ライフサイエンスコーパス: U2AF(65)

1 U2AF65 binds specifically to 3' splice sites, but previo

2 U2AF65 binds to RNA at the polypyrimidine tract, whereas

3 U2AF65 contains an RNA binding domain, required for inte

4 U2AF65 directly contacts the polypyrimidine tract and is

5 relative molecular mass (Mr 65K) of 65,000 (U2AF65) binds to the poly(Y) tract, whereas the role of

6 A U2AF65 fusion named T-RS interacts with the nonphosphory

7 synthesizing a transcript segment that is a U2AF65 binding site.

8 ed from the high resolution coordinates of a U2AF65 deletion variant bound to RNA.

9 rometry were used to show that rather than a U2AF65/U2AF35-like heterodimer, Mud2p forms a complex wi

10 1 sequences are required for MBNL1-activated U2AF65 binding.

11 several SR proteins but also with U1-70K and U2AF65, proteins associated with 5' and 3' splice sites,

12 to FACT and the splicing factors SF2/ASF and U2AF65.

13 n JMJD6 and U2AF65, revealing that JMJD6 and U2AF65 co-regulated a large number of alternative splici

14 gs reveal an intimate link between JMJD6 and U2AF65 in alternative splicing regulation, which has imp

15 RNA-dependent interaction between JMJD6 and U2AF65, revealing that JMJD6 and U2AF65 co-regulated a l

16 Furthermore, MBNL1 and U2AF65 appear to compete by binding to mutually exclusiv

17 This suggests that MBNL1 and U2AF65 play a role in nuclear export of expHTT RNA.

18 of ATXN1 with the splicing factors RBM17 and U2AF65.

19 s for 14-3-3, and splicing factors RBM17 and U2AF65.

20 ntaining proteins such as SC35, ASF/SF2, and U2AF65, restored the splicing activity of the Sip1-immun

21 the SR domains of the SR proteins SRP75 and U2AF65, via fusion to a heterologous MS2 RNA binding pro

22 icated in selection, the proteins U2AF35 and U2AF65 and the U2 snRNP, are able to recognize alternati

23 intron to bind to a splicing factor such as U2AF65, as determined by an RNA electrophoretic mobility

24 Early in mammalian spliceosome assembly, U2AF65 binds to the pyrimidine tract between the BPS and

25 of Ataxin-1 with the spliceosome-associated U2AF65 and the adaptor 14-3-3 proteins.

26 Thus, U2AF35 functions as a bridge between U2AF65 and the enhancer complex to recruit U2AF65 to the

27 2AF35 directly mediates interactions between U2AF65 and proteins bound to the enhancers.

28 e ESS showed that the U-rich 5' region binds U2AF65 and polypyrimidine tract binding protein, the C-r

29 We provide evidence that both U2AF65 and PRP19C are required for CTD-dependent splicin

30 ining the consensus U2AF65 binding site, but U2AF65 was not displaced by a nonconsensus RNA.

31 nd dynamics of 3' splice site recognition by U2AF65 and the role of U2AF35 in the U2AF heterodimer, w

32 e similarity to the previously characterized U2AF65-binding domain of SF1.

33 RNA oligonucleotide containing the consensus U2AF65 binding site, but U2AF65 was not displaced by a n

34 In contrast, U2AF65 is more loosely bound in C28 transcription comple

35 tions that strengthen the stem-loop decrease U2AF65 binding affinity and also repress exon 5 inclusio

36 lymerase II may function not only to deliver U2AF65 to the nascent transcript but also to modulate ef

37 ete, <20 nt poly(A) tail in cells expressing U2AF65.

38 the large subunit of the U2 auxiliary factor U2AF65.

39 The splicing and nuclear export factor U2AF65 has the opposite effect, decreasing expHTT nuclea

40 s with the 3' splice site recognition factor U2AF65 and recruits it to the p21(Cip1) gene and mRNA.

41 in hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites.

42 The mammalian splicing factor U2AF65 binds to the polypyrimidine tract adjacent to the

43 cooperative interaction with splicing factor U2AF65 bound to an adjacent polypyrimidine tract (PPT) f

44 directly with the essential splicing factor U2AF65 for binding at the 3' end of intron 4.

