not DAP-5/NAT1/p97 to bind to eIF4A.

273 ains an MA-3 domain, but it does not bind to eIF4A.

274 3 domain competes with eIF4Gc for binding to eIF4A and surprisingly is sufficient to inhibit translat

275 tion site influenced neither cMA3 binding to eIF4A nor its ability to inhibit translation initiation.

276 expression and inhibition of its binding to eIF4A, eEF2 kinase phosphorylation, and dephosphorylatio

277 yeast eIF4G conducive for stable binding to eIF4A.

278 cp(C3) also stimulates RNA cross-linking to eIF4A in an ATP-independent manner.

279 We show that Su(dpp)(YE9) maps to eIF4A and that this allele is associated with a substitu

280 containing transcripts are also resistant to eIF4A inhibition.

281 In contrast to previous reports, two eIF4A binding domains in eIFiso4G were identified, simil

282 despite the presence of a very short 5' UTR, eIF4A is required to unwind RNA structure in the sapovir

283 -UTR and migrate to the initiation codon via eIF4A-mediated scanning.

284 s genome encodes two isoforms, one of which (eIF4A-1) is required for the coordination between cell c

285 condary structures within 5' UTRs, and while eIF4A cooperates with Ded1 in this function, it also pro

286 PABP and eIF4B compete with eIF4A for binding eIFiso4G in the absence of the C-termi

287 e essential for forming a tight complex with eIF4A in vivo, whereas the equivalent region of the C-te

288 form a tighter and more stable complex with eIF4A, which explains the need for two tandem MA3 domain

289 sites detached HEAT-2 from the complex with eIF4A/-4B/-3 and stimulated the association of HEAT-3 wi

290 lagen alpha2(I) mRNA can be pulled down with eIF4A, and collagen alpha2(I) mRNA is unrestrictedly loa

291 main organization but both can interact with eIF4A, eIF4B, eIF4E isoforms, and the poly(A)-binding pr

292 in other MA-3 domains known to interact with eIF4A, including the preceding domain of Pdcd4, suggesti

293 MA-3(C)), characterized its interaction with eIF4A and compared the features of nuclear magnetic reso

294 translation through direct interaction with eIF4A in the 5' cap-binding complex, revealing a posttra

295 eraction, but not for their interaction with eIF4A.

296 is dependent on an enhanced interaction with eIF4A.

297 onal machinery through its interactions with eIF4A, eIF4G, eIF3, the poly(A)-binding protein (PABP),

298 Vhs also interacts with eIF4A in GST pull-down and coimmunoprecipitation assays.

299 We show that eIF4H interacts physically with eIF4A in the yeast two-hybrid system and in GST pull-dow

300 IF4E, the cap-binding protein, together with eIF4A and eIF4G into a complex termed eIF4F.