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Volumn 35, Issue 13, 2007, Pages 4485-4494

Transcriptional co-activator protein p100 interacts with snRNP proteins and facilitates the assembly of the spliceosome

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; MESSENGER RNA; PROTEIN P100; SMALL NUCLEAR RIBONUCLEOPROTEIN; TUDOR STAPHYLOCOCCUS NUCLEASE; UNCLASSIFIED DRUG; NUCLEAR PROTEIN; RNA PRECURSOR; SND1 PROTEIN, HUMAN;

EID: 34547829272     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm470     Document Type: Article
Times cited : (104)

References (43)
  • 1
    • 0034657917 scopus 로고    scopus 로고
    • Modulation of STAT signaling by STAT-interacting proteins
    • Shuai,K. (2000) Modulation of STAT signaling by STAT-interacting proteins. Oncogene, 19, 2638-2644.
    • (2000) Oncogene , vol.19 , pp. 2638-2644
    • Shuai, K.1
  • 2
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • Will,C.L. and Luhrmann,R. (2001) Spliceosomal UsnRNP biogenesis, structure and function. Curr. Opin. Cell. Biol., 13, 290-301.
    • (2001) Curr. Opin. Cell. Biol , vol.13 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 3
    • 19344378943 scopus 로고    scopus 로고
    • Rules of engagement: Co-transcriptional recruitment of pre-mRNA processing factors
    • Bentley,D.L. (2005) Rules of engagement: Co-transcriptional recruitment of pre-mRNA processing factors. Curr. Opin. Cell. Biol., 17, 251-256.
    • (2005) Curr. Opin. Cell. Biol , vol.17 , pp. 251-256
    • Bentley, D.L.1
  • 4
    • 2142716979 scopus 로고    scopus 로고
    • The link between mRNA processing and transcription: Communication works both ways
    • Zorio,D.A. and Bentley,D.L. (2004) The link between mRNA processing and transcription: Communication works both ways. Exp. Cell Res., 296, 91-97.
    • (2004) Exp. Cell Res , vol.296 , pp. 91-97
    • Zorio, D.A.1    Bentley, D.L.2
  • 6
    • 11844252046 scopus 로고    scopus 로고
    • The C-terminal domain of RNA polymerase II functions as a phosphorylation-dependent splicing activator in a heterologous protein
    • Millhouse,S. and Manley,J.L. (2005) The C-terminal domain of RNA polymerase II functions as a phosphorylation-dependent splicing activator in a heterologous protein. Mol. Cell. Biol., 25, 533-544.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 533-544
    • Millhouse, S.1    Manley, J.L.2
  • 7
    • 0030670094 scopus 로고    scopus 로고
    • A CTD function linking transcription to splicing
    • Corden,J.L. and Patturajan,M. (1997) A CTD function linking transcription to splicing. Trends Biochem. Sci., 22, 413-416.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 413-416
    • Corden, J.L.1    Patturajan, M.2
  • 8
    • 33745220323 scopus 로고    scopus 로고
    • Linking splicing to Pol II transcription stabilizes pre-mRNAs and influences splicing patterns
    • Hicks,M.J., Yang,C.R., Kotlajich,M.V. and Hertel,K.J. (2006) Linking splicing to Pol II transcription stabilizes pre-mRNAs and influences splicing patterns. PLoS Biol., 4, e147.
    • (2006) PLoS Biol , vol.4
    • Hicks, M.J.1    Yang, C.R.2    Kotlajich, M.V.3    Hertel, K.J.4
  • 9
    • 33751090746 scopus 로고    scopus 로고
    • Phosphorylation and functions of the RNA polymerase II CTD
    • Phatnani,H.P. and Greenleaf,A.L. (2006) Phosphorylation and functions of the RNA polymerase II CTD. Genes Dev., 20, 2922-2936.
    • (2006) Genes Dev , vol.20 , pp. 2922-2936
    • Phatnani, H.P.1    Greenleaf, A.L.2
  • 11
    • 33645765165 scopus 로고    scopus 로고
    • RNA editing and alternative splicing: The importance of co-transcriptional coordination
    • Laurencikiene,J., Kallman,A.M., Fong,N., Bentley,D.L. and Ohman,M. (2006) RNA editing and alternative splicing: The importance of co-transcriptional coordination. EMBO Rep., 7, 303-307.