45 , pre-mRNA for the essential splicing factor U2AF65 sometimes is spliced to produce an RNA that inclu

46 e sampled by the multidomain splicing factor U2AF65 using complementary nuclear magnetic resonance sp

47 interaction of the essential splicing factor U2AF65 with the pre-mRNA polypyrimidine tract.

48 h the well studied mammalian splicing factor U2AF65, which binds to the adjacent polypyrimidine (PY)

49 ion and interaction with the splicing factor U2AF65, which promotes mRNA processing and the stabiliza

50 nal strong cross-link to the splicing factor U2AF65.

51 d with decreased cross-linking of the factor U2AF65, whereas regulation at step 2 is correlated with

52 e subunit of the U2 snRNP associated factor (U2AF65), which is essential for splicing of human intron

53 f the U2 small nuclear RNA auxiliary factor (U2AF65) with the splicing factor 1 (SF1) or the spliceos

54 h the 65-kDa subunit of U2 auxiliary factor (U2AF65), a protein associated with the 3' splice site.

55 interacts with an essential splicing factor, U2AF65, and associates with the splicing machinery.

56 he RS domain from a related splicing factor, U2AF65, could not rescue viability and was inactive in i

57 ng of the normally intronic splicing factor, U2AF65, inhibits splicing.

58 RNAi silencing of the basal splicing factors U2AF65, SF1, and U2AF35.

59 complex of two well-known splicing factors: U2AF65 and the Prp19 complex (PRP19C).

60 rmational plasticity as a possible means for U2AF65 to universally identify diverse pre-mRNA splice s

61 d found that the two Pys are responsible for U2AF65's binding with intron 4.

62 ted from high affinity binding sequences for U2AF65.

63 In contrast, a high-affinity site for U2AF65 strongly inhibited exon inclusion.

64 s RNA nonspecifically and that the sites for U2AF65 binding and RNA binding are overlapping (or the s

65 protein SC35 can functionally substitute for U2AF65 in the reconstitution of pre-mRNA splicing in U2A

66 osin, the consensus polypyrimidine tract for U2AF65, AUUUA repeats and r(U)20were used as competitors

67 with transcription regulator BRD4, histones, U2AF65, Luc7L3, and SRSF11.

68 ulated binding can be recapitulated in human U2AF65 which has been mutated to decrease both affinity

69 rp2 protein (spU2AF59), a homologue of human U2AF65.

70 nRNP as well as Mud2p, which resembles human U2AF65.

71 show that SF1 interacts strongly with human U2AF65, and that SF1 is a bona fide E complex component.

72 ins of SR- and SR-related proteins including U2AF65, Luc7-like protein 3 (Luc7L3), SRSF11 and Acinus

73 proteins and SR related proteins, including U2AF65, all of which are known to function in alternativ

74 use this information to clone a human 56-kD U2AF65 associated protein (UAP56).

75 a heterodimer with subunits of 65 and 35 kD (U2AF65 and U2AF35).

76 The large (U2AF65) and small (U2AF35) subunits of the U2AF heterodi

77 a remarkably distinct manner from the local U2AF65 binding mode of SF3b155.

78 ers but may be partially attributed to lower U2AF65 binding and weaker splicing-related motifs.

79 Mammalian U2AF65 and UAP56 are required for prespliceosome (PS) fo

80 In the current model, U2AF65, bound at the polypyrimidine tract of the intron,

81 point binding protein (BBP) (SF1) and Mud2p (U2AF65), but lacks an obvious U2AF35 homolog, leaving op

82 terminal domain of SF3b155 contains multiple U2AF65 binding sites that are distinct from the binding

83 The multiple U2AF65 binding sites on SF3b155 suggest a model in which

84 We propose that the multiple U2AF65 binding sites within SF3b155 regulate conformatio

85 on SF3b155 suggest a model in which multiple U2AF65 molecules bound to the intron could enhance U2 sn

86 rich domain at the N-terminus of Neurospora U2AF65 regulates its RNA binding.

