ライフサイエンスコーパス: mRNP

1 of these cycles would remove proteins from a mRNP, one at a time, akin to a ratchet mechanism for mRN

2 Aberrant mRNPs resulting from faulty events are retained in the n

3 y cooperate to target and eliminate aberrant mRNPs.

4 y that the targeting of Rho-induced aberrant mRNPs is mediated by Rrp6p, which is recruited cotranscr

5 eps RNAs at the periphery, possibly to allow mRNP rearrangements before export.

6 yadenylated mRNAs can enter P-bodies, and an mRNP complex including poly(A)(+) mRNA, Pab1p, eIF4E, an

7 yotic mRNAs exit translation and assemble an mRNP state that accumulates into processing bodies (P bo

8 a repressor of translation, by assembling an mRNP stalled in translation initiation, and as an ATP-de

9 endent on its RGG domain, thereby forming an mRNP repressed for translation initiation.

10 C, binds the Cp 3'-untranslated region in an mRNP containing three additional proteins, and silences

11 EAD-box ATPase Dbp5p is required for such an mRNP rearrangement.

12 e transition of mRNAs from translation to an mRNP complex destined for decapping.

13 ransport through nuclear pore complexes, and mRNP remodeling events prior to translation.

14 ovement of both chromatin in the nucleus and mRNPs in the cytoplasm.

15 ar export, myosin-bound She3p joins the ASH1 mRNP to form a highly specific cocomplex with She2p and

16 zation for the maturation of localizing ASH1 mRNPs.

17 he human interactome of chromatin-associated mRNP particles.

18 Evidence suggests that PB-associated mRNPs are translationally repressed and can be degraded

19 ining TGF-beta-activated-translational (BAT) mRNP complex.

20 DBIRD complex acts at the interface between mRNP particles and RNAPII, integrating transcript elonga

21 It binds mRNPs through adaptor proteins such as ALY and SR splici

22 e of interactions of germ granule and P body mRNP components on AIN-1/GW182 and NTL-1/CNOT1 in Caenor

23 ing after assembly of the mRNA into a P-body mRNP.

24 b2 functions in this process to control both mRNP compaction that facilitates movement through nuclea

25 nab2 and dbp5 mutants show that a Nab2-bound mRNP is a physiological Dbp5 target.

26 for the export factor NXF1 become part of BR mRNPs already at the gene, NXF1 binds to BR mRNPs only i

27 In steady state, a subset of the BR mRNPs in the interchromatin binds NXF1, UPF2, and UPF3.

28 mately equals synthesis and export of the BR mRNPs.

29 mRNPs already at the gene, NXF1 binds to BR mRNPs only in the interchromatin.

30 heir targets, both are greatly influenced by mRNP dynamics.

31 the three-dimensional (3D) pathway taken by mRNPs as they transit through the NPC, and the kinetics

32 of stored mRNPs and also for sorting certain mRNPs into germplasm-containing structures.

33 f distinct biochemical and compartmentalized mRNPs in the cytosol, with implications for the control

34 scriptional assembly of the export competent mRNP and for coordinating export with 3' end processing.

35 A processing or assembly of export-competent mRNP particles.

36 N-ENE blocks assembly of an export-competent mRNP.

37 but inhibits assembly of an export-competent mRNP.

38 ibutes to the generation of export-competent mRNPs and influences gene expression through interaction

39 quired for the formation of export-competent mRNPs have been described, an integrative view of the sp

40 es cerevisiae generation of export-competent mRNPs terminates the nuclear phase of the gene expressio

41 cle in mRNA (messenger RNA)/protein complex (mRNP) remodeling during nuclear export.

42 re ubiquitous messenger-RNA-protein complex (mRNP) remodelling enzymes that have critical roles in al

43 to Rae1p for targeting mRNA-protein complex (mRNP) to the proteins of the nuclear pore complex (NPC).