    • (2006) EMBO Rep , vol.7 , pp. 303-307
    • Laurencikiene, J.1    Kallman, A.M.2    Fong, N.3    Bentley, D.L.4    Ohman, M.5
  • 12
    • 2142763884 scopus 로고    scopus 로고
    • Tobramycin affinity tag purification of spliceosomes
    • Hartmuth,K., Vornlocher,H.P. and Luhrmann,R. (2004) Tobramycin affinity tag purification of spliceosomes. Methods Mol. Biol., 257, 47-64.
    • (2004) Methods Mol. Biol , vol.257 , pp. 47-64
    • Hartmuth, K.1    Vornlocher, H.P.2    Luhrmann, R.3
  • 13
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber,J., Ryder,U., Lamond,A.I. and Mann,M. (2002) Large-scale proteomic analysis of the human spliceosome. Genome Res., 12 1231-1245.
    • (2002) Genome Res , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 14
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R. (2002) Comprehensive proteomic analysis of the human spliceosome. Nature, 419, 182-185.
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 15
    • 0031865048 scopus 로고    scopus 로고
    • CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2 through an unusual RNA recognition motif
    • Yan,D., Perriman,R., Igel,H., Howe,K.J., Neville,M. and Ares,M.Jr. (1998) CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2 through an unusual RNA recognition motif. Mol. Cell Biol., 18, 5000-5009.
    • (1998) Mol. Cell Biol , vol.18 , pp. 5000-5009
    • Yan, D.1    Perriman, R.2    Igel, H.3    Howe, K.J.4    Neville, M.5    Ares Jr., M.6
  • 16
    • 6344277922 scopus 로고    scopus 로고
    • FF domains of CA150 bind transcription and splicing factors through multiple weak interactions
    • Smith,M.J., Kulkarni,S. and Pawson,T. (2004) FF domains of CA150 bind transcription and splicing factors through multiple weak interactions. Mol. Cell Biol., 24, 9274-9285.
    • (2004) Mol. Cell Biol , vol.24 , pp. 9274-9285
    • Smith, M.J.1    Kulkarni, S.2    Pawson, T.3
  • 17
    • 0042818072 scopus 로고    scopus 로고
    • Nuclear coactivator-62 kDa/ Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing
    • Zhang,C., Dowd,D.R., Staal,A., Gu,C., Lian,J.B., van Wijnen,A.J., Stein,G.S. and MacDonald,P.N. (2003) Nuclear coactivator-62 kDa/ Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing. J. Biol. Chem., 278, 35325-35336.
    • (2003) J. Biol. Chem , vol.278 , pp. 35325-35336
    • Zhang, C.1    Dowd, D.R.2    Staal, A.3    Gu, C.4    Lian, J.B.5    van Wijnen, A.J.6    Stein, G.S.7    MacDonald, P.N.8
  • 18
    • 0029131021 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE
    • Tong,X., Drapkin,R., Yalamanchili,R., Mosialos,G. and Kieff,E. (1995) The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. Mol. Cell. Biol., 15, 4735-4744.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 4735-4744
    • Tong, X.1    Drapkin, R.2    Yalamanchili, R.3    Mosialos, G.4    Kieff, E.5
  • 20
    • 17644374227 scopus 로고    scopus 로고
    • The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6
    • Valineva,T., Yang,J., Palovuori,R. and Silvennoinen,O. (2005) The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6. J. Biol. Chem., 280, 14989-14996.
    • (2005) J. Biol. Chem , vol.280 , pp. 14989-14996
    • Valineva, T.1    Yang, J.2    Palovuori, R.3    Silvennoinen, O.4
  • 22
    • 0042835769 scopus 로고    scopus 로고
    • Tudor and nuclease-like domains containing protein p100 function as coactivators for signal transducer and activator of transcription 5
    • Paukku,K., Yang,J. and Silvennoinen,O. (2003) Tudor and nuclease-like domains containing protein p100 function as coactivators for signal transducer and activator of transcription 5. Mol. Endocrinol., 17, 1805-1814.
    • (2003) Mol. Endocrinol , vol.17 , pp. 1805-1814
    • Paukku, K.1    Yang, J.2    Silvennoinen, O.3
  • 23
    • 23044512471 scopus 로고    scopus 로고
    • The p100 EBNA-2 coactivator: A highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle
    • Broadhurst,M.K., Lee,R.S., Hawkins,S. and Wheeler,T.T. (2005) The p100 EBNA-2 coactivator: A highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle. Biochim. Biophys. Acta, 1681, 126-133.
