ライフサイエンスコーパス: eIF3

1 eukaryotic translation initiation factor 3 (eIF3).

2 initiation factors (eIF4A, eIF4G, PABP, and eIF3).

3 tabilizing the interaction between eIF4G and eIF3.

4 tal eukaryotic translation initiation factor eIF3.

5 grity and translation initiation function of eIF3.

6 of protein phosphorylation quantification on eIF3.

7 p48 subunit of translation initiation factor eIF3.

8 ely eukaryotic initiation factor (eIF) 2 and eIF3.

9 aberrant, alternative pathway requiring only eIF3.

10 or modeling the architecture of intact human eIF3.

11 ulti-component translation initiation factor eIF3.

12 protein translation, via an interaction with eIF3.

13 Consequently, P54 inhibited two functions of eIF3.

14 ound to both the "e" and the "c" subunits of eIF3.

15 nd for which this has not been determined is eIF3.

16 ch as five-fold the amount of eIF4G bound to eIF3.

17 a subunit of eIF4F, and eIF3a, a subunit of eIF3.

18 the eIF4G subunit associates with 40S-bound eIF3.

19 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry

20 ukaryotic initiation factor 4E (eIF4E)-eIF4G-eIF3-40S chain of interactions, but the mechanism by whi

21 nsistent with the model in which eIF4E-eIF4G-eIF3-40S interactions place eIF4E at the leading edge of

22 initial event is the formation of a ternary eIF3/40S/IRES complex.

23 of eIF3a is responsible for the formation of eIF3(a:b:i:g) subcomplex and, because of mutually exclus

24 slational regulation and in formation of the eIF3(a:b:i:g) subcomplex remain to be solved.

25 F3a as the docking site for the formation of eIF3(a:b:i:g) subcomplex.

26 onsisting of eIF3a, eIF3b, eIF3g, and eIF3i (eIF3(a:b:i:g)) has also been identified.

27 n mammalian cells requires initiation factor eIF3, a approximately 750-kilodalton complex that contro

28 lectron microscopy reconstructions show that eIF3, a five-lobed particle, interacts with the hepatiti

29 binding to translasome components, including eIF3, a known partner for Sty1, a pattern of protein int

30 Here, we focus on eIF3, a large multiprotein complex that plays a central

31 eukaryotic translation initiation factor 3 (eIF3) acts as a distinct repressor of FTL mRNA translati

32 ed mRNAs can be recruited in the presence of eIF3 alone.

33 eIF3 also associates with ribosome biogenesis factors an

34 We report that eIF5B or eIF5B/eIF3 also promote Met-tRNA(iMet) binding to IRES-40S com

35 ation rates, the former specifically reduced eIF3 amounts in termination complexes.

36 ion of 3e5 diminishes eIF4G interaction with eIF3 and causes abnormal gene expression at the translat

37 Thus, it appears that eIF3 and eIF2 are more critically required than eIF4G fo

38 hat the IRES RNA coordinates interactions of eIF3 and eIF2 on the ribosome required to position the i

39 mutants prevents stable association of both eIF3 and eIF2, preventing initiator tRNA deposition and

40 nable 43S preinitiation complexes containing eIF3 and eIF2-GTP-Met-tRNA(iMet) to bind directly to the

41 ically the recruitment of initiation factors eIF3 and eIF2.

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

43 Detailed modeling of eIF3 and eIF4F onto the 40S ribosomal subunit reveals th

44 multisubunit translation initiation factors eIF3 and eIF4F.

45 F3 and that mTOR controls the association of eIF3 and eIF4G.

46 ifactor complex (MFC) comprising eIF1, eIF2, eIF3 and eIF5, similar to the MFC reported in yeast and

47 m-loop within the c-JUN 5' UTR recognized by eIF3 and essential for specialized translation initiatio

48 4 bound to the translation initiation factor eIF3 and inhibited translation.

49 Human 5MP1 interacts with eIF2 and eIF3 and inhibits general and gene-specific translation

50 Phospho-Upf1 interacts directly with eIF3 and inhibits the eIF3-dependent conversion of 40S/M

51 unctions of HCR1 and TIF32 in 40S binding of eIF3 and is needed for optimal preinitiation complex ass

52 We conclude that the complex formation of eIF3 and its association with the ribosomes might contri

53 at involve the translation initiation factor eIF3 and mRNA decay factors.

