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1 onical polypyrimidine tract binding protein, U2AF65.
2 interact with a U2AF homology motif (UHM) of U2AF65.
3 nal strong cross-link to the splicing factor U2AF65.
4 ete, <20 nt poly(A) tail in cells expressing U2AF65.
5 laboratively with MUD2, the yeast homolog of U2AF65.
6 rp2 protein (spU2AF59), a homologue of human U2AF65.
7 nRNP as well as Mud2p, which resembles human U2AF65.
8 interact with U1-70K and U2AF35 but not with U2AF65.
9 to FACT and the splicing factors SF2/ASF and U2AF65.
10 the large subunit of the U2 auxiliary factor U2AF65.
11 of ATXN1 with the splicing factors RBM17 and U2AF65.
12 s for 14-3-3, and splicing factors RBM17 and U2AF65.
13 ted from high affinity binding sequences for U2AF65.
14 splicing through interfering with binding of U2AF(65).
15 ribute to degenerate Py-tract recognition by U2AF(65).
16 for universal 3' splice site recognition by U2AF(65).
17 nucleoplasm, and RGH3alpha colocalizes with U2AF(65).
18 h the 65-kDa subunit of U2 auxiliary factor (U2AF65), a protein associated with the 3' splice site.
19 he exogenously expressed large U2AF subunit, U2AF65, accumulates in spliced mRNP, leading to the recr
20 em RNA recognition motif domains (RRM1,2) of U2AF65 adopt closed/inactive and open/active conformatio
23 proteins and SR related proteins, including U2AF65, all of which are known to function in alternativ
26 We show that U2AF(26) can associate with U2AF(65) and can functionally substitute for U2AF(35) in
27 ly identified, UHM/ULM-mediated complexes of U2AF(65) and SPF45 with SF3b155, this work demonstrates
28 SF1 phosphorylation on its associations with U2AF(65) and splice-site RNAs are likely to influence pr
30 e RS domain of the essential splicing factor U2AF(65) and then in the prespliceosome by the ESE bound
33 e factor U2 auxiliary factor 65 kDa subunit (U2AF65) and to act as a modulator of alternative splicin
35 licing enhancers and their binding proteins (U2AF65 and ASF/SF2) that had critical roles in splicing
36 e ESS showed that the U-rich 5' region binds U2AF65 and polypyrimidine tract binding protein, the C-r
39 for CTD-dependent splicing activation, that U2AF65 and PRP19C interact both in vitro and in vivo, an
41 s with the 3' splice site recognition factor U2AF65 and recruits it to the p21(Cip1) gene and mRNA.
42 mplex containing RBM39, which interacts with U2AF65 and SF3b155 and promotes U2 snRNP recruitment to
45 Thus, U2AF35 functions as a bridge between U2AF65 and the enhancer complex to recruit U2AF65 to the
47 nd dynamics of 3' splice site recognition by U2AF65 and the role of U2AF35 in the U2AF heterodimer, w
48 icated in selection, the proteins U2AF35 and U2AF65 and the U2 snRNP, are able to recognize alternati
55 ch is recruited to the pre-mRNA dependent on U2AF65, and is required for the U2 snRNP-branchpoint int
56 show that SF1 interacts strongly with human U2AF65, and that SF1 is a bona fide E complex component.
58 intron to bind to a splicing factor such as U2AF65, as determined by an RNA electrophoretic mobility
62 P is not required for splicing or loading of U2AF65 at other investigated p53-induced targets, includ
64 osin, the consensus polypyrimidine tract for U2AF65, AUUUA repeats and r(U)20were used as competitors
65 rylation reduces phospho-SF1 and phospho-SF1-U2AF(65) binding affinities for either optimal or subopt
68 ecifically and regulate splicing by blocking U2AF(65) binding to the 3' splice site upstream of exon
69 tions that strengthen the stem-loop decrease U2AF65 binding affinity and also repress exon 5 inclusio
70 s RNA nonspecifically and that the sites for U2AF65 binding and RNA binding are overlapping (or the s
74 RNA oligonucleotide containing the consensus U2AF65 binding site, but U2AF65 was not displaced by a n
77 terminal domain of SF3b155 contains multiple U2AF65 binding sites that are distinct from the binding
83 relative molecular mass (Mr 65K) of 65,000 (U2AF65) binds to the poly(Y) tract, whereas the role of