    • (2005) Biochim. Biophys. Acta , vol.1681 , pp. 126-133
    • Broadhurst, M.K.1    Lee, R.S.2    Hawkins, S.3    Wheeler, T.T.4
  • 24
    • 29744470060 scopus 로고    scopus 로고
    • Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease
    • Low,S.H., Vasanth,S., Larson,C.H., Mukherjee,S., Sharma,N., Kinter,M.T., Kane,M.E., Obara,T. and Weimbs,T. (2006) Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease. Dev. Cell, 10, 57-69.
    • (2006) Dev. Cell , vol.10 , pp. 57-69
    • Low, S.H.1    Vasanth, S.2    Larson, C.H.3    Mukherjee, S.4    Sharma, N.5    Kinter, M.T.6    Kane, M.E.7    Obara, T.8    Weimbs, T.9
  • 25
    • 22144444302 scopus 로고    scopus 로고
    • The RISC subunit Tudor-SN binds to hyper-edited double-stranded RNA and promotes its cleavage
    • Scadden,A.D. (2005) The RISC subunit Tudor-SN binds to hyper-edited double-stranded RNA and promotes its cleavage. Nat. Struct. Mol. Biol., 12, 489-496.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 489-496
    • Scadden, A.D.1
  • 26
    • 0031027360 scopus 로고    scopus 로고
    • The human EBNA-2 coactivator p100: Multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development
    • Callebaut,I. and Mornon,J.P. (1997) The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development. Biochem. J., 321 (Pt 1), 125-132.
    • (1997) Biochem. J , vol.321 , Issue.PART 1 , pp. 125-132
    • Callebaut, I.1    Mornon, J.P.2
  • 29
    • 0033119176 scopus 로고    scopus 로고
    • Initial recognition of U12-dependent introns requires both U11/5' splice-site and U12/ branchpoint interactions
    • Frilander,M.J. and Steitz,J.A. (1999) Initial recognition of U12-dependent introns requires both U11/5' splice-site and U12/ branchpoint interactions. Genes Dev., 13, 851-863.
    • (1999) Genes Dev , vol.13 , pp. 851-863
    • Frilander, M.J.1    Steitz, J.A.2
  • 30
    • 20344369784 scopus 로고    scopus 로고
    • Proximity of the U12 snRNA with both the 5' splice site and the branch point during early stages of spliceosome assembly
    • Frilander,M.J. and Meng,X. (2005) Proximity of the U12 snRNA with both the 5' splice site and the branch point during early stages of spliceosome assembly. Mol. Cell. Biol., 25, 4813-4825.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 4813-4825
    • Frilander, M.J.1    Meng, X.2
  • 31
    • 33749261487 scopus 로고    scopus 로고
    • The abundance of the spliceosomal snRNPs is not limiting the splicing of U12-type introns
    • Pessa,H.K., Ruokolainen,A. and Frilander,M.J. (2006) The abundance of the spliceosomal snRNPs is not limiting the splicing of U12-type introns. RNA, 12, 1883-1892.
    • (2006) RNA , vol.12 , pp. 1883-1892
    • Pessa, H.K.1    Ruokolainen, A.2    Frilander, M.J.3
  • 32
    • 0020655280 scopus 로고
    • Purification of snRNPs U1, U2, U4, US and U6 with 2,2,7-trimethylguanosine-specific antibody and definition of their constituent proteins reacting with anti-Sm and anti-(U1)RNP antisera
    • Bringmann,P., Rinke,J., Appel,B., Reuter,R. and Luhrmann,R. (1983) Purification of snRNPs U1, U2, U4, US and U6 with 2,2,7-trimethylguanosine-specific antibody and definition of their constituent proteins reacting with anti-Sm and anti-(U1)RNP antisera. EMBO J., 2, 1129-1135.
    • (1983) EMBO J , vol.2 , pp. 1129-1135
    • Bringmann, P.1    Rinke, J.2    Appel, B.3    Reuter, R.4    Luhrmann, R.5
  • 33
    • 0026111471 scopus 로고
    • Assembly and intracellular transport of snRNP particles
    • Andersen,J. and Zieve,G.W. (1991) Assembly and intracellular transport of snRNP particles. Bioessays, 13, 57-64.
