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Volumn 28, Issue 22, 2014, Pages 2518-2531

Stem–loop 4 of U1 snRNA is essential for splicing and interacts with the U2 snRNP-specific SF3A1 protein during spliceosome assembly

Author keywords

Alternative splicing; Gene expression; Pre mRNA splicing; Ribonucleoprotein; RNA protein interaction; snRNA; Spliceosome

Indexed keywords

BIOTIN; MESSENGER RNA PRECURSOR; PROTEIN SF3A1; SMALL NUCLEAR RIBONUCLEOPROTEIN; SMALL NUCLEAR RNA; UNCLASSIFIED DRUG; PROTEIN BINDING; RNA SPLICING; SF3A1 PROTEIN, HUMAN; U1 SMALL NUCLEAR RNA;

EID: 84910664664     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.248625.114     Document Type: Article
Times cited : (46)

References (82)
  • 1
    • 0030911051 scopus 로고    scopus 로고
    • Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals
    • Abovich N., Rosbash M. 1997. Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell 89: 403-412.
    • (1997) Cell , vol.89 , pp. 403-412
    • Abovich, N.1    Rosbash, M.2
  • 2
    • 0023359092 scopus 로고
    • The highly conserved U small nuclear RNA 3′-end formation signal is quite tolerant to mutation
    • Ach R.A., Weiner AM. 1987. The highly conserved U small nuclear RNA 3′-end formation signal is quite tolerant to mutation. Mol Cell Biol 7: 2070-2079.
    • (1987) Mol Cell Biol , vol.7 , pp. 2070-2079
    • Ach, R.A.1    Weiner, A.M.2
  • 3
    • 84887115772 scopus 로고    scopus 로고
    • RNA structure analysis of human spliceosomes reveals a compact 3D arrangement of snRNAs at the catalytic core
    • Anokhina M., Bessonov S, Miao Z, Westhof E, Hartmuth K, Lührmann R. 2013. RNA structure analysis of human spliceosomes reveals a compact 3D arrangement of snRNAs at the catalytic core. EMBO J 32: 2804-2818.
    • (2013) EMBO J , vol.32 , pp. 2804-2818
    • Anokhina, M.1    Bessonov, S.2    Miao, Z.3    Westhof, E.4    Hartmuth, K.5    Lührmann, R.6
  • 4
    • 0027459936 scopus 로고
    • Small nuclear ribonucleoprotein (RNP) U2 contains numerous additional proteins and has a bipartite RNP structure under splicing conditions
    • Behrens S.E., Tyc K, Kastner B, Reichelt J, Lührmann R. 1993. Small nuclear ribonucleoprotein (RNP) U2 contains numerous additional proteins and has a bipartite RNP structure under splicing conditions. Mol Cell Biol 13: 307-319.
    • (1993) Mol Cell Biol , vol.13 , pp. 307-319
    • Behrens, S.E.1    Tyc, K.2    Kastner, B.3    Reichelt, J.4    Lührmann, R.5
  • 5
    • 33748173310 scopus 로고    scopus 로고
    • Functional spliceosomal A complexes can be assembled in vitro in the absence of a penta-snRNP
    • Behzadnia N., Hartmuth K, Will CL, Lührmann R. 2006. Functional spliceosomal A complexes can be assembled in vitro in the absence of a penta-snRNP. RNA 12: 1738-1746.
    • (2006) RNA , vol.12 , pp. 1738-1746
    • Behzadnia, N.1    Hartmuth, K.2    Will, C.L.3    Lührmann, R.4
  • 6
    • 0026748223 scopus 로고
    • Activation of c-src neuron-specific splicing by an unusual RNA element in vivo and in vitro
    • Black DL. 1992. Activation of c-src neuron-specific splicing by an unusual RNA element in vivo and in vitro. Cell 69: 795-807.
    • (1992) Cell , vol.69 , pp. 795-807
    • Black, D.L.1
  • 8
    • 3142675143 scopus 로고    scopus 로고
    • Ser/Arg-rich protein-mediated communication between U1 and U2 small nuclear ribonucleoprotein particles
    • Boukis L.A., Liu N, Furuyama S, Bruzik JP. 2004. Ser/Arg-rich protein-mediated communication between U1 and U2 small nuclear ribonucleoprotein particles. J Biol Chem 279: 29647- 29653.