84 metic aspartate and to alanine, we show that U2AF65 binds Ataxin-1 in a Ser776 phosphorylation indepe
85 Providing the link to the CTD, we show that U2AF65 binds directly to the phosphorylated CTD, and tha
88 ortion of the intron as a stem-loop, whereas U2AF65 binds the same region in a single-strand structur
90 mini-gene, and the results demonstrate that U2AF65 binds to such a site and controls the mRNA stabil
92 Early in mammalian spliceosome assembly, U2AF65 binds to the pyrimidine tract between the BPS and
94 e also determined two baseline structures of U2AF(65) bound to the deoxy-uridine counterparts and com
95 cooperative interaction with splicing factor U2AF65 bound to an adjacent polypyrimidine tract (PPT) f
97 point binding protein (BBP) (SF1) and Mud2p (U2AF65), but lacks an obvious U2AF35 homolog, leaving op
98 thought to play a role in the recruitment of U2AF(65) by serine-arginine-rich (SR) proteins in enhanc
99 n JMJD6 and U2AF65, revealing that JMJD6 and U2AF65 co-regulated a large number of alternative splici
100 rative 3' splice site recognition by the SF1-U2AF(65) complex (where cooperativity is defined as a no
101 2AF(65) splicing factors, as well as the SF1/U2AF(65) complex in the absence and presence of AdML (ad
103 peptides demonstrates that formation the SF1/U2AF65 complex is likely to affect regions of SF1 beyond
109 cing factor 1 (SF1) and U2 auxiliary factor (U2AF(65)) cooperatively recognize the 3' splice site dur
110 , and JMJD6-mediated lysine hydroxylation of U2AF65 could account for, at least partially, their co-r
111 he RS domain from a related splicing factor, U2AF65, could not rescue viability and was inactive in i
112 , particularly to the Arg-Ser (RS) domain of U2AF65, creates Tat inhibitors that localize to subnucle
114 We found that the crystal structure of the U2AF(65)-D231V variant confirms favorable packing betwee
116 The isoform-specific U2AF35 expression was U2AF65-dependent, required interactions between the U2AF
118 Here, we report that two members of the U2AF65 family of proteins, hCC1.3, which we call CAPERal
119 y, we identified a preferred binding site of U2AF(65) for purine substitutions in the 3' regions of P
120 cities of wild-type and site-directed mutant U2AF(65) for region-dependent cytosine- and uracil-conta
123 ate the essential nature of the third RBD of U2AF65 for the interaction between the two proteins, bot
130 gs reveal an intimate link between JMJD6 and U2AF65 in alternative splicing regulation, which has imp
132 protein SC35 can functionally substitute for U2AF65 in the reconstitution of pre-mRNA splicing in U2A
133 o acids, KTS, show stronger interaction with U2AF65 in vitro and better colocalization with splicing
135 splicing assays reveal unforeseen roles for U2AF(65) inter-domain residues in recognizing a contiguo
137 mol-1 relative to the complex of the SF3b155/U2AF65 interacting domains, consistent with the need for
138 this paper we demonstrate that the mBBP/SF1-U2AF65 interaction promotes cooperative binding to a bra
139 ifts and sequence requirements indicate that U2AF65 interactions with each of the SF3b155 sites are s
142 ively poorly conserved in higher eukaryotes, U2AF(65) is faced with the problem of specifying uridine
149 ins of SR- and SR-related proteins including U2AF65, Luc7-like protein 3 (Luc7L3), SRSF11 and Acinus
151 on SF3b155 suggest a model in which multiple U2AF65 molecules bound to the intron could enhance U2 sn
152 RNAs are often interrupted with purines, yet U2AF(65) must identify these degenerate Py-tracts for ac
155 ation is sufficient to explain the action of U2AF65 on spliceosome components located both 5' and 3'
157 NA recognition motif (RRM) of U2AF35 and the U2AF65 polyproline segment interact via reciprocal "tong
161 several SR proteins but also with U1-70K and U2AF65, proteins associated with 5' and 3' splice sites,
162 arge enthalpy-entropy compensation underlies U2AF65 recognition of an optimal polyuridine tract.
