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 rmediate state, and unfolded state for ETR-3 RRM-3, which has canonical RRM fold.

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

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

9 A RRM-U4 RNA structure reveals a unique RNA-binding mechan

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

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

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

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

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

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

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

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

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

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

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

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

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

23 The PUM-HD and RRM domains act in concert to determine RNA-binding spec

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

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

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

27 le differences in binding affinities between RRMs.

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

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

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

31 emical shift deviations are observed in both RRMs, suggesting both play a role in binding the A2RE11.

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

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

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

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

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

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

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

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

40 ace, which typically mediates RNA binding by RRMs.

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

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

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

44 d state for ETR-3 RRM-3, which has canonical RRM fold.

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

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

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

48 ploy aromatic residues outside the canonical RRM RNA-binding motifs to encase and wrench open the RNA

49 study of the complex and its two constituent RRMs.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

68 can shed more light on unfolding events for RRM-containing proteins.

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

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

71 hnRNPA2 RRMs bind the minimal rA2RE11 weakly but at least, and m

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

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

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

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

76 ies, we find that each of the two individual RRMs retain the domain structure observed in complex wit

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

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

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

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

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

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

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

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

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

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

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

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

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

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

91 We also show that a MARF1 RRM plays an essential role in enhancing its endonucleas

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

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

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

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

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

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

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

99 8, interface with the RNA recognition motif (RRM) domain of Aly/REF.

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

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

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

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

104 protein SRRP1 and two RNA Recognition Motif (RRM) domain proteins, CP33C and CP33B, were enriched wit

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

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

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

108 574-3p binds multiple RNA recognition motif (RRM) domains of hnRNP L, synergizes with miR-297, reduce

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

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

111 on connecting the two RNA recognition motif (RRM) domains of U2AF2 mediates autoinhibitory intramolec

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

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

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

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

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

117 2 XS domain adopts an RNA recognition motif (RRM) fold.

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

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

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

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

122 ort a mutation in the RNA recognition motif (RRM) of CSTF2 that changes an aspartic acid at position

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

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

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

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

127 In this study, a RNA recognition motif (RRM)-containing protein, BmLARK, was identified and demo

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

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

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

131 vergent PUM-HD and an RNA recognition motif (RRM).

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

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

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

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

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

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

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

139 TIA1 contains three RNA recognition motifs (RRMs) and a C-terminal low-complexity domain, sometimes

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

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

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

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

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

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

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

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

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

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

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

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

152 of the tandem U2AF2 RNA recognition motifs (RRMs).

153 ptide contains three RNA recognition motifs (RRMs).

154 ne/arginine (SR) and RNA recognition motifs (RRMs).

155 CELF1 contains three RNA recognition motifs (RRMs).

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

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

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

159 HuR contains three RNA recognition motifs (RRMs): a tandem RRM1 and 2, followed by a flexible linke

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 so determined crystal structures of the Puf1 RRM domain that identified a dimerization interface.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

216 Thus, these data indicate that TbRGG2 RRM can bind and remodel several RNA substrates suggesti

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

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

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

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

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

222 These findings suggest that RRM interactions with specific recognition sequences alo

223 The RRM domain of CsPABPN1 displays virtually the same three

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

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

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

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

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

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

230 ERV RNA and Xist A-repeat bind the RRM domains of Spen in a competitive manner.

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

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

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

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

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

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

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

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

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

240 376 residue (K376) of G3BP1, which is in the RRM RNA binding domain, was acetylated.

241 ide chains altering RNA binding sites in the RRM.

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

243 Cooperative action of the RRM and PUM-HD identifies a new mechanism by which multi

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

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

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

247 tes binding to UAAU, and dimerization of the RRM domain favors binding to dual UAAU motifs rather tha

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 modified the electrostatic potential of the RRM leading to a greater affinity for RNA.

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

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

256 that alter the conformational states of the RRM.

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

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

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

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

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

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

263 Here we show that the RRM domain of the essential kRNA-editing factor TbRGG2 b

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

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

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

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

268 e other ALS-linked mutations adjacent to the RRM domains that also disrupt RNA binding and greatly en

269 A region C-terminal to the RRM mediates TbRGG2 dimerization, enhancing RNA binding.

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

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

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

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

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

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

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

277 of an open, side-by-side arrangement of the RRMs.

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

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

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

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

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

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

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

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

286 m(6)A reader protein that binds RNA through RRM and Arg-Gly-Gly (RGG) motifs.

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

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

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

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

291 number of RNA binding domains, including two RRMs and multiple LOTUS domains.

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

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

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

295 oscopy reveals distinct functions of the two RRMs in TDP-43 NB formation.

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

297 nique RNA-binding mechanism in which the two RRMs of the dimer employ aromatic residues outside the c

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

299 eosome components, using solely this unusual RRM.

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