44 ntil the BR messenger RNA protein complexes (mRNPs) enter the interchromatin.

45 Remodeling of RNA-protein complexes (mRNPs) plays a critical role in mRNA biogenesis and meta

46 by translocation of mRNA/protein complexes (mRNPs) through nuclear pore complexes (NPCs).

47 ransport of messenger RNA:protein complexes (mRNPs) through the nuclear pore complexes (NPCs) of euka

48 These mRNA-protein complexes (mRNPs) undergo a series of remodeling events that are in

49 exes (pre-mRNPs) and mRNA-protein complexes (mRNPs), allow the visualization of intact cell nuclei an

50 by proteins to form mRNA-protein complexes (mRNPs), but changes in the composition of mRNPs during p

51 ating messenger ribonucleoprotein complexes (mRNPs) implicated in the regulation of mRNA translation

52 alled messenger ribonucleoprotein complexes (mRNPs) that form when eukaryotic cells encounter environ

53 xonal messenger ribonucleoprotein complexes (mRNPs).

54 ion complex to a translationally compromised mRNP.

55 sm by which Dbp5 recognizes Mex67-containing mRNP is not clear.

56 , although accumulation of Mex67p-containing mRNPs is also observed when a nuclear basket component i

57 o mTORC1 signaling through Nanos2-containing mRNPs and establishes a post-transcriptional buffering s

58 facilitates the transfer of NXF1-containing mRNPs to NPCs.

59 ciates with both PTC-free and PTC-containing mRNPs, but it strongly and preferentially associates wit

60 ive association of SMG-2 with PTC-containing mRNPs, indicating that SMG-2 is phosphorylated only afte

61 ssion modulates the associations of the core mRNP components eIF4E, eIF4G, and PABP and of the decay

62 ficking uncovering a new mechanism to couple mRNPs to endosomes.

63 acterized eIF4E1b as a component of the CPEB mRNP translation repressor complex along with the eIF4E-

64 ms) and that upon arrival in the cytoplasm, mRNPs are frequently confined near the nuclear envelope.

65 Moving from the nucleus to the cytoplasm, mRNPs undergo extensive remodeling as they are first act

66 Here we show that TDP-43 forms cytoplasmic mRNP granules that undergo bidirectional, microtubule-de

67 an essential role for Mex67p in cytoplasmic mRNP release and directionality of transport.

68 stration of the TORC1 complex in cytoplasmic mRNP stress granules provides a negative regulatory mech

69 ping machinery can assemble into cytoplasmic mRNP granules called processing bodies (PBs).

70 r the processing of mRNAs in the cytoplasmic mRNP complexes during stress.

71 mponent of dynamically assembled cytoplasmic mRNPs that sequester mRNAs that are poorly translated du

72 n not being actively translated, cytoplasmic mRNPs can assemble into large multi-mRNP assemblies or b

73 ort a dynamic interplay among deadenylation, mRNP remodeling, and P-body formation in selective decay

74 and the coordinated assembly of a decapping mRNP, but the mechanism of substrate recognition and reg

75 Thus, activation of the decapping mRNP is restricted by access to 5'-proximal nucleotides,

76 uggest that these granules reflect defective mRNP remodeling during mRNA export and during cytoplasmi

77 the surveillance system recognizes defective mRNPs and stimulates their destruction by the RNA degrad

78 otein components are released from degrading mRNPs is unknown.

79 protein component of the splicing-dependent mRNP complex, or exon-exon junction complex (EJC), and a

80 machine, the p97-UBXD8 complex, disassembles mRNPs containing the AU-rich elements (AREs) bound by Hu

81 are segregated in an orderly fashion during mRNP maturation, indicating distinct recycling pathways

82 ct recycling pathways for SR proteins during mRNP maturation.

