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Volumn 28, Issue 2, 2007, Pages 240-252

U2 snRNP Binds Intronless Histone Pre-mRNAs to Facilitate U7-snRNP-Dependent 3′ End Formation

Author keywords

RNA

Indexed keywords

HELICASE; MESSENGER RNA PRECURSOR; RNA POLYMERASE II; SMALL NUCLEAR RIBONUCLEOPROTEIN;

EID: 35348955883     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.09.026     Document Type: Article
Times cited : (50)

References (62)
  • 1
    • 0030671163 scopus 로고    scopus 로고
    • Prp43: an RNA helicase-like factor involved in spliceosome disassembly
    • Arenas J.E., and Abelson J.N. Prp43: an RNA helicase-like factor involved in spliceosome disassembly. Proc. Natl. Acad. Sci. USA 94 (1997) 11798-11802
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11798-11802
    • Arenas, J.E.1    Abelson, J.N.2
  • 2
    • 8844274816 scopus 로고    scopus 로고
    • Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation
    • Barnard D.C., Ryan K., Manley J.L., and Richter J.D. Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation. Cell 119 (2004) 641-651
    • (2004) Cell , vol.119 , pp. 641-651
    • Barnard, D.C.1    Ryan, K.2    Manley, J.L.3    Richter, J.D.4
  • 3
    • 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., and Lührmann R. Small nuclear ribonucleoprotein (RNP) U2 contains numerous additional proteins and has a bipartite RNP structure under splicing conditions. Mol. Cell. Biol. 13 (1993) 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
  • 4
    • 2942648436 scopus 로고    scopus 로고
    • Genome-wide analysis reveals an unexpected function for the Drosophila splicing factor U2AF50 in the nuclear export of intronless mRNAs
    • Blanchette M., Labourier E., Green R.E., Brenner S.E., and Rio D.C. Genome-wide analysis reveals an unexpected function for the Drosophila splicing factor U2AF50 in the nuclear export of intronless mRNAs. Mol. Cell 14 (2004) 775-786
    • (2004) Mol. Cell , vol.14 , pp. 775-786
    • Blanchette, M.1    Labourier, E.2    Green, R.E.3    Brenner, S.E.4    Rio, D.C.5
  • 5
    • 0026047228 scopus 로고
    • Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro
    • Bond U.M., Yario T.A., and Steitz J.A. Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro. Genes Dev. 5 (1991) 1709-1722
    • (1991) Genes Dev. , vol.5 , pp. 1709-1722
    • Bond, U.M.1    Yario, T.A.2    Steitz, J.A.3
  • 6
    • 0032837037 scopus 로고    scopus 로고
    • The movement of coiled bodies visualized in living plant cells by the green fluorescent protein
    • Boudonck K., Dolan L., and Shaw P.J. The movement of coiled bodies visualized in living plant cells by the green fluorescent protein. Mol. Biol. Cell 10 (1999) 2297-2307
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2297-2307
    • Boudonck, K.1    Dolan, L.2    Shaw, P.J.3
  • 7
    • 0027183212 scopus 로고
    • Separation of splicing factor SF3 into two components and purification of SF3a activity
    • Brosi R., Hauri H.P., and Krämer A. Separation of splicing factor SF3 into two components and purification of SF3a activity. J. Biol. Chem. 268 (1993) 17640-17646
    • (1993) J. Biol. Chem. , vol.268 , pp. 17640-17646
    • Brosi, R.1    Hauri, H.P.2    Krämer, A.3
  • 8
    • 33747488951 scopus 로고    scopus 로고
    • The SF3b155 N-terminal domain is a scaffold important for splicing
    • Cass D.M., and Berglund J.A. The SF3b155 N-terminal domain is a scaffold important for splicing. Biochemistry 45 (2006) 10092-10101
    • (2006) Biochemistry , vol.45 , pp. 10092-10101
    • Cass, D.M.1    Berglund, J.A.2
  • 9
    • 0028338991 scopus 로고
    • Characterization and cloning of the human splicing factor 9G8: a novel 35 kDa factor of the serine/arginine protein family