54 of the central translation initiation factor eIF3 and recognition of the HCV genomic RNA start codon,

55 t evidence that mTOR interacts directly with eIF3 and that mTOR controls the association of eIF3 and

56 as revealed how the HCV IRES RNA binds human eIF3 and the 40S ribosomal subunit and positions the sta

57 eIF2 function through its interactions with eIF3 and the 40S ribosomal subunit.

58 uction of a 40S ribosomal complex containing eIF3 and the CSFV IRES.

59 Although capped mRNAs require eIF3 and the eIF4 factors for efficient recruitment to t

60 We show that eIF3 and the eIF4 factors not only stabilize binding of

61 and comparison of the ribosomal positions of eIF3 and the HCV IRES revealed that they overlap, so tha

62 We report that eIF3 and the small ribosomal subunit bind HIV RNA within

63 llular levels of the c, d, and l subunits of eIF3 and their association with the eIF3 core subunit a.

64 nctional analysis of the interaction between eIF3 and two mRNAs encoding the cell proliferation regul

65 ifactor complex with Met-tRNA(i)(Met), eIF2, eIF3, and eIF5 and binds near the P-site.

66 in the multifactor complex (MFC) with eIF2, eIF3, and eIF5 via multiple interactions with the MFC co

67 ukaryotic initiation factor 1 (eIF1), eIF1A, eIF3, and eIF5, and the resulting preinitiation complex

68 sical association with the initiation factor eIF3, and gle1 mutants display genetic interactions with

69 also reduce 40S ribosomal subunit binding to eIF3, and inhibit eIF5B-dependent steps downstream of st

70 y(A) tail, as well as eIF4E, eIF4G, Pab1 and eIF3, and is dependent on the length of both the mRNA an

71 ein subunit of translation initiation factor eIF3, and overexpression of eIF3h malignantly transforms

72 vitro and in vivo, affects 40S occupancy of eIF3, and produces a leaky scanning defect indicative of

73 However, the contributions of eIF1, eIF1A, eIF3, and the eIF2-GTP-Met-tRNAi ternary complex (TC) in

74 nsitivity of 48S complexes assembled by eIF2/eIF3- and eIF5B/eIF3-mediated mechanisms to eIF1-induced

75 lthough 48S complexes assembled both by eIF2/eIF3- and eIF5B/eIF3-mediated Met-tRNA(iMet) recruitment

76 robust protein synthesis promoted by intact eIF3 appears to be a part of the requisites for sound St

77 t interaction sites with the 40S subunit and eIF3 are conserved between HCV and HCV-like IRESs.

78 etry, we show that distinct regions of human eIF3 are sufficient for binding to the HCV IRES RNA and

79 40S and eIF3 are sufficient for initial binding.

80 We identified eIF3 as a component of the 3'BTE recruited complex using

81 of the protein translation initiation factor EIF3, as the direct target of the YTHDF1.

82 eIF3 assembles into a large supercomplex, the translasom

83 he entry channel, augmenting the function of eIF3 at both entry and exit channels.

84 ause eIF3j has been shown to be required for eIF3 binding to 40 S ribosomes in vitro, the results sug

85 D) of the eIF3c/Nip1 subunit, which mediates eIF3 binding to eIF1 and eIF5, to semirandom mutagenesis

86 Limited proteolysis reveals that eIF3 binding to the 40S ribosomal subunit occurs through

87 required neither eIF4E binding to eIF4G nor eIF3 binding to the 40S ribosomal subunit.

88 he RNA-binding motif of subunit eIF3a weaken eIF3 binding to the HCV IRES and the 40S ribosomal subun

89 ng of partially proteolyzed HeLa eIF3 to the eIF3-binding domain of human eIF4G-1, followed by high t

90 subdomains within the previously identified eIF3-binding domain.