    • (2004) J Biol Chem , vol.279 , pp. 29647-29653
    • Boukis, L.A.1    Liu, N.2    Furuyama, S.3    Bruzik, J.P.4
  • 9
    • 0027440306 scopus 로고
    • Interaction of mammalian splicing factor SF3a with U2 snRNP and relation of its 60-kD subunit to yeast PRP9
    • Brosi R., Groning K, Behrens SE, Lührmann R, Kramer A. 1993a. Interaction of mammalian splicing factor SF3a with U2 snRNP and relation of its 60-kD subunit to yeast PRP9. Science 262: 102-105.
    • (1993) Science , vol.262 , pp. 102-105
    • Brosi, R.1    Groning, K.2    Behrens, S.E.3    Lührmann, R.4    Kramer, A.5
  • 10
    • 0027183212 scopus 로고
    • Separation of splicing factor SF3 into two components and purification of SF3a activity
    • Brosi R., Hauri HP, Kramer A. 1993b. Separation of splicing factor SF3 into two components and purification of SF3a activity. J Biol Chem 268: 17640-17646.
    • (1993) J Biol Chem , vol.268 , pp. 17640-17646
    • Brosi, R.1    Hauri, H.P.2    Kramer, A.3
  • 11
    • 0001468848 scopus 로고    scopus 로고
    • Splicing of precursors to mRNAs by the spliceosomes
    • (ed. Gesteland RF, Cech TR, Atkin JF), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Burge B.B., Tuschl T, Sharp PA. 1999. Splicing of precursors to mRNAs by the spliceosomes. In RNA world (ed. Gesteland RF, Cech TR, Atkin JF), pp. 525-560. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) RNA world , pp. 525-560
    • Burge, B.B.1    Tuschl, T.2    Sharp, P.A.3
  • 12
    • 67649774581 scopus 로고    scopus 로고
    • Unbiased RNAprotein interaction screen by quantitative proteomics
    • Butter F., Scheibe M, Morl M, Mann M. 2009. Unbiased RNAprotein interaction screen by quantitative proteomics. Proc Natl Acad Sci 106: 10626-10631.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 10626-10631
    • Butter, F.1    Scheibe, M.2    Morl, M.3    Mann, M.4
  • 13
    • 0028800302 scopus 로고
    • Conserved intron elements repress splicing of a neuron-specific c-src exon in vitro
    • Chan R.C., Black DL. 1995. Conserved intron elements repress splicing of a neuron-specific c-src exon in vitro. Mol Cell Biol 15: 6377-6385.
    • (1995) Mol Cell Biol , vol.15 , pp. 6377-6385
    • Chan, R.C.1    Black, D.L.2
  • 14
    • 77955966729 scopus 로고    scopus 로고
    • snRNA 3′ end formation: The dawn of the integrator complex
    • Chen J., Wagner EJ. 2010. snRNA 3′ end formation: the dawn of the integrator complex. Biochem Soc Trans 38: 1082-1087.
    • (2010) Biochem Soc Trans , vol.38 , pp. 1082-1087
    • Chen, J.1    Wagner, E.J.2
  • 15
    • 0028216431 scopus 로고
    • Specific protein-protein interactions between the essential mammalian spliceosome-associated proteins SAP 61 and SAP 114
    • Chiara M.D., Champion-Arnaud P, Buvoli M, Nadal-Ginard B, Reed R. 1994. Specific protein-protein interactions between the essential mammalian spliceosome-associated proteins SAP 61 and SAP 114. Proc Natl Acad Sci 91: 6403-6407.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 6403-6407
    • Chiara, M.D.1    Champion-Arnaud, P.2    Buvoli, M.3    Nadal-Ginard, B.4    Reed, R.5
  • 16
    • 0033634948 scopus 로고    scopus 로고
    • Multisite RNA binding and release of polypyrimidine tract binding protein during the regulation of c-src neural-specific splicing
    • Chou M.Y., Underwood JG, Nikolic J, Luu MH, Black DL. 2000. Multisite RNA binding and release of polypyrimidine tract binding protein during the regulation of c-src neural-specific splicing. Mol Cell 5: 949-957.
