ライフサイエンスコーパス: U2 snRNP

1 U2 snRNPs depleted of Rds3p fail to form stable presplic

2 leads to the demonstration that the core 17S U2 snRNP components, SF3b145 and SF3b49 bind directly to

3 ntribute to conversion of the 12S to the 17S U2 snRNP particle, which is essential for spliceosome as

4 ts intrinsic interaction with Caper alpha, a U2 snRNP auxiliary factor-related protein previously imp

5 SF3b is a U2 snRNP-associated protein complex essential for splice

6 of the adenine is critical in formation of a U2 snRNP-containing complex on a minimal branch-site oli

7 both minimal requirements for formation of a U2 snRNP-substrate RNA complex, here designated the Amin

8 y interacts with components of the activated U2 snRNP and enhances binding of U2 snRNP to the branch

9 f the branch site is essential for anchoring U2 snRNP to pre-mRNA.

10 and depends on the activities of both U1 and U2 snRNP proteins to activate splicing.

11 ed for maximal binding of both U1 snRNPs and U2 snRNPs to the 5' and 3' splice site, respectively, su

12 SNF is a protein that is found in the U1 and U2 snRNPs (small nuclear ribonucleoproteins) of Drosophi

13 tion of NPL3 reduces the occupancy of U1 and U2 snRNPs at genes whose splicing is stimulated by Nbl3.

14 tent with Prp5 being a bridge between U1 and U2 snRNPs at the time of pre-spliceosome formation.

15 del for spliceosome assembly in which U1 and U2 snRNPs first associate with the spliceosome in the E

16 ay a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex.

17 Communication between U1 and U2 snRNPs is critical during pre-spliceosome assembly; y

18 re required for communication between U1 and U2 snRNPs whether this interaction is across introns or

19 complex stabilizes the association of U1 and U2 snRNPs with pre-mRNA.

20 r (snf), which encodes a component of U1 and U2 snRNPs, participates in this RNA splicing control.

21 vivo, these proteins segregate to the U1 and U2 snRNPs, respectively, where they bind distinct RNA ha

22 the expression of core components of U1 and U2 snRNPs, splicing regulators and other post-transcript

23 protein component of the spliceosomal U1 and U2 snRNPs.

24 ns coilin does not associate with the U1 and U2 snRNPs.

25 II (RNAPIIO) is associated with U1 or U1 and U2 snRNPs.

26 each physically associated with both U1 and U2 snRNPs; Prp5 contains distinct U1- and U2-interacting

27 racts with U2 even in the absence of another U2 snRNP protein, U2A'.

28 basis of ATP use for the interaction between U2 snRNP and the branchpoint is unclear, and, in particu

29 Surprisingly, this element binds U2 snRNP, although it is derived from an intronless mRNA

30 to the target exon splice sites but blocked U2 snRNP assembly in HeLa nuclear extract.

31 study interactions between the UACUAAC box, U2 snRNP, and Prp5p, a DEAD box protein necessary for pr

32 o dependent on U1 snRNP and is stabilized by U2 snRNP.

33 s not comparably enriched in Lea1-containing U2 snRNPs from tgs1Delta cells.

34 forms an ATP-dependent complex that contains U2 snRNP.

35 In contrast, U2 snRNP recruitment, as well as cotranscriptional splic

36 otein complex which can exchange with a core U2 snRNP and which is necessary for U2 snRNP function in

37 ndent activity that releases or destabilizes U2 snRNP from branch sequences.

38 ddition to its established function in early U2 snRNP recruitment, SF3b plays a role in later maturat

39 molecules bound to the intron could enhance U2 snRNP recruitment to the branch point sequence.

40 splicing in the absence of the non-essential U2 snRNP protein Snu17p.

41 adjacent to the 3' splice site to facilitate U2 snRNP recruitment.

42 tion involves binding of the splicing factor U2 snRNP auxiliary factor (U2AF or MUD2 in Saccharomyces

43 uctures of the heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) have revealed two unexp

44 m yeast stably associates with at least five U2 snRNP proteins, Cus1p, Hsh49p, Hsh155p, Rse1p, and Is

45 r normal cellular Cus1p accumulation and for U2 snRNP recruitment in splicing.

46 ting that U2A', but not SNF, is critical for U2 snRNP function.

47 pliceosomal complex, E, and is essential for U2 snRNP binding in the spliceosomal complex A.

48 h a core U2 snRNP and which is necessary for U2 snRNP function in prespliceosome assembly.

49 ty, suggesting that SNF is not necessary for U2 snRNP function in vivo.

50 of the commitment complex, the precursor for U2 snRNP addition.

