ライフサイエンスコーパス: RRM

1 RRM deletion in adult mice was triggered by injecting ra

2 RRM, or RNA-recognition motif, domains are the largest c

3 RRMs are characterized by their alpha/beta sandwich topo

4 s, we infer phylogenies for more than 12,000 RRM domains representing more than 200 broadly sampled o

5 scattering to dissect the roles of the TIA-1 RRMs in RNA recognition.

6 al selection and induced fit of the U2AF(65) RRMs are complementary mechanisms for Py-tract associati

7 ring to demonstrate that the tandem U2AF(65) RRMs exhibit a broad range of conformations in the solut

8 CyP33 contains a PPIase and a RRM domain and regulates MLL1 function through HDAC recr

9 e, we present two interesting findings about RRM domain modifications, found by mapping known PTMs on

10 US and TDP-43, which rank 1st and 10th among RRM-bearing prion candidates, form cytoplasmic inclusion

11 This complex itself is unusual among RRMs, suggesting that it performs a specific function fo

12 that are important for RNA recognition by an RRM-containing protein.

13 ORRM4 contains an RRM domain at the N terminus and a Gly-rich domain at th

14 Snu17p exhibits an RRM domain that resembles a U2AF homology motif (UHM) an

15 Yeast Nop15 is an RRM protein that is essential for large ribosomal subuni

16 tic RRM proteins indicates that it is not an RRM domain but rather an all-helical protein with a fold

17 lved in the formation and dissociation of an RRM-RNA complex.

18 mechanism whereby sequences C-terminal to an RRM can influence RNA binding.

19 In addition to an RRM domain at the N terminus, ORRM3 carries a glycine-ri

20 inding to 3' ends requires the La domain and RRM, a conformationally flexible C terminus allows La to

21 tion with AtMSI4; and most of the associated RRM domain proteins also contain PWWP domains that are s

22 domain contains an xRRM, a class of atypical RRM first identified in the Tetrahymena thermophila telo

23 among SRA1p orthologs and against authentic RRM proteins indicates that it is not an RRM domain but

24 le differences in binding affinities between RRMs.

25 symmetric platform in which the RNA-binding RRM, LRR and NTF2-like domains are arranged on one face.

26 M is implicated in both RNA and CTD binding, RRM point mutations separated these two functions.

27 oth steric constraints in accommodating both RRMs simultaneously at adjacent sites, and also subtle d

28 However, mutations of both RRMs induced aggregation of the protein whereas mutation

29 dopts a compact structure, showing that both RRMs engage with the target 10-nt sequences to form the

30 In addition, we show by NMR that both RRMs of hnRNP A1 can bind simultaneously to a single bip

31 as slow, microsecond motions throughout both RRMs including the interdomain linker.

32 spectroscopy showed that the expanded Bruno RRM contains the familiar RRM fold of four antiparallel

33 This expanded Bruno RRM provides a new example of the features that are impo

34 so showed that a truncated form of the Bruno RRM, lacking the flexible N-terminal amino acids, forms

35 In this Bruno RRM, the deletion of 40 amino acids prior to the N-termi

36 ace, which typically mediates RNA binding by RRMs.

37 f RNA-recognition motifs (RRMs): a canonical RRM and a pseudo-RRM.

38 twined two-domain arrangement of a canonical RRM and second domain.

39 acids, forms a stable and complete canonical RRM, so that the loss of RNA binding activity cannot be

40 This domain adopts a novel non-canonical RRM fold with two additional flanking alpha-helices that

41 motifs, and a third C-terminus non-canonical RRM, specific to TEL proteins.

42 ids prior to the N-terminus of the canonical RRM resulted in a significantly decreased affinity of th

43 study of the complex and its two constituent RRMs.

44 Nito), the only other fly protein containing RRMs and a SPOC domain, acts together with Spen to posit

45 tructural model in which contiguous CsPABPN1 RRM monomers wrap around the RNA molecule creating a sup

46 However, while the CsPABPN1 RRM domain specifically binds poly(A), the full-length p

47 urally characterized both the PHD3 and CYP33 RRM domains and analyzed their binding to one another.