91 ons reveals that eIF4G contains two distinct eIF3-binding subdomains within the previously identified

92 eIF3 binds to a highly specific program of messenger RNA

93 During canonical initiation, eIF3 binds to the 40S subunit as a component of the 43S

94 This structural core in eIF3 binds to the small (40S) ribosomal subunit, to tran

95 We propose a new role for eIF3, where eIF3 bridges BYDV's UTRs, stabilizes the long-range 5'-3

96 cruitment of eukaryotic initiation factor 3 (eIF3), but also requires cap recognition by eIF3d, a new

97 eukaryotic translation initiation factor 3 (eIF3), but the exact functional role of the eIF3 complex

98 omain in eIF4G is responsible for binding to eIF3, but the identity of the eIF3 subunit(s) involved i

99 V-like IRESs also specifically interact with eIF3, but the role of this interaction in IRES-mediated

100 subunit of the translation initiation factor eIF3, but unlike the other members, p49 did not inhibit

101 an p56 proteins block different functions of eIF3 by binding to its different subunits.

102 , and eIF3j, a loosely associated subunit of eIF3, can promote recycling of eukaryotic post-TCs.

103 these two proteins, we suggest that Rps3 and eIF3 closely co-operate to control translation terminati

104 (eIF3), but the exact functional role of the eIF3 complex and of its subunits remains to be precisely

105 mulation promotes mTOR/raptor binding to the eIF3 complex and phosphorylation of S6K1 at its hydropho

106 The eIF3 complex consists of approximately 10 subunits whose

107 y significantly impairs the integrity of the eIF3 complex due to down-regulation of multiple other su

108 small eIF3j subunit is unassociated with the eIF3 complex in quiescent T lymphocytes, but upon activa

109 The p190A-eIF3 complex is distinct from eIF3 complexes containing

110 s the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit.

111 s the highly flexible 800 kDa molecular mass eIF3 complex, and mediates translation initiation.

112 factor 3a), one of the core subunits of the eIF3 complex, has been implicated in regulating translat

113 factor-3a (eIF3a), a putative subunit of the eIF3 complex, has recently been shown to have an importa

114 When inactive, S6K1 associates with the eIF3 complex, while the S6K1 activator mTOR/raptor does

115 the structural integrity and function of the eIF3 complex.

116 F3f) is the p47 subunit of the multi-subunit eIF3 complex.

117 ndent on subunits i and g of the heteromeric eIF3 complex.

118 th PRT1 without substantially disrupting the eIF3 complex; (ii) rnp1 impairs the 40S binding of eIF3

119 eukaryotic translation initiation factor 3 (eIF3) complex, as a key downstream target, and demonstra

120 The p190A-eIF3 complex is distinct from eIF3 complexes containing S6K1 or mammalian target of ra

121 eling, allowed us to position and orient all eIF3 components on the 40SeIF1 complex, revealing an ext

122 The structures of eIF3 components reported here also have implications for

123 Eukaryotic translation initiation factor 3 (eIF3) consists of core subunits that are conserved from

124 trictly requires direct interaction of their eIF3 constituent with eIF4G.

125 does not require direct interaction of their eIF3 constituent with the IRES-bound eIF4G.

126 ereas the latter increased overall levels of eIF3-containing terminating ribosomes in heavy polysomes

127 Mammalian eIF3 contains 13 subunits and participates in nearly all

128 Higher eukaryotic eIF3 contains additional (noncore or nonconserved) subun

129 Eukaryotic initiation factor eIF3 contains at least thirteen non-identical subunits,

130 Based on these results, we hypothesize that eIF3 contributes to hyperactivation of the translation i

131 eukaryotic translation initiation factor 3 (eIF3) controls access of other initiation factors and mR

132 units of eIF3 and their association with the eIF3 core subunit a.

133 inimal, six-subunit Saccharomyces cerevisiae eIF3 core.