51 s an essential splicing protein required for U2 snRNP addition to the spliceosome.

52 stone acetyltransferase Gcn5 is required for U2 snRNP association with the branchpoint.

53 to position a DEAD box protein required for U2 snRNP binding at the pre-mRNA branchpoint region.

54 The BPS is not required for U2 snRNP binding in the E complex.

55 ginine-serine-rich (RS) region, required for U2 snRNP recruitment and splicing.

56 ic regulatory element and uncover a role for U2 snRNP in the regulation of alternative splicing.

57 binding site and an upstream branch site for U2 snRNP binding.

58 12 snRNP, which functionally substitutes for U2 snRNP in the minor spliceosome.

59 In the absence of ATP, when complex E forms, U2 snRNP association is unrestricted.

60 red for splice site pairing independent from U2 snRNP binding to the pre-mRNA.

61 A.Z are especially dependent on a functional U2 snRNP (small nuclear RNA [snRNA] plus associated prot

62 idence that this complex contains functional U2 snRNP and that this snRNP is required for E complex a

63 splicing to proceed on a substrate that had U2 snRNP already bound.

64 protein present in the 17S form of the human U2 snRNP.

65 orylation of the RS domain led to a block in U2 snRNP binding to the substrate.

66 es an ATP-dependent conformational change in U2 snRNP that exposes the BBR.

67 s as a "decoy" acceptor site that engages in U2 snRNP-dependent but nonproductive splicing complexes

68 xes, implicate accessory splicing factors in U2 snRNP function, and support SF3b contribution from ea

69 In sharp contrast to its essential role in U2 snRNP recruitment in vitro, the RS domain on the Dros

70 A1, Pcbp1, and RBM39 stabilizes or increases U2 snRNP recruitment, enhances spliceosome A complex for

71 ral U1 snRNP protein U1-70k, or the integral U2 snRNP protein SF3a(60), has no effect.

72 s U1 snRNP-associated (U1A) whereas RNP-3 is U2 snRNP-associated (U2B'').

73 in vivo and, like its human counterpart, is U2 snRNP specific.

74 was detected by incubating human 32P-labeled U2 snRNP in micrococcal nuclease-treated HeLa nuclear ex

75 pliceosomal complex when rearrangements lock U2 snRNP onto the pre-mRNA.

76 ous to SAP 145, a component of the mammalian U2 snRNP that interacts with pre-mRNA.

77 ns in spliceosome assembly within the mature U2 snRNP (small nuclear ribonucleoprotein particle), and

78 The multimeric U2 snRNP protein complexes SF3a and SF3b are required fo

79 enzyme; activity was also observed on native U2 snRNPs.

80 imidine tract binding protein (PTB), but not U2 snRNP auxiliary factor (U2AF), and that binding of PT

81 tein complex with a tightly bound U1 but not U2 snRNP.

82 t sudemycin E interferes with the ability of U2 snRNP to maintain an H3K36me3 modification in activel

83 h prior to and subsequent to the addition of U2 snRNP to the 3' acceptor.

84 de mechanistic insights into the assembly of U2 snRNP.

85 K4me3 levels by siRNA reduced association of U2 snRNP components with chromatin and, more importantly

86 The association of U2 snRNP with the pre-mRNA branch region is a critical s

87 the first of which is the stable binding of U2 snRNP at the pre-mRNA branchpoint.

88 tors are not necessary for stable binding of U2 snRNP per se, but rather are necessary for accessibil

89 mRNA splicing involves the stable binding of U2 snRNP to form the prespliceosome.

90 Although U2 stem IIc inhibits binding of U2 snRNP to pre-mRNA during assembly, we found that weak

91 some assembly by preventing tight binding of U2 snRNP to pre-mRNA.

92 the presence of ATP, and supports binding of U2 snRNP to the 3' end of introns, yielding a weak ATP-i

93 edly was not dependent upon prior binding of U2 snRNP to the branch point.

94 e activated U2 snRNP and enhances binding of U2 snRNP to the branch site located upstream of the exon

95 complex followed by ATP-dependent binding of U2 snRNP to the branchpoint sequence (BPS) in the A comp

96 A splicing reaction is the stable binding of U2 snRNP to the branchpoint sequence (BPS) to form the A

97 Pases, is required for the stable binding of U2 snRNP to the pre-mRNA branchpoint.

98 istinguishable mechanisms for the binding of U2 snRNP to the pre-mRNA, including U2AF-dependent and -

99 lone is insufficient for specific binding of U2 snRNP.

100 ex and recruits and/or stabilizes binding of U2 snRNP.

101 ssential splicing factor SF3, a component of U2 snRNP.