    • (1991) Bioessays , vol.13 , pp. 57-64
    • Andersen, J.1    Zieve, G.W.2
  • 34
    • 0033608216 scopus 로고    scopus 로고
    • An homologue of the human 100-kDa protein (p100) is differentially expressed by Histoplasma capsulatum during infection of murine macrophages
    • Porta,A., Colonna-Romano,S., Callebaut,I., Franco,A., Marzullo,L., Kobayashi,G.S. and Maresca,B. (1999) An homologue of the human 100-kDa protein (p100) is differentially expressed by Histoplasma capsulatum during infection of murine macrophages. Biochem. Biophys. Res. Commun., 254, 605-613.
    • (1999) Biochem. Biophys. Res. Commun , vol.254 , pp. 605-613
    • Porta, A.1    Colonna-Romano, S.2    Callebaut, I.3    Franco, A.4    Marzullo, L.5    Kobayashi, G.S.6    Maresca, B.7
  • 35
    • 0037337719 scopus 로고    scopus 로고
    • A Tudor protein with multiple SNc domains from pea seedlings: Cellular localization, partial characterization, sequence analysis, and phylogenetic relationships
    • Abe,S., Sakai,M., Yagi,K., Hagino,T., Ochi,K., Shibata,K. and Davies,E. (2003) A Tudor protein with multiple SNc domains from pea seedlings: cellular localization, partial characterization, sequence analysis, and phylogenetic relationships. J. Exp. Bot., 54, 971-983.
    • (2003) J. Exp. Bot , vol.54 , pp. 971-983
    • Abe, S.1    Sakai, M.2    Yagi, K.3    Hagino, T.4    Ochi, K.5    Shibata, K.6    Davies, E.7
  • 36
    • 0032515969 scopus 로고    scopus 로고
    • The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro
    • Laggerbauer,B., Achsel,T. and Luhrmann,R. (1998) The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro. Proc. Natl Acad. Sci. USA, 95, 4188-4192.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4188-4192
    • Laggerbauer, B.1    Achsel, T.2    Luhrmann, R.3
  • 37
    • 0030826730 scopus 로고    scopus 로고
    • The role of U5 snRNP in pre-mRNA splicing
    • Newman,A.J. (1997) The role of U5 snRNP in pre-mRNA splicing. EMBO J. 16, 5797-5800.
    • (1997) EMBO J , vol.16 , pp. 5797-5800
    • Newman, A.J.1
  • 39
    • 0031741144 scopus 로고    scopus 로고
    • The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein
    • Achsel,T., Ahrens,K., Brahms,H., Teigelkamp,S. and Luhrmann,R. (1998) The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein. Mol. Cell. Biol., 18, 6756-6766.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 6756-6766
    • Achsel, T.1    Ahrens, K.2    Brahms, H.3    Teigelkamp, S.4    Luhrmann, R.5
  • 40
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms,H., Meheus,L., de Brabandere,V., Fischer,U. and Luhrmann,R. (2001) Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA, 7, 1531-1542.
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    de Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 41
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • Cote,J. and Richard,S. (2005) Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem., 280, 28476-28483.
    • (2005) J. Biol. Chem , vol.280 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 42
    • 0035903086 scopus 로고    scopus 로고
    • SPF 30 is an essential human splicing factor required for assembly of the U4/U5/U6. tri-small nuclear ribonucleoprotein into the spliceosome
    • Rappsilber,J., Ajuh,P., Lamond,A.I. and Mann,M. (2001) SPF 30 is an essential human splicing factor required for assembly of the U4/U5/U6. tri-small nuclear ribonucleoprotein into the spliceosome. J. Biol. Chem., 276, 31142-31150.
    • (2001) J. Biol. Chem , vol.276 , pp. 31142-31150
    • Rappsilber, J.1    Ajuh, P.2    Lamond, A.I.3    Mann, M.4
  • 43
    • 0035341214 scopus 로고    scopus 로고
    • SMNrp is an essential pre-mRNA splicing factor required for the formation of the mature spliceosome
    • Meister,G., Hannus,S., Plottner,O., Baars,T., Hartmann,E., Fakan,S., Laggerbauer,B. and Fischer,U. (2001) SMNrp is an essential pre-mRNA splicing factor required for the formation of the mature spliceosome. EMBO J., 20, 2304-2314.
    • (2001) EMBO J , vol.20 , pp. 2304-2314
    • Meister, G.1    Hannus, S.2    Plottner, O.3    Baars, T.4    Hartmann, E.5    Fakan, S.6    Laggerbauer, B.7    Fischer, U.8


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