134 cting with the translation initiation factor eIF3, Cpeb4 represses the translation of a large set of

135 nteracts directly with eIF3 and inhibits the eIF3-dependent conversion of 40S/Met-tRNA(i)(Met)/mRNA t

136 gram includes PERK-dependent switching to an eIF3-dependent translation initiation mechanism, resulti

137 oes not explain genetic evidence correlating eIF3 deregulation with tissue-specific cancers and devel

138 Mutations throughout eIF3 disrupt its interaction with the PIC and diminish i

139 To overcome this, eIF3 dramatically increases the affinity of eIF1 and eIF

140 the O. furnacalis feeding group: LOX1, ASN1, eIF3, DXS, AOS, TIM, LOX5, BBTI2, BBTI11, BBTI12, BBTI13

141 eIF2, eIF3, eIF1 and eIF1A promote efficient 48S initiation co

142 The TC, eIF3, eIF1, and eIF1A cooperatively bind to the 40S subu

143 In cooperation with eIF3, eIF1, and eIF1A, Met-tRNA(Met)(i)/eIF2/GTP binds t

144 t-TCs) can be mediated by initiation factors eIF3, eIF1, and eIF1A, this energy-free mechanism can fu

145 top codon and report that initiation factors eIF3, eIF1, eIF1A, and eIF3j, a loosely associated subun

146 The presence of eIF2, eIF3, eIF1, eIF1A, and Met-tRNAi(Met) was sufficient for

147 tiple initiation factors in vitro, including eIF3, eIF1, eIF5, and eIF1A.

148 (i)(Met) ternary complex (TC) interacts with eIF3-eIF1-eIF5 complex to form the multifactor complex (

149 -tRNA(i)(Met) ternary complex (TC) binds the eIF3/eIF1/eIF5 complex to form the multifactor complex (

150 All of them require eIF2, eIF3, eIF4A, eIF4G, eIF4B, eIF1A, and a single ITAF, pol

151 leading to a temporary stabilization of the eIF3-eIF4G interaction on the 48S complex.

152 r study reveals unexpected complexity to the eIF3-eIF4G interaction that provides new insight into th

153 eukaryotic translation initiation factor 3 (eIF3), eIF5, and eIF2, but not with other translation in

154 ize the multifactor complex containing eIF1, eIF3, eIF5, and TC, showing that eIF1 promotes PIC assem

155 , we examined the effects of depleting eIF2, eIF3, eIF5, or eIF4G in Saccharomyces cerevisiae cells o

156 cated in the yeast multifactor complex (eIF1-eIF3-eIF5-eIF2-GTP-Met-tRNA(i)(Met)).

157 extreme C-terminus of the a/Tif32 subunit of eIF3 either suppressed (R116D) or exacerbated (K108E) th

158 Yeast eIF3 engages 40S in a clamp-like manner, fully encirclin

159 ubiquitin levels in its role as a subunit of eIF3 (eukaryote translation initiation factor 3), we fou

160 lso functions as an essential subunit of the eIF3 eukaryotic translation initiation factor in animals

161 lieving the competition between the IRES and eIF3 for a common binding site on the 40S subunit, and r

162 t FLAG-eIF3e specifically competed with HeLa eIF3 for binding to eIF4G in vitro.

163 s that initiate translation independently of eIF3 from the CrPV IRES.

164 However, current understanding of eIF3 function does not explain genetic evidence correlat

165 Consistent with phospho-Upf1 impairing eIF3 function, NMD fails to detectably target nonsense-c

166 NA recruitment of a library of S. cerevisiae eIF3 functional variants spanning its 5 essential subuni

167 e report that mouse p56 also interferes with eIF3 functions and inhibits translation.

168 ve-stain EM reconstructions of reconstituted eIF3 further reveal how the approximately 400 kDa molecu

169 In contrast, eIF3, G3BP, eIF4G, and PABP-1 are restricted to SGs, whe

170 P170, the largest putative subunit of eIF3, has been found elevated in human breast, cervical,

171 ), Y-box binding protein (YBX1), DDX3, DDX5, eIF3, IGF2BP1, multiple myeloma tumor protein 2, interle

172 Depleting eIF2 or eIF3 impaired mRNA binding to free 40S subunits, but dep

173 The role of mammalian eIF3 in assembly of the 48 S complex occurs through high

174 n yeast and higher eukaryotes and a role for eIF3 in elongation.