83 t mRNA from a scanning form into an effector mRNP particle by sequentially recruiting the CCR4-NOT co

84 ur findings define dynamic steps of effector mRNP assembly in miRNA-mediated silencing, and identify

85 er-associated nuclear protein) for efficient mRNP nuclear export and for efficient recruitment of NXF

86 impacts protein composition of the emerging mRNP.

87 understanding of past and current eukaryotic mRNP research.

88 formation on how export competent eukaryotic mRNPs are formed.

89 ly required to displace Mex67p from exported mRNPs, thus terminating export.

90 efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic

91 At the NPC cytoplasmic face, mRNP remodeling prevents its return to the nucleus and s

92 Since the discovery of the first mRNP component more than 40 years ago, what is known as

93 main, thus revealing a sorting mechanism for mRNP transition from splicing to export.

94 is an octa-zinc finger protein required for mRNP-gRNP docking, pre-mRNA and RECC loading, and RNP fo

95 NPC and might function as a docking site for mRNP during nuclear export.

96 s the first endosomal component specific for mRNP trafficking uncovering a new mechanism to couple mR

97 ilar to reported NPC translocation rates for mRNPs.

98 certed mechanisms that allow PV mRNA to form mRNP complexes that evade cellular mRNA degradation mach

99 oteins (such as hnRNPs) are required to form mRNPs capable of cytoplasmic localization.

100 on initiation inhibition and release of free mRNPs that are rapidly degraded or stored.

101 ' UTR exhibit a bimodal distribution in free-mRNPs and polysomes, indicating that the 3' UTR blocks t

102 ction at multiple steps of mRNA export, from mRNP biogenesis to their targeting and translocation thr

103 mRNA and is thought to dissociate Mex67 from mRNP upon translocation, thereby generating directional

104 sts that stress granules primarily form from mRNPs in preexisting P bodies, which is also supported b

105 inued synthesis and transport of the histone mRNP to the cytoplasm.

106 Ps, how they assemble and rearrange, and how mRNP composition differentially affects mRNA biogenesis,

107 ermediates, we detect significant changes in mRNP composition, marked by dissociation of eIF4G and PA

108 cally disordered proteins, key components in mRNP architectures, in the embryonic function of lsy-6 m

109 vo; however, the mechanistic role of Dbp5 in mRNP export is poorly understood and it is not known how

110 y positions, consistent with its function in mRNP organization and compaction as well as poly(A) tail

111 presence of polyadenylated uncapped mRNA in mRNPs was confirmed by separation into capped and uncapp

112 by sequestration of the core factor mTOR in mRNPs.

113 on with the functional approximately 680-kDa mRNP complex in which it normally resides on polysomes.

114 e spatiotemporal coordinated cascade leading mRNPs from their site of transcription to their site of

115 and their regulators localize to P body-like mRNP granules in the Caenorhabditis elegans germ line.

116 itively to a segment of mRNA of a linearized mRNP, passing through the NPC on its way to the cytoplas

117 tubule-associated protein capable of linking mRNP complexes to microtubules.

118 NA complexes, and emphasize that closed-loop mRNP formation via PABP-eIF4G interaction is non-essenti

119 raction supports the notion of a closed-loop mRNP, but the mechanistic events that lead to its format

120 The nonrandom distribution of major mRNP proteins observed in transcriptome-wide studies lea

121 After transport-competent mature mRNP export complexes are formed in the nucleus, their p

122 xport by facilitating the transfer of mature mRNPs from the nuclear interior to NPCs.

123 ed mechanism for stepwise assembly of mature mRNPs in the nucleus.

124 oplasmic mRNPs can assemble into large multi-mRNP assemblies or be permanently disassembled and degra

125 To investigate it, we labeled native mRNP particles in living Chironomus tentans salivary gla

126 Nontranslatable mRNPs may accumulate in P-bodies, which contain factors

127 stead form by condensation of nontranslating mRNPs in proportion to their length and lack of associat

128 Only MES identified the novel mRNP protein Nab6p and the tRNA transporter Los1p, which

129 latory REH2 and (H2)F1 subunits of the novel mRNP that may control specificity checkpoints in the edi

130 This novel mRNP targets a specific guanine-rich pentanucleotide in

131 THO surveys common landmarks in each nuclear mRNP to localize Sub2 for targeted loading of Yra1.

132 e new insights into the mechanism of nuclear mRNP export in live human cells.