48 insight into the multiple functions of Cyp33 RRM and suggest a Cyp33-dependent mechanism for regulati

49 binds H3K4me3 (preferentially) and the CYP33 RRM domain at distinct sites.

50 The Cyp33 RRM domain folds into a five-stranded antiparallel beta-

51 of H3K4me3 to PHD3 and binding of the CYP33 RRM domain to PHD3 are mutually inhibitory, implying tha

52 The RNA-binding pocket of the Cyp33 RRM domain, mapped on the basis of NMR CSP and mutagenes

53 H3K4me3/2 and CyP33-RRM target different surfaces of MLL1-PHD3 and can bind

54 binding of the MLL1-PHD3 domain to the CyP33-RRM domain.

55 dular protein constructed from four domains (RRM, LRR, NTF2-like and UBA domains).

56 dular protein constructed from four domains (RRM, LRR, NTF2-like and UBA) that have been thought to b

57 is mediated by the RNA recognition domains (RRM) of serine/arginine-rich splicing factor 1 (SRSF1),

58 r the loss of RNA binding capacity of either RRM impairs splicing repression by hnRNP A1.

59 This work characterizes an expanded RRM, which is present in the Drosophila Bruno protein, a

60 the expanded Bruno RRM contains the familiar RRM fold of four antiparallel beta-strands and two alpha

61 the binding specificity of three MSI family RRM domains using a quantitative fluorescence anisotropy

62 mutations of conserved residues in the first RRM domain reduce FIR's affinity for FUSE, while analogo

63 ndependently of the interaction of the first RRM.

64 The interaction partners of each of the four RRMs of Prp24 and how these interactions direct U4/U6 pa

65 unequal division of labour between the four RRMs of PTB.

66 The presence of a functional RRM domain, but not ZnK domain was essential for AdRSZ21

67 Indeed, of 210 human RRM-bearing proteins, 29 have a putative prion domain, a

68 Our data highlight structural diversity in RRM-protein interactions, analogous to the one seen for

69 These experiments using the individual RRM domains from hnRNP LL confirm the role of this trans

70 probing, targeted inactivation of individual RRMs and single molecule analyses revealed an unequal di

71 of SL3(ESS3) using its RRM1 domain and inter-RRM linker only.

72 at Py tract variations select distinct inter-RRM spacings from a pre-existing ensemble of U2AF(65) co

73 ortunity to select compact or extended inter-RRM proximities from the U2AF(65) conformational pool.

74 Results of these studies suggest inter-RRM conformational plasticity as a possible means for U2

75 mity of the N and C termini within the inter-RRM configuration is sufficient to explain the action of

76 The disruption of the inter-RRM interaction or the loss of RNA binding capacity of e

77 The inter-RRM linker forms the lid of the nucleobase pocket and we

78 ker sequences or a deletion within the inter-RRM linker.

79 the beta-sheet surface of RRM1 and the inter-RRM linker; RRM2 does not contact the RNA.

80 A subpopulation adopts tight inter-RRM contacts, such as independently reported based on pa

81 ation, and mislocalization of Sm proteins is RRM-dependent.

82 ng of the protein toward G4 DNA requires its RRM domain.

83 d binds directly to TGE in vitro through its RRM domain.

84 RNA-binding activity residing outside of its RRMs.

85 ultiple independent binding sites within its RRMs, PABPC interacts with importin alpha, a component o

86 harboring a canonical RNA recognition motif (RRM) and a putative prion domain.