175 Here we reconstitute the 13-subunit human eIF3 in Escherichia coli, revealing its structural core

176 Our findings illuminate a new role for eIF3 in governing a specialized repertoire of gene expre

177 eIF3 in mammals is the largest translation initiation fa

178 32; and (v) hcr1Delta impairs 40S binding of eIF3 in otherwise wild-type cells.

179 specific interaction of HCV-like IRESs with eIF3 in preventing ribosomal association of eIF3, which

180 the Ts(-) phenotype and increases 40S-bound eIF3 in rnp1 cells; (iv) the rnp1 Ts(-) phenotype is exa

181 esence of initiation factors eIF1, eIF1A and eIF3 in the 40S preinitiation complex (40S.eIF1.eIF1A.eI

182 sent a cryo-electron microscopy structure of eIF3 in the context of the DHX29-bound 43S complex, show

183 HEAT domain to interact with eIF1, eIF2, and eIF3 in the multifactor complex and with eIF4G in the 48

184 an simultaneously and non-competitively bind eIF3 in the presence of active helicase factors forming

185 mutations diminished 40S-bound TC, eIF5 and eIF3 in vivo, and deltaC impaired TC recruitment in vitr

186 hat TC recruitment is a critical function of eIF3 in vivo.

187 ith eukaryotic translation initiation factor eIF3, in termination.

188 Further, quantitative studies showed eIF3 increased recruitment of the 40S subunit by more th

189 opy assay to demonstrate that eIF4G binds to eIF3 independently of eIF4A binding to the middle region

190 and alleviate the necessity for direct eIF4G/eIF3 interaction.

191 ission of eIF4A or disruption of eIF4E-eIF4G-eIF3 interactions converted eIF4E into a specific inhibi

192 Our data reveal the breadth of the eIF3 interactome and suggest that factors involved in tr

193 itive LC-MS/MS to decipher the fission yeast eIF3 interactome, which was found to contain 230 protein

194 contacts position (-)3, and now report that eIF3 interacts with positions (-)8-(-)17, forming an ext

195 eukaryotic translation initiation factor 3 (eIF3) interacts with eIF3 subunits j/Hcr1 and b/Prt1 and

196 is to investigate the molecular mechanism of eIF3 involvement in these reactions.

197 On the other hand, the CDV IRES forms a 40S/eIF3/IRES ternary complex, with multiple points of conta

198 the HCV IRES in the 40S-IRES binary complex, eIF3 is completely displaced from its ribosomal position

199 Mammalian eIF3 is composed of 13 subunits and is the largest eukar

200 tedly show that the eIF4G-binding surface in eIF3 is comprised of the -c, -d and -e subunits.

201 Whether eIF3 is essential for embryonic development and homeosta

202 es as abundant as eIF1, eIF2 and eIF5, while eIF3 is half as abundant as the latter three and hence,

203 nalyze ribosome complexes, we find that most eIF3 is not bound to 40 S ribosomal subunits in unactiva

204 t unlike for host cellular mRNAs, the entire eIF3 is not required for HCV RNA translation, favoring v

205 eIF3 is the principal factor that promotes splitting of

206 eukaryotic initiation factor 4G (eIF4G) and eIF3 is thought to act as the molecular bridge between t

207 Eukaryotic translation initiation factor 3 (eIF3) is a central player in recruitment of the pre-init

208 eukaryotes, translation initiation factor 3 (eIF3) is thought to play an essential role in this proce

209 nd eIF3j to eIF3b, different subcomplexes of eIF3 likely exist and may perform noncanonical functions

210 on AUG recognition; notably, a proportion of eIF3 lingers on during the initial elongation cycles.

211 tinct repressor of FTL mRNA translation, and eIF3-mediated FTL repression is disrupted by a subset of

212 However, 48S complexes formed by the eIF5B/eIF3-mediated mechanism on the truncated IRES could not

213 complexes assembled by eIF2/eIF3- and eIF5B/eIF3-mediated mechanisms to eIF1-induced destabilization

214 lexes assembled both by eIF2/eIF3- and eIF5B/eIF3-mediated Met-tRNA(iMet) recruitment were destabiliz

215 These results identify a direct role for eIF3-mediated translational control in a specific human

216 he 40S preinitiation complex (40S.eIF1.eIF1A.eIF3.Met-tRNA(i).eIF2.GTP) and the subsequent binding of

217 omplex; (ii) rnp1 impairs the 40S binding of eIF3 more so than the 40S binding of HCR1; (iii) overexp

218 In order to do so, eIF3 must associate with pre-termination complexes where

219 utants display genetic interactions with the eIF3 mutant nip1-1.