102 d pre-mRNA, underscoring the conservation of U2 snRNP proteins that function in spliceosome assembly.

103 gion spanning from immediately downstream of U2 snRNP's binding site at the BPS to just beyond the 3'

104 Entry of U2 snRNP into the spliceosome is initiated by interactio

105 prior data showing that loss of function of U2 snRNP components can interfere with cell growth and i

106 Surprisingly, inactivation of U2 snRNP also decreased U11 binding to the NRS.

107 Notably, pharmacologic inhibition of U2 snRNP activity phenocopied PHF5A knockdown in GSCs an

108 determined that U1 snRNP-directed loading of U2 snRNP onto the branch site as well as efficient trans

109 Recruitment of U2 snRNP to the branch point sequence of introns is a ne

110 raphy and identified as the large subunit of U2 snRNP auxiliary factor (U2AF).

111 lex forms with stoichiometric association of U2 snRNPs and the U2 snRNA is base-paired to the pre-mRN

112 of nuclear export or targeted degradation of U2 snRNPs caused a marked decrease in the levels of U2 s

113 he anchoring site, has no apparent effect on U2 snRNP binding.

114 E7107 has no apparent effect on U2 snRNP integrity.

115 r formation for either its vital function or U2 snRNP assembly.

116 2 snRNP, as H2A.Z loss results in persistent U2 snRNP association and decreased recruitment of downst

117 ied role for phosphorylated SR proteins post-U2-snRNP addition coincides with the recruitment of the

118 dition, the antibody to PRPF40A precipitated U2 snRNPs from nuclear extracts, indicating that PRPF40A

119 teracts with U2AF65 and SF3b155 and promotes U2 snRNP recruitment to the branch point.

120 teins associate with one another in purified U2 snRNP.

121 x and then interacts with SAP 155 to recruit U2 snRNP to the BPS.

122 ecognizing the 3' splice site and recruiting U2 snRNP.

123 nchpoint and the 3' splice site and recruits U2 snRNP to the branch site at an early step in spliceos

124 polypyrimidine tract of the intron, recruits U2 snRNP to the branch point sequence by interacting wit

125 The resultant U2 snRNP particle migrates exceptionally slowly in polya

126 n of the U2 small nuclear ribonucleoprotein (U2 snRNP).

127 e sites into a splicing pattern after stable U2 snRNP association to the branch point.

128 ATP-dependent step results in highly stable U2 snRNP binding to the BPS in the A complex.

129 n of the polypyrimidine tract and subsequent U2 snRNP assembly at the branch point.

130 -the hU2AF65 RS domain is required to target U2 snRNP to the branch site and the hU2AF35 RS domain is

131 anchpoint and the 3' splice site and targets U2 snRNP to the branch site at an early step in spliceos

132 We conclude that U2 snRNP plays a nonsplicing role in histone mRNA matura

133 Finally, we show that U2 snRNP associates with histone pre-mRNAs in vivo.

134 e chromatin immunoprecipitations showed that U2 snRNPs physically interact with nucleosomes.

135 The U2 snRNP component SAP 155 contacts pre-mRNA on both sid

136 The U2 snRNP promotes prespliceosome assembly through intera

137 The U2 snRNP-intron interaction is disrupted in all complexe

138 reby Cus2p first helps Prp5p to activate the U2 snRNP for prespliceosome formation but then is displa

139 p9, Prp11, Prp21, and Prp5 in activating the U2 snRNP for assembly into the pre-spliceosome.

140 int binding proteins Mud2p and Bbp1p and the U2 snRNP protein Prp11p by two-hybrid assays.

141 an interface between U4/U6 di-snRNP and the U2 snRNP SF3b-containing domain, which also transiently

142 rokering an interaction between PRP5 and the U2 snRNP that depends on correct U2 RNA structure.

143 tion, the proteins U2AF35 and U2AF65 and the U2 snRNP, are able to recognize alternative candidate si

144 ent in facilitating interactions between the U2 snRNP complex and ATP-dependent helicases, we examine

145 ined with deletion of the genes encoding the U2 snRNP components Lea1 or Msl1.

146 t are distinct from the binding site for the U2 snRNP protein p14, mapped to amino acids 396-424 of S

147 dependent on U2AF65, and is required for the U2 snRNP-branchpoint interaction.

148 Mutations in the U2 snRNP component SF3B1 are prominent in myelodysplasti

149 e U2B" counterpart, Sans-Fille (SNF), in the U2 snRNP is dispensable for viability, suggesting that S

150 kely promotes a conformational change in the U2 snRNP.

151 were cross-linked to 32P-nucleotides in the U2 snRNP.