163 consecutive RNA recognition motifs (RRM) of U2AF(65) recognize a polypyrimidine tract at the 3' spli
164 Tandem RNA recognition motifs (RRM)s of U2AF65 recognize polypyrimidine tract signals adjacent t
166 How the essential pre-mRNA splicing factor U2AF(65) recognizes the polypyrimidine (Py) signals of t
168 A splicing factor, U2 auxiliary factor 65KD (U2AF(65)) recognizes the polypyrimidine tract (Py-tract)
170 nd show that their preferential responses to U2AF65-related proteins and SRSF3 are associated with un
171 In this report we identify a new region of U2AF65 required for function, and use this information t
172 ntaining proteins such as SC35, ASF/SF2, and U2AF65, restored the splicing activity of the Sip1-immun
173 RNA-dependent interaction between JMJD6 and U2AF65, revealing that JMJD6 and U2AF65 co-regulated a l
174 characteristics, the X-ray structure of the U2AF(65) RNA binding domain bound to a Py tract composed
175 rwise distance distribution functions of the U2AF65 RNA binding domain and those either previously ob
177 shapes and RNA interactions of the wild-type U2AF65 RNA binding domain were compared with those of U2
178 We determined four structures of an extended U2AF(65)-RNA-binding domain bound to Py-tract oligonucle
179 nges that are induced by assembly of the SF1/U2AF(65)/RNA complex serve to position the pre-mRNA spli
181 e of U2AF35, whose UHM domain interacts with U2AF65 RRM1, increases the population of the open arrang
182 es the population of the open arrangement of U2AF65 RRM1,2 in the absence and presence of a weak Py-t
183 ay structure of the N-terminal RRM domain of U2AF(65) (RRM1) is described at 1.47 A resolution in the
184 formational selection and induced fit of the U2AF(65) RRMs are complementary mechanisms for Py-tract
185 ay scattering to demonstrate that the tandem U2AF(65) RRMs exhibit a broad range of conformations in
186 recognition, the relative arrangement of the U2AF65 RRMs and the energetic forces driving polypyrimid
192 , pre-mRNA for the essential splicing factor U2AF65 sometimes is spliced to produce an RNA that inclu
193 anges were observed for the isolated SF1 and U2AF(65) splicing factors or their individual complexes
194 and ab initio shape restorations of SF1 and U2AF(65) splicing factors, as well as the SF1/U2AF(65) c
197 cts and potentially could rearrange when the U2AF(65) structure adapts to different Py tract sequence
199 ted the interaction between ZC3H14 and U2AF2/U2AF(65) Taking all the findings into consideration, we
200 he complete spectrum of the unbound forms of U2AF65 that coexist with the small percentage of a prefo
201 evealed that Urp specifically interacts with U2AF65 through a U2AF35-homologous region and with SR pr
202 ur work demonstrates that in vivo binding of U2AF(65) to a polypyrimidine tract requires a flexible R
203 nformations may contribute to the ability of U2AF(65) to recognize a variety of Py-tract sequences.
204 the splicing defect is due to the failure of U2AF(65) to recognize the pseudouridylated polypyrimidin
206 domain mutants indicated that the ability of U2AF65 to contact the branch point, to promote the U2 sn
207 est that MBNL1 directly activates binding of U2AF65 to enhance upstream intron removal to ultimately
208 lation shift toward the open conformation of U2AF65 to facilitate the recognition of weak Py-tracts a
211 lymerase II may function not only to deliver U2AF65 to the nascent transcript but also to modulate ef
213 ex assembly by competing with the binding of U2AF65 to the polypyrimidine tracts of repressed 3' spli
215 rmational plasticity as a possible means for U2AF65 to universally identify diverse pre-mRNA splice s
218 sociated with spliceosome formation (U2AF35, U2AF65, U1A, and U1-70K) correlated with splicing effici
220 he branchpoint binding protein, SF1, and the U2AF65-U2AF35 heterodimer bound at an adjacent sequence.
222 rometry were used to show that rather than a U2AF65/U2AF35-like heterodimer, Mud2p forms a complex wi
224 K)nXRW(DE) consensus sequence for predicting U2AF65-UHM ligands from genomic sequences, where parenth
225 ntaining SF3b155 sites are recognized by the U2AF65-UHM using intrinsic tryptophan fluorescence exper
226 tein auxiliary factor 65-kilodalton subunit (U2AF65) undergoes posttranslational lysyl-5-hydroxylatio
227 e sampled by the multidomain splicing factor U2AF65 using complementary nuclear magnetic resonance sp
229 evant mutations, and that a structure-guided U2AF(65) variant is capable of manipulating gene express
230 A binding domain were compared with those of U2AF65 variants containing either Py tract-binding prote
231 the SR domains of the SR proteins SRP75 and U2AF65, via fusion to a heterologous MS2 RNA binding pro
233 d with decreased cross-linking of the factor U2AF65, whereas regulation at step 2 is correlated with
234 ulated binding can be recapitulated in human U2AF65 which has been mutated to decrease both affinity
235 e subunit of the U2 snRNP associated factor (U2AF65), which is essential for splicing of human intron
236 h the well studied mammalian splicing factor U2AF65, which binds to the adjacent polypyrimidine (PY)
237 Furthermore, overexpression of the truncated U2AF65, which contains the arginine and serine dipeptide
238 ion and interaction with the splicing factor U2AF65, which promotes mRNA processing and the stabiliza
239 f the U2 small nuclear RNA auxiliary factor (U2AF65) with the splicing factor 1 (SF1) or the spliceos
241 e scRNAPy interfered with the interaction of U2AF65 with the intron and repressed the IE2 expression.
244 dition of the small U2AF subunit (U2AF35) to U2AF65 with weakened RNA binding affinity significantly
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