220 well as how eIF4F interacts with subunits of eIF3 near the mRNA exit channel in the 43S The location

221 The increase in eIF4G associated with eIF3 occurred rapidly and at physiological concentration

222 bunit of the translational initiation factor eIF3, occurs in human breast cancers, but how INT6 relat

223 ependence on eukaryotic initiation factor 3 (eIF3) of reinitiation by recycled 40S subunits, which ca

224 specific enhancement of eIF5-CTD binding to eIF3 on its binding to eIF2beta.

225 ers, such as eukaryotic initiation factor 3 (eIF3) or eIF4A, or the processing body (PB) markers, suc

226 ts having PCI (proteasome, COP9 signalosome, eIF3) or MPN (Mpr1, Pad1, amino-terminal) domains consti

227 Depleting eIF2, eIF3, or eIF5 reduced 40S binding of all constituents of

228 0-kilodalton eukaryotic initiation factor 3 (eIF3) organizes initiation factor and ribosome interacti

229 e e-subunit of translation initiation factor eIF3, other evidence indicates that it interacts with pr

230 ear-complete polyalanine-level models of the eIF3 PCI/MPN core and of two peripheral subunits.

231 -like fold and a proteasome COP9/signalosome eIF3 (PCI) module in a right-handed suprahelical configu

232 eIF3 plays a key role in protein biosynthesis.

233 eIF3 plays an important role in translation initiation.

234 Eukaryotic translation initiation factor 3 (eIF3) plays a central role in translation initiation and

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

236 Thus, the eIF3 preinitiation complex acts as a scaffold to coordin

237 eIF3 promotes translation initiation, but relatively lit

238 The structure exhibits similarity to eIF3 recognizing motifs found in hepatitis C virus (HCV)

239 How these RNA structures mediate eIF3 recruitment to affect translation of specific mRNAs

240 Thus, increasing eIF4G association with eIF3 represents a potentially important mechanism by whi

241 t channels, we uncovered a critical role for eIF3 requiring the eIF3a NTD, in stabilizing mRNA intera

242 The structural core of eIF3 resides on the back of the 40S subunit, establishin

243 Importantly, the eIF3 role in programmed readthrough is conserved between

244 on coupled with mass spectroscopy identified eIF3 subunit b (eIF3b) as a novel P311 binding partner.

245 ing eIF3 to bind to the larger ribosome-free eIF3 subunit complex, and then to the 40 S ribosomes.

246 Toward this goal, here we focused on eIF3 subunit e.

247 Notably, the eIF3 subunit eIF3b is protected by HCV IRES RNA binding,

248 cordingly, we observed reduced levels of the eIF3 subunit eIF3f in ER-positive breast cancer cells co

249 cted hydroxyl radical probing that the human eIF3 subunit eIF3j binds to the aminoacyl (A) site and m

250 ore, our study reveals the role of a noncore eIF3 subunit in modulating a specific developmental prog

251 Here, we identify an eIF3 subunit that regulates eIF4F modification and show

252 for binding to eIF3, but the identity of the eIF3 subunit(s) involved is less clear.

253 dy, we have sought to identify the mammalian eIF3 subunit(s) that directly interact(s) with eIF4G.

254 ranslation and is synchronized by a specific eIF3 subunit.

255 ain in yeast eukaryotic initiation factor 3 (eIF3) subunit b/PRT1 (prt1-rnp1) impairs its direct inte

256 eukaryotic translation initiation factor 3 (eIF3) subunit eIF3e/INT6 has been described in various t

257 hocytes, but upon activation joins the other eIF3 subunits and binds 40 S ribosomal subunits.