87 We show that Neurospora U2AF65 binds RNA with low affinity and specificity, appa

88 em RNA recognition motif domains (RRM1,2) of U2AF65 adopt closed/inactive and open/active conformatio

89 domain mutants indicated that the ability of U2AF65 to contact the branch point, to promote the U2 sn

90 ation is sufficient to explain the action of U2AF65 on spliceosome components located both 5' and 3'

91 Addition of U2AF65 protein further enhanced the splicing reconstitut

92 es the population of the open arrangement of U2AF65 RRM1,2 in the absence and presence of a weak Py-t

93 Therefore, the association of U2AF65 with RNA polymerase II may function not only to d

94 est that MBNL1 directly activates binding of U2AF65 to enhance upstream intron removal to ultimately

95 Here it is reported that binding of U2AF65 to the polypyrimidine tract directed the RS domai

96 ex assembly by competing with the binding of U2AF65 to the polypyrimidine tracts of repressed 3' spli

97 posal is that enhancers stabilize binding of U2AF65 to weak polypyrimidine (Py) tracts.

98 , while the first Py enhanced the binding of U2AF65 with the intron.

99 lation shift toward the open conformation of U2AF65 to facilitate the recognition of weak Py-tracts a

100 The spatial distribution of U2AF65 conformations is found to be highly anisotropic,

101 , particularly to the Arg-Ser (RS) domain of U2AF65, creates Tat inhibitors that localize to subnucle

102 he complete spectrum of the unbound forms of U2AF65 that coexist with the small percentage of a prefo

103 Our results reveal a new function of U2AF65: to position a DEAD box protein required for U2 s

104 laboratively with MUD2, the yeast homolog of U2AF65.

105 , and JMJD6-mediated lysine hydroxylation of U2AF65 could account for, at least partially, their co-r

106 Despite the central importance of U2AF65 for splice site recognition, the relative arrange

107 e scRNAPy interfered with the interaction of U2AF65 with the intron and repressed the IE2 expression.

108 Cross-linking of U2AF65 to RNA in a C28 complex was eliminated by the add

109 P is not required for splicing or loading of U2AF65 at other investigated p53-induced targets, includ

110 of complex A is associated with the loss of U2AF65 and 35.

111 Coexpression of a plant orthologue of U2AF65 alleviated the splicing repression of AtPTB1.

112 Overexpression of U2AF65 in cells transfected with a PLE-containing report

113 ate the essential nature of the third RBD of U2AF65 for the interaction between the two proteins, bot

114 eraction results in increased recruitment of U2AF65 and PRP19C to the pre-mRNA.

115 In this report we identify a new region of U2AF65 required for function, and use this information t

116 central domain and a proline-rich region of U2AF65, has been determined at 2.2 A resolution.

117 Tandem RNA recognition motifs (RRM)s of U2AF65 recognize polypyrimidine tract signals adjacent t

118 ressor hnRNP A1 and interfering with that of U2AF65 at the 3' splice site of exon 7.

119 A binding domain were compared with those of U2AF65 variants containing either Py tract-binding prote

120 interact with a U2AF homology motif (UHM) of U2AF65.

121 ch is recruited to the pre-mRNA dependent on U2AF65, and is required for the U2 snRNP-branchpoint int

122 vitro splicing, we found it had no effect on U2AF65 binding.

123 NA is still contained within the polymerase, U2AF65 is tightly bound.

124 K)nXRW(DE) consensus sequence for predicting U2AF65-UHM ligands from genomic sequences, where parenth

125 Thus, by preventing U2AF65 binding to Alu elements, hnRNP C plays a critical

126 onical polypyrimidine tract binding protein, U2AF65.

127 icing requires a heterodimer of the proteins U2AF65/U2AF35.

128 licing enhancers and their binding proteins (U2AF65 and ASF/SF2) that had critical roles in splicing

129 cally reduced by the addition of recombinant U2AF65 to the transcription reaction.

130 n U2AF65 and the enhancer complex to recruit U2AF65 to the adjacent intron.

131 s RNA may represent an adaption for reducing U2AF65 levels when pre-mRNA levels are low.

132 this paper we demonstrate that the mBBP/SF1-U2AF65 interaction promotes cooperative binding to a bra

133 peptides demonstrates that formation the SF1/U2AF65 complex is likely to affect regions of SF1 beyond

134 Furthermore, the complex of the SF1/U2AF65 interacting domains is stabilized by 3.3 kcal mol

135 mol-1 relative to the complex of the SF3b155/U2AF65 interacting domains, consistent with the need for

136 Since U2AF65 recognizes the polypyrimidine tract (PPT) and for

137 e factor U2 auxiliary factor 65 kDa subunit (U2AF65) and to act as a modulator of alternative splicin

138 cleoprotein auxiliary factor 65 kDa subunit (U2AF65) on the upstream intron.