    • Cavaloc Y., Popielarz M., Fuchs J.P., Gattoni R., and Stevenin J. Characterization and cloning of the human splicing factor 9G8: a novel 35 kDa factor of the serine/arginine protein family. EMBO J. 13 (1994) 2639-2649
    • (1994) EMBO J. , vol.13 , pp. 2639-2649
    • Cavaloc, Y.1    Popielarz, M.2    Fuchs, J.P.3    Gattoni, R.4    Stevenin, J.5
  • 10
    • 0029982647 scopus 로고    scopus 로고
    • The cap and the 3′ splice site similarly affect polyadenylation efficiency
    • Cooke C., and Alwine J.C. The cap and the 3′ splice site similarly affect polyadenylation efficiency. Mol. Cell. Biol. 16 (1996) 2579-2584
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2579-2584
    • Cooke, C.1    Alwine, J.C.2
  • 11
    • 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., and Reed R. Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155. Mol. Cell. Biol. 19 (1999) 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
  • 12
    • 0028104077 scopus 로고
    • Selection on silent sites in the rodent H3 histone gene family
    • DeBry R.W., and Marzluff W.F. Selection on silent sites in the rodent H3 histone gene family. Genetics 138 (1994) 191-202
    • (1994) Genetics , vol.138 , pp. 191-202
    • DeBry, R.W.1    Marzluff, W.F.2
  • 13
    • 4143151952 scopus 로고    scopus 로고
    • Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization
    • Dettwiler S., Aringhieri C., Cardinale S., Keller W., and Barabino S.M. Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization. J. Biol. Chem. 279 (2004) 35788-35797
    • (2004) J. Biol. Chem. , vol.279 , pp. 35788-35797
    • Dettwiler, S.1    Aringhieri, C.2    Cardinale, S.3    Keller, W.4    Barabino, S.M.5
  • 14
    • 26244452759 scopus 로고    scopus 로고
    • The polyadenylation factor CPSF-73 is involved in histone-pre-mRNA processing
    • Dominski Z., Yang X.C., and Marzluff W.F. The polyadenylation factor CPSF-73 is involved in histone-pre-mRNA processing. Cell 123 (2005) 37-48
    • (2005) Cell , vol.123 , pp. 37-48
    • Dominski, Z.1    Yang, X.C.2    Marzluff, W.F.3
  • 15
    • 9344271506 scopus 로고    scopus 로고
    • Modified nucleotides at the 5′ end of human U2 snRNA are required for spliceosomal E-complex formation
    • Donmez G., Hartmuth K., and Lührmann R. Modified nucleotides at the 5′ end of human U2 snRNA are required for spliceosomal E-complex formation. RNA 10 (2004) 1925-1933
    • (2004) RNA , vol.10 , pp. 1925-1933
    • Donmez, G.1    Hartmuth, K.2    Lührmann, R.3
  • 17
    • 0029064131 scopus 로고
    • Coiled bodies contain U7 small nuclear RNA and associate with specific DNA sequences in interphase human cells
    • Frey M.R., and Matera A.G. Coiled bodies contain U7 small nuclear RNA and associate with specific DNA sequences in interphase human cells. Proc. Natl. Acad. Sci. USA 92 (1995) 5915-5919
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5915-5919
    • Frey, M.R.1    Matera, A.G.2
  • 19
    • 0030044836 scopus 로고    scopus 로고
    • Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A
    • Gozani O., Feld R., and Reed R. Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A. Genes Dev. 10 (1996) 233-243
    • (1996) Genes Dev. , vol.10 , pp. 233-243
    • Gozani, O.1    Feld, R.2    Reed, R.3
  • 20
    • 0024443874 scopus 로고
    • Functional analysis of mutant Xenopus U2 snRNAs
    • Hamm J., Dathan N.A., and Mattaj I.W. Functional analysis of mutant Xenopus U2 snRNAs. Cell 59 (1989) 159-169
    • (1989) Cell , vol.59 , pp. 159-169
    • Hamm, J.1    Dathan, N.A.2    Mattaj, I.W.3
  • 21
    • 33748169778 scopus 로고    scopus 로고