87 nds to the N-terminal RNA Recognition Motif (RRM) and induces a conformational change that prevents R

88 ABH8), which contains RNA recognition motif (RRM) and methyltransferase domains flanking its AlkB dom

89 ed protein carries an RNA recognition motif (RRM) at its C terminus and has therefore been named Orga

90 FIA is mediated by an RNA recognition motif (RRM) contained in the Rna15 subunit of the complex.

91 eaturing at least one RNA recognition motif (RRM) domain and a carboxyl-terminal region enriched in s

92 ycine-rich domain and RNA recognition motif (RRM) domain have a minor contribution and the glutamine-

93 8, interface with the RNA recognition motif (RRM) domain of Aly/REF.

94 The N-terminal RNA-recognition motif (RRM) domain of Cyp33 has been found to associate with th

95 rands from the single RNA recognition motif (RRM) domain of each subunit.

96 to interact with the RNA-recognition motif (RRM) domain of human nuclear Cyclophilin33 (CYP33).

97 ons of the N-terminal RNA Recognition Motif (RRM) domain of spliceosomal A protein of the U1 small nu

98 of SR45, and not the RNA recognition motif (RRM) domain, associate independently with both U2AF(35)

99 LIRP that harbours an RNA recognition motif (RRM) domain.

100 ggested to contain an RNA recognition motif (RRM) domain.

101 574-3p binds multiple RNA recognition motif (RRM) domains of hnRNP L, synergizes with miR-297, reduce

102 ernary complex of the RNA recognition motif (RRM) domains of Hrp1 and Rna15 bound to this pair of RNA

103 stigated how the four RNA recognition motif (RRM) domains of Polypyrimidine tract binding (PTB) prote

104 deletion (lacking two RNA recognition motif (RRM) domains) and is therefore missing antibody epitopes

105 r Prp24 contains four RNA Recognition Motif (RRM) domains, and functions to anneal U6 and U4 RNAs dur

106 They contain two RNA recognition motif (RRM) domains, which recognize a defined sequence element

107 AtMSI4 have distinct RNA recognition motif (RRM) domains, which we determined to be responsible for

108 PABPNs) with a single RNA recognition motif (RRM) flanked by an acidic N-terminus and a GRPF-rich C-t

109 2 XS domain adopts an RNA recognition motif (RRM) fold.

110 imilar to that of the RNA recognition motif (RRM) found in many RNA-binding proteins.

111 lso interact with the RNA recognition motif (RRM) in b/Prt1, and mutations in both subunits that disr

112 The RNA recognition motif (RRM) is the most abundant RNA-binding domain in eukaryot

113 ing their targets.The RNA Recognition Motif (RRM) is the most ubiquitous RNA binding domain.

114 ns one amino-terminal RNA recognition motif (RRM) known to bind uridine (U)-rich sequences.

115 Mice in which the RNA recognition motif (RRM) of one of the RNA binding motif-20 alleles was flox

116 The RNA Recognition Motif (RRM) type RNA binding protein Bruno is required for the

117 AdRSZ21 exhibits a RNA recognition motif (RRM), a CCHC type zinc finger domain (Zinc Knuckle, ZnK)

118 a domain and adjacent RNA recognition motif (RRM), the mechanisms by which La stabilizes diverse RNAs

119 s between RNA and the RNA recognition motif (RRM), which is one of the most common RNA binding domain

120 e soma and encodes an RNA recognition motif (RRM)-containing protein.

121 o a distinct clade of RNA Recognition Motif (RRM)-containing proteins, most of which are predicted to

122 et of the human eIF3b RNA recognition motif (RRM).

123 ich also include an "RNA recognition motif" (RRM) (residues 77-184).

124 ion structure of the RNA recognition motifs (RRM) domain of free human SRSF2 (residues 9-101).

125 Two consecutive RNA recognition motifs (RRM) of U2AF(65) recognize a polypyrimidine tract at the

126 proteins containing RNA recognition motifs (RRM) to the conserved terminal loop of pri-miR-7.