    • (2000) Mol Cell , vol.5 , pp. 949-957
    • Chou, M.Y.1    Underwood, J.G.2    Nikolic, J.3    Luu, M.H.4    Black, D.L.5
  • 17
    • 84861984263 scopus 로고    scopus 로고
    • Structure, function and regulation of spliceosomal RNA helicases
    • Cordin O., Hahn D, Beggs JD. 2012. Structure, function and regulation of spliceosomal RNA helicases. Curr Opin Cell Biol 24: 431-438.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 431-438
    • Cordin, O.1    Hahn, D.2    Beggs, J.D.3
  • 18
    • 84876875040 scopus 로고    scopus 로고
    • Single-molecule colocalization FRET evidence that spliceosome activation precedes stable approach of 5′ splice site and branch site
    • Crawford D.J., Hoskins AA, Friedman LJ, Gelles J, Moore MJ. 2013. Single-molecule colocalization FRET evidence that spliceosome activation precedes stable approach of 5′ splice site and branch site. Proc Natl Acad Sci 110: 6783-6788.
    • (2013) Proc Natl Acad Sci , vol.110 , pp. 6783-6788
    • Crawford, D.J.1    Hoskins, A.A.2    Friedman, L.J.3    Gelles, J.4    Moore, M.J.5
  • 19
    • 0032880119 scopus 로고    scopus 로고
    • Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155
    • Das B.K., Xia L, Palandjian L, Gozani O, Chyung Y, Reed R. 1999. Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155. Mol Cell Biol 19: 6796-6802.
    • (1999) Mol Cell Biol , vol.19 , pp. 6796-6802
    • Das, B.K.1    Xia, L.2    Palandjian, L.3    Gozani, O.4    Chyung, Y.5    Reed, R.6
  • 20
    • 0033636518 scopus 로고    scopus 로고
    • Functional association of U2 snRNP with the ATP-independent spliceosomal complex E
    • Das R., Zhou Z, Reed R. 2000. Functional association of U2 snRNP with the ATP-independent spliceosomal complex E. Mol Cell 5: 779-787.
    • (2000) Mol Cell , vol.5 , pp. 779-787
    • Das, R.1    Zhou, Z.2    Reed, R.3
  • 21
    • 0025261680 scopus 로고
    • Preparation of extracts from higher eukaryotes
    • Dignam JD. 1990. Preparation of extracts from higher eukaryotes. Methods Enzymol 182: 194-203.
    • (1990) Methods Enzymol , vol.182 , pp. 194-203
    • Dignam, J.D.1
  • 22
    • 0026039804 scopus 로고
    • Selection of splice sites in premRNAs with short internal exons
    • Dominski Z., Kole R. 1991. Selection of splice sites in premRNAs with short internal exons. Mol Cell Biol 11: 6075- 6083.
    • (1991) Mol Cell Biol , vol.11 , pp. 6075-6083
    • Dominski, Z.1    Kole, R.2
  • 23
    • 33846665912 scopus 로고    scopus 로고
    • The 5′ end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes
    • Donmez G., Hartmuth K, Kastner B, Will CL, Lührmann R. 2007. The 5′ end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes. Mol Cell 25: 399-411.
    • (2007) Mol Cell , vol.25 , pp. 399-411
    • Donmez, G.1    Hartmuth, K.2    Kastner, B.3    Will, C.L.4    Lührmann, R.5
  • 24
    • 33645212088 scopus 로고    scopus 로고
    • U2 snRNA-protein contacts in purified human 17S U2 snRNPs and in spliceosomal A and B complexes
    • Dybkov O., Will CL, Deckert J, Behzadnia N, Hartmuth K, Lührmann R. 2006. U2 snRNA-protein contacts in purified human 17S U2 snRNPs and in spliceosomal A and B complexes. Mol Cell Biol 26: 2803-2816.