    • A spliceosomal intron binding protein, IBP160, links position-dependent assembly of intron-encoded box C/D snoRNP to pre-mRNA splicing
    • Hirose T., Ideue T., Nagai M., Hagiwara M., Shu M.D., and Steitz J.A. A spliceosomal intron binding protein, IBP160, links position-dependent assembly of intron-encoded box C/D snoRNP to pre-mRNA splicing. Mol. Cell 23 (2006) 673-684
    • (2006) Mol. Cell , vol.23 , pp. 673-684
    • Hirose, T.1    Ideue, T.2    Nagai, M.3    Hagiwara, M.4    Shu, M.D.5    Steitz, J.A.6
  • 22
    • 0036000009 scopus 로고    scopus 로고
    • Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes
    • Hofmann I., Schnolzer M., Kaufmann I., and Franke W.W. Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes. Mol. Biol. Cell 13 (2002) 1665-1676
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1665-1676
    • Hofmann, I.1    Schnolzer, M.2    Kaufmann, I.3    Franke, W.W.4
  • 23
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA
    • Huang Y., and Steitz J.A. Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol. Cell 7 (2001) 899-905
    • (2001) Mol. Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 24
    • 0033559693 scopus 로고    scopus 로고
    • Intronless mRNA transport elements may affect multiple steps of pre-mRNA processing
    • Huang Y., Wimler K.M., and Carmichael G.G. Intronless mRNA transport elements may affect multiple steps of pre-mRNA processing. EMBO J. 18 (1999) 1642-1652
    • (1999) EMBO J. , vol.18 , pp. 1642-1652
    • Huang, Y.1    Wimler, K.M.2    Carmichael, G.G.3
  • 25
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang Y., Gattoni R., Stevenin J., and Steitz J.A. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol. Cell 11 (2003) 837-843
    • (2003) Mol. Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 26
    • 26944459450 scopus 로고    scopus 로고
    • Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs
    • Kolev N.G., and Steitz J.A. Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs. Genes Dev. 19 (2005) 2583-2592
    • (2005) Genes Dev. , vol.19 , pp. 2583-2592
    • Kolev, N.G.1    Steitz, J.A.2
  • 27
    • 0028624659 scopus 로고
    • Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo
    • Krämer A., Legrain P., Mulhauser F., Groning K., Brosi R., and Bilbe G. Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo. Nucleic Acids Res. 22 (1994) 5223-5228
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5223-5228
    • Krämer, A.1    Legrain, P.2    Mulhauser, F.3    Groning, K.4    Brosi, R.5    Bilbe, G.6
  • 29
    • 33745944934 scopus 로고    scopus 로고
    • Direct interactions between subunits of CPSF and the U2 snRNP contribute to the coupling of pre-mRNA 3′ end processing and splicing
    • Kyburz A., Friedlein A., Langen H., and Keller W. Direct interactions between subunits of CPSF and the U2 snRNP contribute to the coupling of pre-mRNA 3′ end processing and splicing. Mol. Cell 23 (2006) 195-205
    • (2006) Mol. Cell , vol.23 , pp. 195-205
    • Kyburz, A.1    Friedlein, A.2    Langen, H.3    Keller, W.4
  • 31
    • 0019570066 scopus 로고
    • Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease
    • Lerner E.A., Lerner M.R., Janeway Jr. C.A., and Steitz J.A. Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease. Proc. Natl. Acad. Sci. USA 78 (1981) 2737-2741
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2737-2741
    • Lerner, E.A.1    Lerner, M.R.2    Janeway Jr., C.A.3    Steitz, J.A.4
  • 32
    • 0028269622 scopus 로고
    • Direct interaction of the U1 snRNP-A protein with the upstream efficiency element of the SV40 late polyadenylation signal