127 Tandem RNA recognition motifs (RRM)s of U2AF65 recognize polypyrimidine tract signals a

128 tains two N-terminal RNA recognition motifs (RRMs) (RRM1 and RRM2) and a 50-residue C-terminal RS (ar

129 We show that the RNA recognition motifs (RRMs) 3 and 4 of PTB can bind two distant pyrimidine tra

130 ith three N-terminal RNA recognition motifs (RRMs) and a C-terminal glutamine-rich (Q-rich) domain.

131 is composed of three RNA recognition motifs (RRMs) and a glutamine-rich domain and binds to uridine-r

132 r protein containing RNA recognition motifs (RRMs) and a SPOC domain, is required for optimal Wg sign

133 24 (Prp24) has four RNA recognition motifs (RRMs) and facilitates U6 RNA base-pairing with U4 RNA du

134 tructures of its two RNA recognition motifs (RRMs) in complex with short RNA.

135 ree highly conserved RNA recognition motifs (RRMs) in the absence of other clearly defined protein do

136 two tandemly arrayed RNA recognition motifs (RRMs) near the N terminus, followed by a basic hinge dom

137 The RNA recognition motifs (RRMs) of hnRNP LL were expressed individually, and both

138 The N-terminal RNA recognition motifs (RRMs) of PABPC1 are necessary for the direct interaction

139 ion encompassing the RNA recognition motifs (RRMs) of PSF using a previously uncharacterized, 70 resi

140 ues between the dual RNA recognition motifs (RRMs) recognize the central nucleotide, whereas the N- a

141 nsecutive N-terminal RNA recognition motifs (RRMs) separated from the C-terminal RRM.

142 ree highly conserved RNA recognition motifs (RRMs) whereas RNPC1 carries one.

143 wo unusually compact RNA recognition motifs (RRMs), and identifies the RNA recognition surface in Npl

144 RNA binding domains, RNA-recognition motifs (RRMs), and prion regions.

145 its second and third RNA recognition motifs (RRMs), with specificity for U-rich sequences directed by

146 HuD possesses three RNA recognition motifs (RRMs), ZBP1 contains two RRMs and four K homology (KH) d

147 vivo depends on its RNA recognition motifs (RRMs).

148 ptide contains three RNA recognition motifs (RRMs).

149 CELF1 contains three RNA recognition motifs (RRMs).

150 pendent on the PABPC RNA recognition motifs (RRMs).

151 roteins that possess RNA-recognition motifs (RRMs).

152 a, have two types of RNA-recognition motifs (RRMs): a canonical RRM and a pseudo-RRM.

153 consisting of tandem RNA recognition motifs (RRMs; RRM1-RRM2) and a C-terminal arginine-serine repeat

154 This approach can be applied to other multi-RRM domain proteins to assess binding site degeneracy an

155 ad previously been overlooked in other multi-RRM structures, although a careful analysis suggests tha

156 A discrimination possibly common to multiple RRMs as several prominent members display a similar rear

157 ude its beta-sheet face, forming an occluded RRM (oRRM) domain.

158 at the RRM in ORRM1 clusters with a clade of RRM proteins that are targeted to organelles.

159 Despite its abundance, diversity of RRM structure and function is generated by variations on

160 et of RRM 3, but also in a conserved loop of RRM 2.

161 st there are unique regulatory mechanisms of RRM function that have yet to be uncovered and that the

162 The five binding pockets of RRM recognize uridines with an unusual 5'-to-3' gradient

163 ing reveals a previously undescribed role of RRM-containing proteins as mitochondrial RNA editing fac

164 of RRMs 1 and 2, but leave the beta-sheet of RRM 3 exposed.

165 The beta-sheet of RRM 3 then influences U4/U6 pairing through interaction

166 RNAs cluster primarily in the beta-sheet of RRM 3, but also in a conserved loop of RRM 2.

167 These findings advance our understanding of RRM domain regulation, poly(A) recognition, and are rele

168 some inhibition highlights the uniqueness of RRM domain ubiquitination - RRM domain ubiquitination de

169 canonical RNA-binding faces (beta-sheets) of RRMs 1 and 2, but leave the beta-sheet of RRM 3 exposed.