133 we call ZNF-protein interacting with nuclear mRNPs and DBC1 (ZIRD)) as subunits of a novel protein co

134 lex, by facilitating the recognition of NXF1-mRNP complexes by DBP5 during translocation, thereby con

135 Analysis of mRNP complexes in K562 cells demonstrates in vivo associ

136 ve demonstrated that GRTH, as a component of mRNP particles, acts as a negative regulator of the tumo

137 d spermatids and functions as a component of mRNP particles, implicating its post-transcriptional reg

138 Xp54 functions to change the conformation of mRNP complexes, displacing one subset of proteins to acc

139 e a model whereby Yra1 terminates a cycle of mRNP assembly by Dbp2.

140 ide-bound state, allowing multiple cycles of mRNP remodeling by a single Dbp5 at the NPC.

141 ells, we have characterized the diffusion of mRNP complexes in the nucleus.

142 The diffusion of mRNP complexes is restricted to the extranucleolar, inte

143 ubiquitin signaling-dependent disassembly of mRNP promoted by the p97-UBXD8 complex to control mRNA s

144 assembly that entails controlled docking of mRNP and gRNP modules via specific base pairing between

145 ts one of the best-characterized examples of mRNP translocation.

146 Although the movement of mRNP complexes occurs without the expenditure of metabol

147 deling machine, in the dynamic regulation of mRNP disassembly.

148 NA degradation and in earlier remodelling of mRNP for entry into translation, storage or decay pathwa

149 litate spatial control of the remodelling of mRNP protein composition during directional transport an

150 bp5 mediates export by triggering removal of mRNP proteins in a spatially controlled manner.

151 rhaps by aiding in the assembly of a type of mRNP within P-bodies that is poised to reenter translati

152 rotein Nab2 changes the scanning behavior of mRNPs at the nuclear periphery, shortens residency time

153 Herein, we review the components of mRNPs, how they assemble and rearrange, and how mRNP com

154 s (mRNPs), but changes in the composition of mRNPs during posttranscriptional regulation remain large

155 changes in the intracellular composition of mRNPs in response to physical, chemical or developmental

156 the RNA helicase Upf1 allows disassembly of mRNPs undergoing nonsense-mediated mRNA decay (NMD).

157 The formation of mRNPs controls the interaction of the translation and de

158 tion inhibits mRNA export, with retention of mRNPs and NXF1 in punctate foci within the nucleus.

159 tein particles (mRNPs), the translocation of mRNPs through the nuclear pore complex (NPC), and the mR

160 elease from NPCs and retrograde transport of mRNPs was observed.

161 s, disassembly and completion of turnover of mRNPs undergoing NMD requires ATP hydrolysis by Upf1.

162 rrespond to a repositioning and unfolding of mRNPs before the actual translocation.

163 the variation in either PABP association or mRNP organization more generally.

164 ling target within stress granules and other mRNPs that accumulate during flooding stress responses.

165 4 activity, possibly through effects on PAB1-mRNP structure, and to be capable of retaining the CCR4-

166 These results indicate that the PAB1-mRNP structure is critical for PUF3 action.

167 romyces cerevisiae to follow single-particle mRNP export events with high spatial precision and tempo

168 t is sorted as a ribonucleoprotein particle (mRNP or locasome) to the distal tip of the bud where tra

169 mature messenger ribonucleoprotein particle (mRNP).

170 cytoplasm as complex mRNA-protein particles (mRNPs), and translocation through the nuclear pore compl

171 orted messenger ribonucleoprotein particles (mRNPs) and polysomes.