    • (2006) Mol Cell Biol , vol.26 , pp. 2803-2816
    • Dybkov, O.1    Will, C.L.2    Deckert, J.3    Behzadnia, N.4    Hartmuth, K.5    Lührmann, R.6
  • 25
    • 0033022124 scopus 로고    scopus 로고
    • The SRm160/ 300 splicing coactivator is required for exon-enhancer function
    • Eldridge A.G., Li Y, Sharp PA, Blencowe BJ. 1999. The SRm160/ 300 splicing coactivator is required for exon-enhancer function. Proc Natl Acad Sci 96: 6125-6130.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 6125-6130
    • Eldridge, A.G.1    Li, Y.2    Sharp, P.A.3    Blencowe, B.J.4
  • 26
    • 77449146854 scopus 로고    scopus 로고
    • Target-decoy search strategy for mass spectrometry-based proteomics
    • Elias J.E., Gygi SP. 2010. Target-decoy search strategy for mass spectrometry-based proteomics. Methods Mol Biol 604: 55-71.
    • (2010) Methods Mol Biol , vol.604 , pp. 55-71
    • Elias, J.E.1    Gygi, S.P.2
  • 27
    • 0030611640 scopus 로고    scopus 로고
    • U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction
    • Fleckner J., Zhang M, Valcarcel J, Green MR. 1997. U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction. Genes Dev 11: 1864- 1872.
    • (1997) Genes Dev , vol.11 , pp. 1864-1872
    • Fleckner, J.1    Zhang, M.2    Valcarcel, J.3    Green, M.R.4
  • 29
    • 60549104588 scopus 로고    scopus 로고
    • Splice-site pairing is an intrinsically high fidelity process
    • Fox-Walsh K.L., Hertel KJ. 2009. Splice-site pairing is an intrinsically high fidelity process. Proc Natl Acad Sci 106: 1766-1771.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 1766-1771
    • Fox-Walsh, K.L.1    Hertel, K.J.2
  • 30
    • 0030044836 scopus 로고    scopus 로고
    • Evidence that sequenceindependent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A
    • Gozani O., Feld R, Reed R. 1996. Evidence that sequenceindependent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A. Genes Dev 10: 233-243.
    • (1996) Genes Dev , vol.10 , pp. 233-243
    • Gozani, O.1    Feld, R.2    Reed, R.3
  • 31
    • 0031878108 scopus 로고    scopus 로고
    • A potential role for U2AF- SAP 155 interactions in recruiting U2 snRNP to the branch site
    • Gozani O., Potashkin J, Reed R. 1998. A potential role for U2AF- SAP 155 interactions in recruiting U2 snRNP to the branch site. Mol Cell Biol 18: 4752-4760.
    • (1998) Mol Cell Biol , vol.18 , pp. 4752-4760
    • Gozani, O.1    Potashkin, J.2    Reed, R.3
  • 32
    • 0026442896 scopus 로고
    • The 5′ splice site consensus RNA oligonucleotide induces assembly of U2/U4/U5/U6 small nuclear ribonucleoprotein complexes
    • Hall K.B., Konarska MM. 1992. The 5′ splice site consensus RNA oligonucleotide induces assembly of U2/U4/U5/U6 small nuclear ribonucleoprotein complexes. Proc Natl Acad Sci 89: 10969-10973.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 10969-10973
    • Hall, K.B.1    Konarska, M.M.2
  • 33
    • 0022102252 scopus 로고
    • Formation of the 3′ end of U1 snRNA is directed by a conserved sequence located downstream of the coding region
    • Hernandez N. 1985. Formation of the 3′ end of U1 snRNA is directed by a conserved sequence located downstream of the coding region. EMBO J 4: 1827-1837.
    • (1985) EMBO J , vol.4 , pp. 1827-1837
    • Hernandez, N.1
  • 34
    • 34147179830 scopus 로고    scopus 로고
    • U2 toggles iteratively between the stem IIa and stem IIc conformations to promote pre-mRNA splicing
    • Hilliker A.K., Mefford MA, Staley JP. 2007. U2 toggles iteratively between the stem IIa and stem IIc conformations to promote pre-mRNA splicing. Genes Dev 21: 821-834.
    • (2007) Genes Dev , vol.21 , pp. 821-834
    • Hilliker, A.K.1    Mefford, M.A.2    Staley, J.P.3
  • 36
    • 0242569349 scopus 로고    scopus 로고
    • A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture
    • Ibarrola N., Kalume DE, Gronborg M, Iwahori A, Pandey A. 2003. A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture. Anal Chem 75: 6043-6049.