152 nt spliceosomal rearrangements involving the U2 snRNP, as H2A.Z loss results in persistent U2 snRNP a

153 n occurs without ATP in extracts lacking the U2 snRNP protein Cus2p.

154 proteins, Prp5p and yUAP/Sub2p, mediate the U2 snRNP-branchpoint interaction.

155 prevented from binding to the pre-mRNA, the U2 snRNP can no longer be recruited and the following ex

156 lso results in persistent association of the U2 snRNP and a severe defect in the association of downs

157 ding six proteins that are components of the U2 snRNP and required for A complex formation.

158 The large subunit of the U2 snRNP associated factor (U2AF65), which is essential

159 n (U1 70K) and with the small subunit of the U2 snRNP auxiliary factor (U2AF35) in live-cell nuclei.

160 Although the protein components of the U2 snRNP have been identified, their individual contribu

161 11, and Prp21 influence the structure of the U2 snRNP in a manner that alters the accessibility of th

162 The 3' region of the U2 snRNP is flexibly attached to the SF3b-containing dom

163 blish Rds3p as an essential component of the U2 snRNP SF3b complex and suggest a new link between the

164 and Prp21, are necessary for addition of the U2 snRNP to the pre-mRNA in an early step of spliceosome

165 Recruitment of the U2 snRNP to the pre-mRNA is an essential step in spliceo

166 important for the stable association of the U2 snRNP with pre-mRNA.

167 ized by the ATP-dependent association of the U2 snRNP with the branch point.

168 a and human proteins suggest that two of the U2 snRNP-specific proteins, U2A' and U2B", function excl

169 ent on the integrity and conformation of the U2 snRNP.

170 cruitment of SR proteins, and binding of the U2 snRNP.

171 RNP proteins bind to the 5' stem-loop of the U2 snRNP.

172 -SL4 interacts with the SF3A1 protein of the U2 snRNP.

173 nonhistone methyltransferase that primes the U2 snRNP for interaction with SMN.

174 SF3b1 plays a key role in recruiting the U2 snRNP to the BS.

175 cognizes the 3' splice site and recruits the U2 snRNP to the branch point.

176 We show that the U2 snRNP protein SAP 155 UV cross-links to pre-mRNA on b

177 Friend et al. now report that the U2 snRNP, required for pre-mRNA splicing, is also requir

178 oteins and the pre-mRNA, indicating that the U2 snRNP-intron interaction is Prp43's major target.

179 ng of the 2'-O-methyl oligonucleotide to the U2 snRNP in yeast cell extract was assayed by gel electr

180 s determine splicing efficiency prior to the U2 snRNP-BPS interaction.

181 linked to interactions of alphaCPs with the U2 snRNP complex and may be mediated by cooperative inte

182 ranch point sequence by interacting with the U2 snRNP protein SF3b155.

183 Sudemycin E induces a dissociation of the U2 snRNPs and decreases their interaction with nucleosom

184 antisense morpholino oligonucleotide or the U2-snRNP-inactivating drug spliceostatin A unless U1 ant

185 remodeling, which exposes the BBR for tight U2 snRNP binding to pre-mRNA.

186 C hnRNP protein cross-linking to U2 snRNP was efficiently competed by a mini-RNA correspo

187 -as PRMT9-binding partners, linking PRMT9 to U2 snRNP maturation.

188 bserved cross-linking of C hnRNP proteins to U2 snRNP was efficiently competed by excess U2 RNA and b

189 terfering with the spliceosome subsequent to U2 snRNP addition.

190 concurrently by two molecules of U2AF or two U2 snRNPs, so none of the components are restricted.

191 The pre-mRNA splicing factor U2AF (U2 snRNP auxiliary factor) has an essential role in 3' s

192 The splicing factor U2AF (U2 snRNP auxiliary factor) is a heterodimer with subunit

193 eterodimeric pre-mRNA splicing factor, U2AF (U2 snRNP auxiliary factor), plays a critical role in 3'

194 he splicing factor SF3b that associates with U2 snRNP and is recruited to prespliceosomal complexes.

195 by an interaction (direct or indirect) with U2 snRNP bound at the BPS and by a direct interaction wi

196 .Z shows extensive genetic interactions with U2 snRNP-associated proteins, and RNA sequencing (RNA-se

197 that was found to associate physically with U2 snRNP.

198 d spliceosomal complex A, is associated with U2 snRNPs, and colocalizes with splicing factors in nucl

199 cts, indicating that PRPF40A associates with U2 snRNPs.

200 east protein (YU2B") is a component of yeast U2 snRNP, and it is related to other members of the UIA-