258 ntical p190B paralog, associates with all 13 eIF3 subunits and several other translational preinitiat

259 The association of eIF3j with the other eIF3 subunits appears to be inhibited by rapamycin, sugg

260 A pulldown analysis of eIF3 subunits associated with the HCV IRES disclosed sim

261 Addition of the remaining eIF3 subunits enables reconstituted eIF3 to assemble int

262 bind eIF4G, but the potential role of other eIF3 subunits in stabilizing this interaction has not be

263 s to be established whether up-regulation of eIF3 subunits is a consequence or a cause of the maligna

264 on initiation factor 3 (eIF3) interacts with eIF3 subunits j/Hcr1 and b/Prt1 and can bind helices 16

265 of sucrose gradient fractions for individual eIF3 subunits show that the small eIF3j subunit is unass

266 solution structure of an interaction between eIF3 subunits.

267 they do not rule out participation of other eIF3 subunits.

268 evealing an extended, modular arrangement of eIF3 subunits.

269 ning the 40S ribosomal subunit, eIF1, eIF1A, eIF3, ternary complex (eIF2-GTP-Met-tRNAi), and eIF5.

270 mal subunit and the 20 S complex composed of eIF3, ternary complex, eIF4F, and mRNA.

271 nsequently, it has only a marginal effect on eIF3.ternary complex interaction.

272 show eIF2beta as well as a configuration of eIF3 that appears to encircle the 40S, occupying part of

273 c initiation factor (eIF) 3j is a subunit of eIF3 that binds to the mRNA entry channel and A-site of

274 y two highly conserved RNA-binding motifs in eIF3 that direct translation initiation from the hepatit

275 through its interactions with eIF4A, eIF4G, eIF3, the poly(A)-binding protein (PABP), and RNA.

276 emaining eIF3 subunits enables reconstituted eIF3 to assemble intact initiation complexes with the HC

277 to an activation of eIF3j, thereby enabling eIF3 to bind to the larger ribosome-free eIF3 subunit co

278 recipitation indicated diminished binding of eIF3 to eIF4G, signifying a reduction in recruitment of

279 nitiation in vivo and reduces 40S-binding of eIF3 to native preinitiation complexes.

280 gene expression and suggest that binding of eIF3 to specific mRNAs could be targeted to control carc

281 Like P56, it inhibited the ability of eIF3 to stabilize the eIF2 x GTP x Met-tRNA(i) ternary c

282 ow the HCV IRES binds to specific regions of eIF3 to target the translational machinery to the viral

283 hat the rnp1 lesion decreases recruitment of eIF3 to the 40S subunit by HCR1: (i) rnp1 strongly impai

284 wever, binding of partially proteolyzed HeLa eIF3 to the eIF3-binding domain of human eIF4G-1, follow

285 TORC1 pathway, which enhances the binding of eIF3 to the eIF4F complex and, consequently, the assembl

286 l) domains constitute the structural core of eIF3, to which five peripheral subunits are flexibly lin

287 is required for the binding of eIF4B to the eIF3 translation initiation complex.

288 l, discover an unidentified function for the eIF3 translation initiation factor as a scaffold for the

289 and off the eukaryotic initiation factor 3 (eIF3) translation initiation complex in a signal-depende

290 Sel-TCP-seq demonstrated that eIF2 and eIF3 travel along 5' UTRs with scanning 40Ss to successi

291 40S ribosomal subunits (types 3 and 4), and eIF3 (type 3).

292 ation regulators c-JUN and BTG1 reveals that eIF3 uses different modes of RNA stem-loop binding to ex

293 onto the 40S ribosomal subunit reveals that eIF3 uses eIF4F or the HCV IRES in structurally similar

294 very of human transcripts that interact with eIF3 using photoactivatable ribonucleoside-enhanced cros

295 In addition, eIF3 was proposed to coordinate their functions in this

296 We propose a new role for eIF3, where eIF3 bridges BYDV's UTRs, stabilizes the lon

297 rectly binds eukaryotic initiation factor 3 (eIF3), which is sufficient to recruit the 43S complex to

298 eIF3 in preventing ribosomal association of eIF3, which could serve two purposes: relieving the comp

299 initiation (not termination) factor, namely eIF3, which critically promotes programmed readthrough o

300 hought to require the functions of eIF4F and eIF3, with the latter serving as an adaptor between the