    • Lutz C.S., and Alwine J.C. Direct interaction of the U1 snRNP-A protein with the upstream efficiency element of the SV40 late polyadenylation signal. Genes Dev. 8 (1994) 576-586
    • (1994) Genes Dev. , vol.8 , pp. 576-586
    • Lutz, C.S.1    Alwine, J.C.2
  • 34
    • 0037124096 scopus 로고    scopus 로고
    • Prp43 is an essential RNA-dependent ATPase required for release of lariat-intron from the spliceosome
    • Martin A., Schneider S., and Schwer B. Prp43 is an essential RNA-dependent ATPase required for release of lariat-intron from the spliceosome. J. Biol. Chem. 277 (2002) 17743-17750
    • (2002) J. Biol. Chem. , vol.277 , pp. 17743-17750
    • Martin, A.1    Schneider, S.2    Schwer, B.3
  • 35
    • 19344366158 scopus 로고    scopus 로고
    • Metazoan replication-dependent histone mRNAs: a distinct set of RNA polymerase II transcripts
    • Marzluff W.F. Metazoan replication-dependent histone mRNAs: a distinct set of RNA polymerase II transcripts. Curr. Opin. Cell Biol. 17 (2005) 274-280
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 274-280
    • Marzluff, W.F.1
  • 37
    • 0036132667 scopus 로고    scopus 로고
    • SRm160 splicing coactivator promotes transcript 3′-end cleavage
    • McCracken S., Lambermon M., and Blencowe B.J. SRm160 splicing coactivator promotes transcript 3′-end cleavage. Mol. Cell. Biol. 22 (2002) 148-160
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 148-160
    • McCracken, S.1    Lambermon, M.2    Blencowe, B.J.3
  • 38
    • 7044272280 scopus 로고    scopus 로고
    • Evidence for reassociation of RNA-binding proteins after cell lysis: implications for the interpretation of immunoprecipitation analyses
    • Mili S., and Steitz J.A. Evidence for reassociation of RNA-binding proteins after cell lysis: implications for the interpretation of immunoprecipitation analyses. RNA 10 (2004) 1692-1694
    • (2004) RNA , vol.10 , pp. 1692-1694
    • Mili, S.1    Steitz, J.A.2
  • 39
    • 0036747331 scopus 로고    scopus 로고
    • A novel function for the U2AF 65 splicing factor in promoting pre-mRNA 3′-end processing
    • Millevoi S., Geraghty F., Idowu B., Tam J.L., Antoniou M., and Vagner S. A novel function for the U2AF 65 splicing factor in promoting pre-mRNA 3′-end processing. EMBO Rep. 3 (2002) 869-874
    • (2002) EMBO Rep. , vol.3 , pp. 869-874
    • Millevoi, S.1    Geraghty, F.2    Idowu, B.3    Tam, J.L.4    Antoniou, M.5    Vagner, S.6
  • 40
    • 33750200773 scopus 로고    scopus 로고
    • An interaction between U2AF 65 and CF I(m) links the splicing and 3′ end processing machineries
    • Millevoi S., Loulergue C., Dettwiler S., Karaa S.Z., Keller W., Antoniou M., and Vagner S. An interaction between U2AF 65 and CF I(m) links the splicing and 3′ end processing machineries. EMBO J. 25 (2006) 4854-4864
    • (2006) EMBO J. , vol.25 , pp. 4854-4864
    • Millevoi, S.1    Loulergue, C.2    Dettwiler, S.3    Karaa, S.Z.4    Keller, W.5    Antoniou, M.6    Vagner, S.7
  • 41
    • 5444231229 scopus 로고    scopus 로고
    • A role for Cajal bodies in the final steps of U2 snRNP biogenesis
    • Nesic D., Tanackovic G., and Krämer A. A role for Cajal bodies in the final steps of U2 snRNP biogenesis. J. Cell Sci. 117 (2004) 4423-4433
    • (2004) J. Cell Sci. , vol.117 , pp. 4423-4433
    • Nesic, D.1    Tanackovic, G.2    Krämer, A.3
  • 42
    • 0037107547 scopus 로고    scopus 로고
    • On the importance of being co-transcriptional
    • Neugebauer K.M. On the importance of being co-transcriptional. J. Cell Sci. 115 (2002) 3865-3871
    • (2002) J. Cell Sci. , vol.115 , pp. 3865-3871
    • Neugebauer, K.M.1
  • 43
    • 0345169036 scopus 로고    scopus 로고
    • Splicing double: insights from the second spliceosome