    • (2003) Anal Chem , vol.75 , pp. 6043-6049
    • Ibarrola, N.1    Kalume, D.E.2    Gronborg, M.3    Iwahori, A.4    Pandey, A.5
  • 37
    • 28844480841 scopus 로고    scopus 로고
    • Identification of ubiquitination sites and determination of ubiquitin-chain architectures by mass spectrometry
    • Kaiser P., Wohlschlegel J. 2005. Identification of ubiquitination sites and determination of ubiquitin-chain architectures by mass spectrometry. Methods Enzymol 399: 266-277.
    • (2005) Methods Enzymol , vol.399 , pp. 266-277
    • Kaiser, P.1    Wohlschlegel, J.2
  • 38
    • 0036315512 scopus 로고    scopus 로고
    • Early organization of premRNA during spliceosome assembly
    • Kent O.A., MacMillan AM. 2002. Early organization of premRNA during spliceosome assembly. Nat Struct Biol 9: 576-581.
    • (2002) Nat Struct Biol , vol.9 , pp. 576-581
    • Kent, O.A.1    McMillan, A.M.2
  • 39
    • 0035177309 scopus 로고    scopus 로고
    • Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase
    • Kistler A.L., Guthrie C. 2001. Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase. Genes Dev 15: 42-49.
    • (2001) Genes Dev , vol.15 , pp. 42-49
    • Kistler, A.L.1    Guthrie, C.2
  • 40
    • 77149180424 scopus 로고    scopus 로고
    • Release of SF3 from the intron branchpoint activates the first step of pre-mRNA splicing
    • Lardelli R.M., Thompson JX, Yates JR III, Stevens SW. 2010. Release of SF3 from the intron branchpoint activates the first step of pre-mRNA splicing. RNA 16: 516-528.
    • (2010) RNA , vol.16 , pp. 516-528
    • Lardelli, R.M.1    Thompson, J.X.2    Yates, J.R.3    Stevens, S.W.4
  • 41
    • 84867665144 scopus 로고    scopus 로고
    • AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus
    • Lee N., Pimienta G, Steitz JA. 2012. AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus. RNA 18: 2073-2082.
    • (2012) RNA , vol.18 , pp. 2073-2082
    • Lee, N.1    Pimienta, G.2    Steitz, J.A.3
  • 43
    • 0035180388 scopus 로고    scopus 로고
    • Multiple roles for the yeast SUB2/yUAP56 gene in splicing
    • Libri D., Graziani N, Saguez C, Boulay J. 2001. Multiple roles for the yeast SUB2/yUAP56 gene in splicing. Genes Dev 15: 36- 41.
    • (2001) Genes Dev , vol.15 , pp. 36-41
    • Libri, D.1    Graziani, N.2    Saguez, C.3    Boulay, J.4
  • 44
    • 4143078172 scopus 로고    scopus 로고
    • Commitment to splice site pairing coincides with A complex formation
    • Lim S.R., Hertel KJ. 2004. Commitment to splice site pairing coincides with A complex formation. Mol Cell 15: 477-483.
    • (2004) Mol Cell , vol.15 , pp. 477-483
    • Lim, S.R.1    Hertel, K.J.2
  • 45
    • 84858800333 scopus 로고    scopus 로고
    • Structure and assembly of the SF3a splicing factor complex of U2 snRNP
    • Lin P.C., Xu RM. 2012. Structure and assembly of the SF3a splicing factor complex of U2 snRNP. EMBO J 31: 1579- 1590.
    • (2012) EMBO J , vol.31 , pp. 1579-1590
    • Lin, P.C.1    Xu, R.M.2
  • 46
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M. 2006. Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 7: 952-958.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 47
    • 0033800453 scopus 로고    scopus 로고
    • Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein
    • Markovtsov V., Nikolic JM, Goldman JA, Turck CW, Chou MY, Black DL. 2000. Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. Mol Cell Biol 20: 7463-7479.
    • (2000) Mol Cell Biol , vol.20 , pp. 7463-7479
    • Markovtsov, V.1    Nikolic, J.M.2    Goldman, J.A.3    Turck, C.W.4    Chou, M.Y.5    Black, D.L.6
  • 48
    • 0037322576 scopus 로고    scopus 로고
    • Assembly of the U1 snRNP involves interactions with the backbone of the terminal stem of U1 snRNA
    • McConnell T.S., Lokken RP, Steitz JA. 2003. Assembly of the U1 snRNP involves interactions with the backbone of the terminal stem of U1 snRNA. RNA 9: 193-201.