172 coded messenger ribonucleoprotein particles (mRNPs) and tubular endoplasmic reticulum (tER).

173 etent messenger ribonucleoprotein particles (mRNPs) are under the surveillance of quality control ste

174 into messenger ribonucleoprotein particles (mRNPs) in the nucleus.

175 ocation of mRNA-ribonucleoprotein particles (mRNPs) through nuclear pore complexes (NPCs) that are em

176 -loop messenger ribonucleoprotein particles (mRNPs) via eIF4F-poly(A)-binding protein 1 (Pab1) associ

177 ly of messenger ribonucleoprotein particles (mRNPs), the translocation of mRNPs through the nuclear p

178 into messenger ribonucleoprotein particles (mRNPs), their transport through nuclear pore complexes,

179 form messenger ribonucleoprotein particles (mRNPs), which are then actively remodeled during various

180 f pre-messenger ribonucleoprotein particles (mRNPs).

181 wn as messenger ribonucleoprotein particles (mRNPs).

182 urthermore, we show that Matr3 is part of PB mRNP complexes, is a regulator of miRNA-mediated gene si

183 Many peripherin mRNPs contain multiple mRNAs, possibly amplifying the to

184 hat the motility and targeting of peripherin mRNPs, their translational control, and the assembly of

185 Prior to export through the nuclear pore, mRNPs undergo several obligatory remodeling reactions.

186 the asymmetric synthesis of HO 1 (ASH1) pre-mRNP originates already cotranscriptionally and passes t

187 and support SF3b contribution from early pre-mRNP recognition to late steps in splicing.

188 g with their pre-mRNA-protein complexes (pre-mRNPs) and mRNA-protein complexes (mRNPs), allow the vis

189 s cofactors interact directly with premature mRNPs.

190 Mex67p functions as the principal mRNP export receptor in budding yeast.

191 uitment of activated S6K1 to newly processed mRNPs serves as a conduit between mTOR checkpoint signal

192 the RNA helicase DHX34 was found to promote mRNP remodelling, leading to activation of NMD.

193 n control of granule morphology and promotes mRNP stability in arrested oocytes.

194 The mechanism of transport of mRNA-protein (mRNP) complexes from transcription sites to nuclear pore

195 The aggregation of mRNA-protein (mRNP) complexes into PBs involves interactions between l

196 Gle1 to mediate remodeling of mRNA-protein (mRNP) complexes.

197 odies (P bodies) are conserved mRNA-protein (mRNP) granules that are thought to be cytoplasmic center

198 ssion occurs through a complex mRNA-protein (mRNP) system that stretches from transcription to transl

199 sequent remodeling of messenger RNA-protein (mRNP) complexes that occurs at the cytoplasmic side of t

200 SMG-2 marking of PTC-mRNPs is enhanced by SMG-3 and SMG-4, but SMG-3 and SMG-

201 ned and involve the formation of a quiescent mRNP, which can accumulate in cytoplasmic foci referred

202 matic eukaryotic cells assemble into related mRNPs that accumulate in specific cytoplasmic foci refer

203 ons in mRNA export and is thought to remodel mRNPs at the nuclear pore complex (NPC).

204 sts that the DEAD-box helicase Dbp5 remodels mRNPs at the NPC cytoplasmic face by removing Mex67 and

205 relative rates of translational repression, mRNP multimerization, and mRNA decay.

206 ations control the mRNA ribonucleoparticles (mRNPs) pipeline from synthesis to nuclear exit.