    • Patel A.A., and Steitz J.A. Splicing double: insights from the second spliceosome. Nat. Rev. Mol. Cell Biol. 4 (2003) 960-970
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 960-970
    • Patel, A.A.1    Steitz, J.A.2
  • 44
    • 0037154967 scopus 로고    scopus 로고
    • Integrating mRNA processing with transcription
    • Proudfoot N.J., Furger A., and Dye M.J. Integrating mRNA processing with transcription. Cell 108 (2002) 501-512
    • (2002) Cell , vol.108 , pp. 501-512
    • Proudfoot, N.J.1    Furger, A.2    Dye, M.J.3
  • 45
    • 1642488290 scopus 로고    scopus 로고
    • Evidence that polyadenylation factor CPSF-73 is the mRNA 3′ processing endonuclease
    • Ryan K., Calvo O., and Manley J.L. Evidence that polyadenylation factor CPSF-73 is the mRNA 3′ processing endonuclease. RNA 10 (2004) 565-573
    • (2004) RNA , vol.10 , pp. 565-573
    • Ryan, K.1    Calvo, O.2    Manley, J.L.3
  • 46
    • 0031885702 scopus 로고    scopus 로고
    • Molecular characterization of a novel, widespread nuclear protein that colocalizes with spliceosome components
    • Schmidt-Zachmann M.S., Knecht S., and Krämer A. Molecular characterization of a novel, widespread nuclear protein that colocalizes with spliceosome components. Mol. Biol. Cell 9 (1998) 143-160
    • (1998) Mol. Biol. Cell , vol.9 , pp. 143-160
    • Schmidt-Zachmann, M.S.1    Knecht, S.2    Krämer, A.3
  • 47
    • 0031877713 scopus 로고    scopus 로고
    • Cyclin E associates with components of the pre-mRNA splicing machinery in mammalian cells
    • Seghezzi W., Chua K., Shanahan F., Gozani O., Reed R., and Lees E. Cyclin E associates with components of the pre-mRNA splicing machinery in mammalian cells. Mol. Cell. Biol. 18 (1998) 4526-4536
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4526-4536
    • Seghezzi, W.1    Chua, K.2    Shanahan, F.3    Gozani, O.4    Reed, R.5    Lees, E.6
  • 48
    • 0023409733 scopus 로고
    • Electrophoretic separation of polyadenylation-specific complexes
    • Skolnik-David H., Moore C.L., and Sharp P.A. Electrophoretic separation of polyadenylation-specific complexes. Genes Dev. 1 (1987) 672-682
    • (1987) Genes Dev. , vol.1 , pp. 672-682
    • Skolnik-David, H.1    Moore, C.L.2    Sharp, P.A.3
  • 49
    • 0033984159 scopus 로고    scopus 로고
    • Complex protein interactions within the human polyadenylation machinery identify a novel component
    • Takagaki Y., and Manley J.L. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol. Cell. Biol. 20 (2000) 1515-1525
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1515-1525
    • Takagaki, Y.1    Manley, J.L.2
  • 50
    • 14844312915 scopus 로고    scopus 로고
    • Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo
    • Tanackovic G., and Krämer A. Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo. Mol. Biol. Cell 16 (2005) 1366-1377
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1366-1377
    • Tanackovic, G.1    Krämer, A.2
  • 51
    • 29144515824 scopus 로고    scopus 로고
    • Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2
    • Tsai R.T., Fu R.H., Yeh F.L., Tseng C.K., Lin Y.C., Huang Y.H., and Cheng S.C. Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2. Genes Dev. 19 (2005) 2991-3003
    • (2005) Genes Dev. , vol.19 , pp. 2991-3003
    • Tsai, R.T.1    Fu, R.H.2    Yeh, F.L.3    Tseng, C.K.4    Lin, Y.C.5    Huang, Y.H.6    Cheng, S.C.7
  • 52
    • 9244225692 scopus 로고    scopus 로고
    • Guide RNAs with 5′ caps and novel box C/D snoRNA-like domains for modification of snRNAs in metazoa
    • Tycowski K.T., Aab A., and Steitz J.A. Guide RNAs with 5′ caps and novel box C/D snoRNA-like domains for modification of snRNAs in metazoa. Curr. Biol. 14 (2004) 1985-1995