170 large basic patch evident on the surface of RRMs 1 and 2 is part of a high affinity U6 RNA binding s

171 ng groove in the large lobe of SRPK1 and one RRM (RRM2) on the N-terminal flank of the RS domain.

172 Our results reveal that any one RRM in combination with a Q domain is necessary and suff

173 ifications, found by mapping known PTMs onto RRM domain alignments and structures.

174 y proteins within these bodies contain KH or RRM RNA-binding domains as well as low complexity (LC) s

175 The RNA recognition motif (or RRM) is a ubiquitous RNA-binding module present in appro

176 t the identification of ORRM4 (for organelle RRM protein 4) as a novel, major mitochondrial editing f

177 minus and has therefore been named Organelle RRM protein 1 (ORRM1).

178 tification of two proteins, ORRM2 (organelle RRM protein 2) and ORRM3 (organelle RRM protein 3), as t

179 rganelle RRM protein 2) and ORRM3 (organelle RRM protein 3), as the first members of the ORRM clade t

180 s rather different to that observed in other RRM-RNA structures and is structurally conserved in CstF

181 tes that OA may inhibit the binding of other RRM-containing protein/s necessary for miR-16 processing

182 We propose that other RRM proteins could act as metabolite sensors to couple g

183 ed RS domain of SRSF1 interacts with its own RRM, thus competing with U1-70K binding, whereas the hyp

184 asks nuclear import signals within the PABPC RRMs, thereby ensuring efficient cytoplasmic retention o

185 While some plastid RRM proteins are involved in other forms of RNA processi

186 d found that it does not have the postulated RRM (RNA recognition motif).

187 hat mutating the RNP1 motif in the predicted RRM domain in yeast eukaryotic initiation factor 3 (eIF3

188 omic resolution structure of any TIA protein RRM in complex with oligonucleotide.

189 /HCR1 closely cooperates with the eIF3b/PRT1 RRM and eIF1A on the ribosome to ensure proper formation

190 subunit-mRNA interaction and that the b/Prt1-RRM-j/Hcr1-a/Tif32-CTD module binds near the mRNA entry

191 ongly suggest that SR proteins with a pseudo-RRM frequently regulate splicing by competing with, rath

192 motifs (RRMs): a canonical RRM and a pseudo-RRM.

193 Furthermore, the isolated pseudo-RRM is sufficient to regulate splicing of about half of

194 ving the structure of the human SRSF1 pseudo-RRM bound to RNA, we discovered a very unusual and seque

195 s mode of binding is conserved in all pseudo-RRMs tested.

196 Although pseudo-RRMs are crucial for activity of SR proteins, their mode

197 PID directly inhibits the interaction of PSF RRMs with RNA, which is mediated through RRM2.

198 EMSA, ITC, and NMR studies show that PTB RRMs 1 and 2 bind the pyrimidine-rich internal loop of U

199 oteostasis of TAF15, which is the 2nd ranked RRM-bearing prion candidate, has been connected with ALS

200 complex between precursor miR-20b and Rbfox RRM shows the molecular basis for recognition, and revea

201 ence-specific binding of the conserved Rbfox RRM to miRNA precursors containing the same sequence mot

202 ecific C2H2 zinc finger and RNA recognition (RRM) domains.

203 he sigmaNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that sig

204 also called RNPC1 [RNA-binding region (RNP1, RRM) containing 1], is a target of the p53 family and mo

205 tion in the rnpc3 [RNA-binding region (RNP1, RRM) containing 3] gene.

206 ith RNA and within the RNP1 motif of SLIRP's RRM domain.

207 Importantly, a second RRM domain (RRM2) of RBM10 recognizes a C-rich sequence,

208 The second RRM adds affinity but does not contribute to binding spe

209 ed by the RNA-binding activity of the second RRM and involves an intronic element of the tau pre-mRNA

210 USE, while analogous mutations in the second RRM domain either destabilize the protein or have no eff

211 d Matrin3 by its interaction with the second RRM domain of the splicing regulator PTB.