207 H2C is an mRNA-associated ribonucleoprotein (mRNP) subcomplex with editing substrates, intermediates,

208 nules are large messenger ribonucleoprotein (mRNP) aggregates composed of translation initiation fact

209 a model whereby messenger ribonucleoprotein (mRNP) assembly requires Dbp2 unwinding activity and once

210 ical program of messenger ribonucleoprotein (mRNP) assembly, but instead form by condensation of nont

211 rectionality of messenger ribonucleoprotein (mRNP) complex export from the nucleus remain largely und

212 ted beta-globin messenger ribonucleoprotein (mRNP) complex in both cultured K562 cells and erythroid-

213 of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SGs) and process

214 n vivo targets, messenger ribonucleoprotein (mRNP) complexes containing HuD were first immunoprecipit

215 associated with messenger ribonucleoprotein (mRNP) complexes during export and are released during tr

216 mRNAs exist in messenger ribonucleoprotein (mRNP) complexes, which undergo transitions during the li

217 otease-modified messenger ribonucleoprotein (mRNP) complexes.

218 other cellular messenger ribonucleoprotein (mRNP) components to ensure the primitive status of SSCs

219 s by regulating messenger ribonucleoprotein (mRNP) dynamics.

220 By use of messenger ribonucleoprotein (mRNP) immunopurification, we show that UBP1C constitutiv

221 ssembled into a messenger ribonucleoprotein (mRNP) particle; this is the functional form of the nasce

222 omponent of the messenger ribonucleoprotein (mRNP) particles of Xenopus oocytes.

223 cking sites and messenger ribonucleoprotein (mRNP) remodeling machinery right over the NPC's central

224 ts of the oskar messenger ribonucleoprotein (mRNP), proper localization of which is required for esta

225 sent in a c-mos messenger ribonucleoprotein (mRNP).

226 ciated with messenger RNA ribonucleoprotein (mRNP) complexes including stress granules, which are kno

227 assembles with messenger ribonucleoproteins (mRNP) in the nucleus and guides them through the nuclear

228 te with proteins to form ribonucleoproteins (mRNPs).

229 nally silenced messenger ribonucleoproteins (mRNPs) and serve as extensions of translation regulation

230 t of cytosolic messenger ribonucleoproteins (mRNPs) and was catalytically active on RNA.

231 ly synthesized messenger ribonucleoproteins (mRNPs) are matured.

232 At the NPC, messenger ribonucleoproteins (mRNPs) first encounter the nuclear basket where mRNP rea

233 tion of single messenger ribonucleoproteins (mRNPs) in human cells.

234 to specialized messenger ribonucleoproteins (mRNPs) localized in the germ (pole) plasm at the posteri

235 lear export of messenger ribonucleoproteins (mRNPs) through nuclear pore complexes (NPCs) is mediated

236 components of messenger ribonucleoproteins (mRNPs).

237 ing particles (messenger ribonucleoproteins [mRNPs]) move mainly along microtubules (MT).

238 ein complexes (messenger ribonucleoproteins [mRNPs]).

239 electron micrographs of giant Balbiani ring mRNPs.

240 DFMR1 and ppk1 mRNA are present in the same mRNP complex in vivo and can directly bind to each other

241 are not detectably associated with the same mRNPs.

242 orm foci containing translationally silenced mRNPs termed stress granules (SGs).

243 ge sites containing translationally silenced mRNPs that can be released to resume translation after s

244 storage depots for translationally silenced mRNPs until the cell signals for renewed translation and

245 r RNA, we observe that translation of single mRNPs stochastically turns on and off while they diffuse

246 decapping machinery recruitment to specific mRNPs and how their assembly into PBs is governed by the

247 splicing, is a major constituent of spliced mRNPs.

248 Assembly of stabilizing mRNP complexes in the nucleus prior to export may maximi

249 tor of translation, by resolving the stalled mRNP.

250 ating the translational activation of stored mRNPs and also for sorting certain mRNPs into germplasm-

251 ity in targeting to polysome-bound substrate mRNP was determined by testing the ability of full-lengt

252 ways release protein components of substrate mRNPs.

253 accumulation and raise the possibility that mRNP dynamics are posttranslationally regulated.