    • (2003) RNA , vol.9 , pp. 193-201
    • McConnell, T.S.1    Lokken, R.P.2    Steitz, J.A.3
  • 49
    • 0030832044 scopus 로고    scopus 로고
    • A complex intronic splicing enhancer from the c-src pre-mRNA activates inclusion of a heterologous exon
    • Modafferi E.F., Black DL. 1997. A complex intronic splicing enhancer from the c-src pre-mRNA activates inclusion of a heterologous exon. Mol Cell Biol 17: 6537-6545.
    • (1997) Mol Cell Biol , vol.17 , pp. 6537-6545
    • Modafferi, E.F.1    Black, D.L.2
  • 50
    • 0034805909 scopus 로고    scopus 로고
    • Domains in human splicing factors SF3a60 and SF3a66 required for binding to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formation
    • Nesic D., Kramer A. 2001. Domains in human splicing factors SF3a60 and SF3a66 required for binding to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formation. Mol Cell Biol 21: 6406-6417.
    • (2001) Mol Cell Biol , vol.21 , pp. 6406-6417
    • Nesic, D.1    Kramer, A.2
  • 52
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • Park S.K., Venable JD, Xu T, Yates JR III. 2008. A quantitative analysis software tool for mass spectrometry-based proteomics. Nat Methods 5: 319-322.
    • (2008) Nat Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates, J.R.4
  • 53
    • 2242443509 scopus 로고    scopus 로고
    • Essential role for the SMN complex in the specificity of snRNP assembly
    • Pellizzoni L., Yong J, Dreyfuss G. 2002. Essential role for the SMN complex in the specificity of snRNP assembly. Science 298: 1775-1779.
    • (2002) Science , vol.298 , pp. 1775-1779
    • Pellizzoni, L.1    Yong, J.2    Dreyfuss, G.3
  • 54
    • 34147174235 scopus 로고    scopus 로고
    • Rearrangement of competing U2 RNA helices within the spliceosome promotes multiple steps in splicing
    • Perriman R.J., Ares MJ. 2007. Rearrangement of competing U2 RNA helices within the spliceosome promotes multiple steps in splicing. Genes Dev 21: 811-820.
    • (2007) Genes Dev , vol.21 , pp. 811-820
    • Perriman, R.J.1    Ares, M.J.2
  • 55
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution
    • Pomeranz Krummel DA, Oubridge C, Leung AK, Li J, Nagai K. 2009. Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. Nature 458: 475-480.
    • (2009) Nature , vol.458 , pp. 475-480
    • Pomeranz Krummel, D.A.1    Oubridge, C.2    Leung, A.K.3    Li, J.4    Nagai, K.5
  • 56
    • 0034069505 scopus 로고    scopus 로고
    • Mechanisms of fidelity in pre-mRNA splicing
    • Reed R. 2000. Mechanisms of fidelity in pre-mRNA splicing. Curr Opin Cell Biol 12: 340-345.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 340-345
    • Reed, R.1
  • 57
    • 62149110993 scopus 로고    scopus 로고
    • A splicing component adapted to gene silencing
    • Roca X., Krainer AR. 2009. A splicing component adapted to gene silencing. Nat Biotechnol 27: 250-251.
    • (2009) Nat Biotechnol , vol.27 , pp. 250-251
    • Roca, X.1    Krainer, A.R.2
  • 58
    • 84861159694 scopus 로고    scopus 로고
    • Widespread recognition of 5′ splice sites by noncanonical base-pairing to U1 snRNA involving bulged nucleotides
    • Roca X., Akerman M, Gaus H, Berdeja A, Bennett CF, Krainer AR. 2012. Widespread recognition of 5′ splice sites by noncanonical base-pairing to U1 snRNA involving bulged nucleotides. Genes Dev 26: 1098-1109.
    • (2012) Genes Dev , vol.26 , pp. 1098-1109
    • Roca, X.1    Akerman, M.2    Gaus, H.3    Berdeja, A.4    Bennett, C.F.5    Krainer, A.R.6
  • 59
    • 77950870601 scopus 로고    scopus 로고
    • Exon definition complexes contain the tri-snRNP and can be directly converted into B-like precatalytic splicing complexes
    • Schneider M., Will CL, Anokhina M, Tazi J, Urlaub H, Lührmann R. 2010. Exon definition complexes contain the tri-snRNP and can be directly converted into B-like precatalytic splicing complexes. Mol Cell 38: 223-235.