212 The affinity of each separate RRM for polypyrimidine tracts is far weaker than that of

213 ing type II PABPs and an example of a single RRM domain protein that transitions from a homodimer to

214 eractions by polar amino acids in the single RRM domain of SLIRP and three neighbouring PPR motifs in

215 ants, that depends on the third TEL-specific RRM.

216 action of a racemic mixture (stereodivergent RRM) involving [4+2] cycloaddition.

217 Strikingly, RRM 2 forms extensive inter-domain contacts with RRMs 1

218 al nucleotide, whereas the N- and C-terminal RRM extensions recognize the 3' terminus and third nucle

219 motifs (RRMs) separated from the C-terminal RRM.

220 The N-terminal RRM domain by itself provides the editing activity of OR

221 nds FUSE as a dimer, and only the N-terminal RRM domain participates in nucleic acid recognition.

222 se either previously observed for N-terminal RRMs of Py tract-binding protein that lack interdomain c

223 binding function is modular: the N-terminal RRMs preferentially bind to short (U/C) tracts displayed

224 ot bind RNA as an individual domain and that RRM 2, 3, and 4 exhibit different RNA binding specificit

225 cations (PTMs), ProteomeScout, we found that RRM domains are also one of the most heavily modified do

226 The RRM domain of CsPABPN1 displays virtually the same three

227 The RRM domain provides the editing activity of ORRM4, where

228 The RRM domain, but not the catalytic module of Cyp33, binds

229 The RRM-domain proteins FCA and FPA have previously been cha

230 The RRM-SRPK1 contact residues control the folding of a crit

231 Although the RRM is implicated in both RNA and CTD binding, RRM point

232 t RNPC1 and HuR physically interact, and the RRM domain in RNPC1 and RRM3 in HuR are necessary for th

233 s in p63 3' UTR in vitro and in vivo and the RRM domain in RNPC1 is required for binding, and regulat

234 Both the RRM and N-terminal RS-rich region of Tra2beta were requi

235 NA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-l

236 splicing factor 1 (SRSF1), which bridges the RRM of U1-70K to pre-mRNA by using the surface opposite

237 stal structure of a construct comprising the RRM and AlkB domains shows disordered loops flanking the

238 elta5 (amino acids 1670-1962) containing the RRM, both induced comparable silencing in a tethering as

239 Conversely, the RRM domain and especially the UBA domain are more mobile

240 ation in the RRM of SRSF1 that disrupted the RRM-RRM interaction also inhibits the formation of splic

241 This result re-establishes the RRM as the primary RNA-binding domain of the hnRNP C tet

242 Specific mutation in the RRM of SRSF1 that disrupted the RRM-RRM interaction also

243 egions outside the PUF domain, including the RRM, enhance discrimination among targets.

244 esolution view of an important member of the RRM class of RNA-binding domains highlights the role of

245 s with the unfolding of a beta strand of the RRM domain and binding of the unfolded region to the doc

246 volving the L3 loop, N- and C-termini of the RRM domain are collectively important for determining se

247 beta strands and the beta2-beta3 loop of the RRM domain are involved in the interaction with PHD3.

248 a 1.9 A resolution crystal structure of the RRM domain of Cyp33 and describe the molecular mechanism

249 a basic alpha-helix at the N terminus of the RRM domain.

250 en the expanded functional repertoire of the RRM family, it was unknown whether TIA-1 RRM1 contribute

251 ty cannot be attributed to disruption of the RRM fold.

252 We solved the solution structures of the RRM in complex with poly(U) oligomers of five and seven

253 turally derived recognition consensus of the RRM with a thermodynamic description of its multi-regist

254 residues in the free and bound states of the RRM.

255 that alter the conformational states of the RRM.