139 tein auxiliary factor 65-kilodalton subunit (U2AF65) undergoes posttranslational lysyl-5-hydroxylatio

140 The U2 auxiliary factor large subunit (U2AF65) is an essential pre-mRNA splicing factor for the

141 is a heterodimer comprising a large subunit, U2AF65, and a small subunit, U2AF35.

142 he exogenously expressed large U2AF subunit, U2AF65, accumulates in spliced mRNP, leading to the recr

143 Similarly to TAP, U2AF65 stimulated directly the nuclear export and expres

144 for CTD-dependent splicing activation, that U2AF65 and PRP19C interact both in vitro and in vivo, an

145 mini-gene, and the results demonstrate that U2AF65 binds to such a site and controls the mRNA stabil

146 ifts and sequence requirements indicate that U2AF65 interactions with each of the SF3b155 sites are s

147 These findings indicate that U2AF65 shifts from protein-protein to protein-RNA intera

148 metic aspartate and to alanine, we show that U2AF65 binds Ataxin-1 in a Ser776 phosphorylation indepe

149 Providing the link to the CTD, we show that U2AF65 binds directly to the phosphorylated CTD, and tha

150 Here we show that U2AF65 crosslinking is replaced by crosslinking of three

151 NA recognition motif (RRM) of U2AF35 and the U2AF65 polyproline segment interact via reciprocal "tong

152 he branchpoint binding protein, SF1, and the U2AF65-U2AF35 heterodimer bound at an adjacent sequence.

153 ntaining SF3b155 sites are recognized by the U2AF65-UHM using intrinsic tryptophan fluorescence exper

154 pen reading frame is similar to that for the U2AF65 from mammals and flies.

155 Here, we report that two members of the U2AF65 family of proteins, hCC1.3, which we call CAPERal

156 rwise distance distribution functions of the U2AF65 RNA binding domain and those either previously ob

157 Here, the solution conformation of the U2AF65 RNA binding domain determined using small angle x

158 recognition, the relative arrangement of the U2AF65 RRMs and the energetic forces driving polypyrimid

159 Our results suggest that the U2AF65-U2AF35 complex identifies the U4CAG/R, with U2AF3

160 Thus, the U2AF65 RS domain plays a direct role in modulating splic

161 etion showed that Urp is associated with the U2AF65/U2AF35 heterodimer.

162 Thus, U2AF65 binding can be blocked either by MBNL1 binding or

163 d with DDS enhanced both -KTS WT1 binding to U2AF65 and splicing-factor colocalization.

164 nteraction between HCC1, a factor related to U2AF65, with both subunits of U2AF.

165 nd show that their preferential responses to U2AF65-related proteins and SRSF3 are associated with un

166 dition of the small U2AF subunit (U2AF35) to U2AF65 with weakened RNA binding affinity significantly

167 Furthermore, overexpression of the truncated U2AF65, which contains the arginine and serine dipeptide

168 shapes and RNA interactions of the wild-type U2AF65 RNA binding domain were compared with those of U2

169 sociated with spliceosome formation (U2AF35, U2AF65, U1A, and U1-70K) correlated with splicing effici

170 riptomes of HEK293 cells with varying U2AF35/U2AF65 and U2AF35a/b ratios.

171 arge enthalpy-entropy compensation underlies U2AF65 recognition of an optimal polyuridine tract.

172 The isoform-specific U2AF35 expression was U2AF65-dependent, required interactions between the U2AF

173 When U2AF65 is prevented from binding to the pre-mRNA, the U2

174 ortion of the intron as a stem-loop, whereas U2AF65 binds the same region in a single-strand structur

175 o acids, KTS, show stronger interaction with U2AF65 in vitro and better colocalization with splicing

176 mplex containing RBM39, which interacts with U2AF65 and SF3b155 and promotes U2 snRNP recruitment to

177 e of U2AF35, whose UHM domain interacts with U2AF65 RRM1, increases the population of the open arrang

178 evealed that Urp specifically interacts with U2AF65 through a U2AF35-homologous region and with SR pr

179 interact with U1-70K and U2AF35 but not with U2AF65.

180 Moreover, the fission yeast U2AF65 homolog, Prp2/Mis11 protein, was phosphorylated m