    • (2010) Mol Cell , vol.38 , pp. 223-235
    • Schneider, M.1    Will, C.L.2    Anokhina, M.3    Tazi, J.4    Urlaub, H.5    Lührmann, R.6
  • 60
    • 84883480928 scopus 로고    scopus 로고
    • Structure-function analysis of the 5′ end of yeast U1 snRNA highlights genetic interactions with the Msl5•Mud2 branchpoint-binding complex and other spliceosome assembly factors
    • Schwer B., Chang J, Shuman S. 2013. Structure-function analysis of the 5′ end of yeast U1 snRNA highlights genetic interactions with the Msl5•Mud2 branchpoint-binding complex and other spliceosome assembly factors. Nucleic Acids Res 41: 7485-7500.
    • (2013) Nucleic Acids Res , vol.41 , pp. 7485-7500
    • Schwer, B.1    Chang, J.2    Shuman, S.3
  • 61
    • 84862865359 scopus 로고    scopus 로고
    • Staying on message: Ensuring fidelity in pre-mRNA splicing
    • Semlow D.R., Staley JP. 2012. Staying on message: ensuring fidelity in pre-mRNA splicing. Trends Biochem Sci 37: 263-273.
    • (2012) Trends Biochem Sci , vol.37 , pp. 263-273
    • Semlow, D.R.1    Staley, J.P.2
  • 62
    • 84863022278 scopus 로고    scopus 로고
    • A U1-U2 snRNP interaction network during intron definition
    • Shao W., Kim HS, Cao Y, Xu YZ, Query CC. 2012. A U1-U2 snRNP interaction network during intron definition. Mol Cell Biol 32: 470-478.
    • (2012) Mol Cell Biol , vol.32 , pp. 470-478
    • Shao, W.1    Kim, H.S.2    Cao, Y.3    Xu, Y.Z.4    Query, C.C.5
  • 63
    • 23744484618 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein blocks the 5′ splice site-dependent assembly of U2AF and the prespliceosomal E complex
    • Sharma S., Falick AM, Black DL. 2005. Polypyrimidine tract binding protein blocks the 5′ splice site-dependent assembly of U2AF and the prespliceosomal E complex. Mol Cell 19: 485-496.
    • (2005) Mol Cell , vol.19 , pp. 485-496
    • Sharma, S.1    Falick, A.M.2    Black, D.L.3
  • 64
    • 38849187162 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome
    • Sharma S., Kohlstaedt LA, Damianov A, Rio DC, Black DL. 2008. Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome. Nat Struct Mol Biol 15: 183-191.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 183-191
    • Sharma, S.1    Kohlstaedt, L.A.2    Damianov, A.3    Rio, D.C.4    Black, D.L.5
  • 65
    • 79951996054 scopus 로고    scopus 로고
    • U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression
    • Sharma S., Maris C, Allain FHT, Black DL. 2011. U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression. Mol Cell 41: 579-588.
    • (2011) Mol Cell , vol.41 , pp. 579-588
    • Sharma, S.1    Maris, C.2    Allain, F.H.T.3    Black, D.L.4
  • 66
    • 46249107277 scopus 로고    scopus 로고
    • Distinct activities of the DExD/H-box splicing factor hUAP56 facilitate stepwise assembly of the spliceosome
    • Shen H., Zheng X, Shen J, Zhang L, Zhao R, Green MR. 2008. Distinct activities of the DExD/H-box splicing factor hUAP56 facilitate stepwise assembly of the spliceosome. Genes Dev 22: 1796-1803.
    • (2008) Genes Dev , vol.22 , pp. 1796-1803
    • Shen, H.1    Zheng, X.2    Shen, J.3    Zhang, L.4    Zhao, R.5    Green, M.R.6
  • 67
    • 0022386757 scopus 로고
    • Trans splicing of mRNA precursors
    • Solnick D. 1985. Trans splicing of mRNA precursors. Cell 42: 157-164.