    • (2004) Curr. Biol. , vol.14 , pp. 1985-1995
    • Tycowski, K.T.1    Aab, A.2    Steitz, J.A.3
  • 53
    • 0032523934 scopus 로고    scopus 로고
    • Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis
    • Wang C., Chua K., Seghezzi W., Lees E., Gozani O., and Reed R. Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis. Genes Dev. 12 (1998) 1409-1414
    • (1998) Genes Dev. , vol.12 , pp. 1409-1414
    • Wang, C.1    Chua, K.2    Seghezzi, W.3    Lees, E.4    Gozani, O.5    Reed, R.6
  • 54
    • 34347386541 scopus 로고    scopus 로고
    • Developmental and cell cycle regulation of the Drosophila histone locus body
    • White A.E., Leslie M.E., Calvi B.R., Marzluff W.F., and Duronio R.J. Developmental and cell cycle regulation of the Drosophila histone locus body. Mol. Biol. Cell 18 (2007) 2491-2502
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2491-2502
    • White, A.E.1    Leslie, M.E.2    Calvi, B.R.3    Marzluff, W.F.4    Duronio, R.J.5
  • 55
    • 0037634375 scopus 로고    scopus 로고
    • Identification of both shared and distinct proteins in the major and minor spliceosomes
    • Will C.L., Schneider C., Reed R., and Lührmann R. Identification of both shared and distinct proteins in the major and minor spliceosomes. Science 284 (1999) 2003-2005
    • (1999) Science , vol.284 , pp. 2003-2005
    • Will, C.L.1    Schneider, C.2    Reed, R.3    Lührmann, R.4
  • 57
    • 0037119975 scopus 로고    scopus 로고
    • Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein
    • Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., and Lührmann R. Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. EMBO J. 21 (2002) 4978-4988
    • (2002) EMBO J. , vol.21 , pp. 4978-4988
    • Will, C.L.1    Urlaub, H.2    Achsel, T.3    Gentzel, M.4    Wilm, M.5    Lührmann, R.6
  • 58
    • 0023867362 scopus 로고
    • A 64 kd nuclear protein binds to RNA segments that include the AAUAAA polyadenylation motif
    • Wilusz J., and Shenk T. A 64 kd nuclear protein binds to RNA segments that include the AAUAAA polyadenylation motif. Cell 52 (1988) 221-228
    • (1988) Cell , vol.52 , pp. 221-228
    • Wilusz, J.1    Shenk, T.2
  • 59
    • 0027180675 scopus 로고
    • U7 small nuclear RNA in C snurposomes of the Xenopus germinal vesicle
    • Wu C.H., and Gall J.G. U7 small nuclear RNA in C snurposomes of the Xenopus germinal vesicle. Proc. Natl. Acad. Sci. USA 90 (1993) 6257-6259
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6257-6259
    • Wu, C.H.1    Gall, J.G.2
  • 60
    • 0032189145 scopus 로고    scopus 로고
    • Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing
    • Yu Y.T., Shu M.D., and Steitz J.A. Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing. EMBO J. 17 (1998) 5783-5795
    • (1998) EMBO J. , vol.17 , pp. 5783-5795
    • Yu, Y.T.1    Shu, M.D.2    Steitz, J.A.3
  • 61
    • 0026716104 scopus 로고
    • SR proteins: a conserved family of pre-mRNA splicing factors
    • Zahler A.M., Lane W.S., Stolk J.A., and Roth M.B. SR proteins: a conserved family of pre-mRNA splicing factors. Genes Dev. 6 (1992) 837-847
    • (1992) Genes Dev. , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 62
    • 0037373095 scopus 로고    scopus 로고
    • Phosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase
    • Zheng L., Dominski Z., Yang X.C., Elms P., Raska C.S., Borchers C.H., and Marzluff W.F. Phosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase. Mol. Cell. Biol. 23 (2003) 1590-1601
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1590-1601
    • Zheng, L.1    Dominski, Z.2    Yang, X.C.3    Elms, P.4    Raska, C.S.5    Borchers, C.H.6    Marzluff, W.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.