256 the RIP-RIP domain or a region spanning the RRM domain of ORRM1 demonstrated that the RRM domain is

257 Using UV cross-linking, we showed that the RRM alone binds RNA, although a larger segment extending

258 Mapping data showed that the RRM and its flanking sequences in Delta5, but not the Ag

259 ng lower plants and monocots showed that the RRM and ZnK domains are evolutionarily conserved.

260 Our analyses reveal that the RRM domain is not restricted to eukaryotes and that all

261 he RRM domain of ORRM1 demonstrated that the RRM domain is sufficient for the editing function of ORR

262 n that have yet to be uncovered and that the RRM domain represents a model system for further studies

263 Phylogenetic analysis reveals that the RRM in ORRM1 clusters with a clade of RRM proteins that

264 cular dynamics simulations and show that the RRM RNA binding surface exists in different states and t

265 an alpha-helix immediately C-terminal to the RRM domain (helix C), which occludes the RNA binding sur

266 of this alpha3-helix by appending it to the RRM of the unrelated U1A protein and show that this fusi

267 the phospho-CTD-interacting domain up to the RRM) results in a 10-fold decrease in Yra1 recruitment t

268 ble linkers like beads on a string, with the RRM and LRR domains binding RNAs and the NTF2-like and U

269 its that disrupt their interactions with the RRM increase leaky scanning of an AUG codon.

270 7 by HopU1 required two arginines within the RRM, indicating that this modification may interfere wit

271 These structural differences between the RRMs were reinforced by the specificities of wild-type a

272 nformations exhibit few contacts between the RRMs, such as observed in the crystal structure.

273 to a 2:1 FIR(2)-FUSE complex mediated by the RRMs.

274 heir alpha/beta sandwich topology, and these RRMs use their beta-sheet as the RNA binding surface.

275 followed by a basic hinge domain and a third RRM near the C terminus.

276 the PpTEL1 C-terminus (including this third RRM) or only 16-18 amino acids within it seriously impai

277 n, suggesting a critical role for this third RRM.

278 Unique to this RRM family is the tyrosine-glutamine-phenylalanine (YQF)

279 Nam8 is composed of three RRM domains, flanked by N-terminal leader and C-terminal

280 for binding AU-rich fas sites, yet all three RRMs were required to bind a polyU RNA with high affinit

281 ort the crystal structure of the first three RRMs and the solution structure of the first two RRMs of

282 e for a TIA-1 construct comprising the three RRMs and revealed that its dimensions became more compac

283 sable for splicing regulation, and the three RRMs are required for splicing regulation of each target

284 serine-arginine (SR) protein family, has two RRM domains (RRM1 and RRM2) and a C-terminal domain rich

285 nition is determined by the first of the two RRM domains.

286 recognition motifs (RRMs), ZBP1 contains two RRMs and four K homology (KH) domains that either increa

287 gate the recognition of RNA by the first two RRMs of CELF1.

288 and the solution structure of the first two RRMs of Prp24.

289 The entire RBD, comprised of two RRMs and a glycine-rich linker, is essential for ESE bin

290 municate with each other in bringing the two RRMs close together to form the complex with RNA.

291 n that of PTB1:34, and simply mixing the two RRMs does not create an equivalent binding platform.

292 the architecture and organization of the two RRMs is essential to hnRNP A1 function.

293 rms a single globular structure, but the two RRMs of Npl3 are not equivalent, with the second domain

294 inding to G+U-rich RNAs observed for the two RRMs of Npl3 is masked in the full-length protein by a m

295 tion, the relative arrangement of the U2AF65 RRMs and the energetic forces driving polypyrimidine tra

296 he uniqueness of RRM domain ubiquitination - RRM domain ubiquitination decreases in response to prote

297 eosome components, using solely this unusual RRM.

298 2 forms extensive inter-domain contacts with RRMs 1 and 3.

299 that Prp24 binds free U6 RNA primarily with RRMs 1 and 2, which may remodel the U6 secondary structu

300 lap of ubiquitination and acetylation within RRM domains, suggesting the possibility for ubiquitinati