    • (1985) Cell , vol.42 , pp. 157-164
    • Solnick, D.1
  • 68
    • 0035945611 scopus 로고    scopus 로고
    • Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle
    • Stark H., Dube P, Lührmann R, Kastner B. 2001. Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle. Nature 409: 539-542.
    • (2001) Nature , vol.409 , pp. 539-542
    • Stark, H.1    Dube, P.2    Lührmann, R.3    Kastner, B.4
  • 70
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb D.L., McDonald WH, Yates JR. 2002. DTASelect and contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1: 21-28.
    • (2002) J Proteome Res , vol.1 , pp. 21-28
    • Tabb, D.L.1    McDonald, W.H.2    Yates, J.R.3
  • 71
    • 14844312915 scopus 로고    scopus 로고
    • Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo
    • Tanackovic G., Kramer A. 2005. Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo. Mol Biol Cell 16: 1366-1377.
    • (2005) Mol Biol Cell , vol.16 , pp. 1366-1377
    • Tanackovic, G.1    Kramer, A.2
  • 72
    • 0033559581 scopus 로고    scopus 로고
    • Characterization of SYBR Gold nucleic acid gel stain: A dye optimized for use with 300-nm ultraviolet transilluminators
    • Tuma R.S., Beaudet MP, Jin X, Jones LJ, Cheung CY, Yue S, Singer VL. 1999. Characterization of SYBR Gold nucleic acid gel stain: a dye optimized for use with 300-nm ultraviolet transilluminators. Anal Biochem 268: 278-288.
    • (1999) Anal Biochem , vol.268 , pp. 278-288
    • Tuma, R.S.1    Beaudet, M.P.2    Jin, X.3    Jones, L.J.4    Cheung, C.Y.5    Yue, S.6    Singer, V.L.7
  • 73
    • 78650273324 scopus 로고    scopus 로고
    • Functional organization of the Sm core in the crystal structure of human U1 snRNP
    • Weber G., Trowitzsch S, Kastner B, Lührmann R, Wahl MC. 2010. Functional organization of the Sm core in the crystal structure of human U1 snRNP. EMBO J 29: 4172-4184.
    • (2010) EMBO J , vol.29 , pp. 4172-4184
    • Weber, G.1    Trowitzsch, S.2    Kastner, B.3    Lührmann, R.4    Wahl, M.C.5
  • 76
    • 59249097527 scopus 로고    scopus 로고
    • Identification of SUMO-conjugated proteins and their SUMO attachment sites using proteomic mass spectrometry
    • Wohlschlegel JA. 2009. Identification of SUMO-conjugated proteins and their SUMO attachment sites using proteomic mass spectrometry. Methods Mol Bio 497: 33-49.
    • (2009) Methods Mol Bio , vol.497 , pp. 33-49
    • Wohlschlegel, J.A.1
  • 77
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu J.Y., Maniatis T. 1993. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell 75: 1061-1070.
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 78
    • 36749080450 scopus 로고    scopus 로고
    • Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly
    • Xu Y.Z., Query CC. 2007. Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly. Mol Cell 28: 838-849.
    • (2007) Mol Cell , vol.28 , pp. 838-849
    • Xu, Y.Z.1    Query, C.C.2
  • 80
    • 0036500546 scopus 로고    scopus 로고
    • Sequence-specific interaction of U1 snRNA with the SMN complex
    • Yong J., Pellizzoni L, Dreyfuss G. 2002. Sequence-specific interaction of U1 snRNA with the SMN complex. EMBO J 21: 1188-1196.
    • (2002) EMBO J , vol.21 , pp. 1188-1196
    • Yong, J.1    Pellizzoni, L.2    Dreyfuss, G.3
  • 81
    • 0022550119 scopus 로고
    • A compensatory base change in U1 snRNA suppresses a 5′ splice site mutation
    • Zhuang Y., Weiner AM. 1986. A compensatory base change in U1 snRNA suppresses a 5′ splice site mutation. Cell 46: 827- 835.
    • (1986) Cell , vol.46 , pp. 827-835
    • Zhuang, Y.1    Weiner, A.M.2
  • 82
    • 0042121256 scopus 로고    scopus 로고
    • Mfold Web server for nucleic acid folding and hybridization prediction
    • Zuker M. 2003. Mfold Web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31: 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1


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