254 These data reveal that mRNP export, consisting of nuclear docking, transport, a

255 Franks et al. now show that mRNP remodeling is required even for the death of an mRN

256 We find that mRNPs exiting the nucleus are decelerated and selected a

257 struction of the export route indicates that mRNPs primarily interact with the periphery on the nucle

258 iptome-wide studies leads us to propose that mRNPs are organized into three major domains loosely cor

259 The mRNP complexes move freely by Brownian diffusion at a ra

260 ough the nuclear pore complex (NPC), and the mRNP remodeling events at the cytoplasmic side of the NP

261 r controlling interactions with Gle1 and the mRNP.

262 After ATP hydrolysis by Ded1, the mRNP exits stress granules and completes translation ini

263 We also describe how properties of the mRNP "interactome" lead to emergent principles affecting

264 This study of the mRNP proteome is the first step in allowing future exper

265 e underlying mechanism and regulation of the mRNP remodeling.

266 d in vivo demonstrated the importance of the mRNP to normal steady-state levels of beta-globin mRNA i

267 ep in gene expression is the turnover of the mRNP, which involves degradation of the mRNA and recycli

268 A biology, as trans-acting components of the mRNP.

269 anied by extensive structural changes of the mRNP.

270 equires Dbp2 unwinding activity and once the mRNP is properly assembled, inhibition by Yra1 prevents

271 ntrol mRNA export efficiency and release the mRNP from the NPC.

272 the Rae1*Nup98 complex directly binds to the mRNP at several stages of the mRNA export pathway.

273 Xp54-associated factor, RapA/B, binds to the mRNP complex in the cytoplasm.

274 connect the transcribing polymerase with the mRNP particle and help to integrate transcript elongatio

275 rted by the colocalization of CML38 with the mRNP stress granule marker RNA Binding Protein 47 (RBP47

276 ynamic equilibrium between polysomes and the mRNPs seen in P bodies.

277 plexity regions of protein components of the mRNPs.

278 e ongoing transcription and suggest that the mRNPs within dots may make a major contribution to the g

279 by the formation and rearrangement of their mRNPs.

280 These mRNPs are translationally silent, initiating translation

281 a nuclear basket component is mutated, these mRNPs still contain the nuclear export factor Yra1p.

282 ins unclear how Loc1p is recruited into this mRNP and why Loc1p is important for ASH1 mRNA localizati

283 We isolated this mRNP from mitochondria lacking gRNA-bound RNP (gRNP) sub

284 ese data suggest that the NTD contributes to mRNP remodeling events at the cytoplasmic face of the NP

285 The recruitment of TOP3beta to mRNPs was independent of RNA cis-elements and was couple

286 der of events for Dbp2 in co-transcriptional mRNP assembly.

287 distribute from polysomes to non-translating mRNPs, and recapping is all that is needed for their ret

288 get mRNAs on polysomes or in non-translating mRNPs, and the presence of polyadenylated uncapped mRNA

289 ranscripts from polysomes to non-translating mRNPs, where they accumulate in an uncapped but nonethel

290 In contrast, the dbp5-trapped mRNPs lack Yra1p.

291 matin remodeling complex as an unanticipated mRNP nuclear export surveillance factor that retains exp

292 initiated by stable assembly of untranslated mRNPs into core structures, which could provide sufficie

293 ete cytoplasmic foci into which untranslated mRNPs are assembled during stress, in this process.

294 Using the previously established VRP-mRNP tagging system, a new method to distinguish the hos

295 When mRNP complexes wander into dense chromatin, they tend to

296 Ps) first encounter the nuclear basket where mRNP rearrangements are thought to allow access to the t

297 However, whether mRNP assembly into a PB is important for translational r

298 Using an experimental approach in which mRNP formation in yeast is disturbed by the action of th

299 les, one for Myo4p and one each for zipcoded mRNP and tER.

300 We propose a model whereby zipcoded mRNP and/or tER ligands couple two Myo4p*She3p heterotri