메뉴 건너뛰기




Volumn 11, Issue 3, 1999, Pages 347-351

Coupling RNA polymerase II transcription with pre-mRNA processing

Author keywords

[No Author keywords available]

Indexed keywords

CHICKEN OVALBUMIN UPSTREAM PROMOTER TRANSCRIPTION FACTOR; MESSENGER RNA PRECURSOR; RIBONUCLEOPROTEIN; RNA POLYMERASE II;

EID: 0033152538     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80048-9     Document Type: Review
Times cited : (196)

References (51)
  • 1
    • 0021960698 scopus 로고
    • Transcription of herpes simplex virus tk sequences under the control of wild-type and mutant human RNA polymerase I promoters
    • Smale ST, Tjian R: Transcription of herpes simplex virus tk sequences under the control of wild-type and mutant human RNA polymerase I promoters. Mol Cell Biol 1985, 5:352-362.
    • (1985) Mol Cell Biol , vol.5 , pp. 352-362
    • Smale, S.T.1    Tjian, R.2
  • 2
    • 0023424069 scopus 로고
    • Specificity of RNA maturation pathways: RNAs transcribed by RNA polymerase III are not substrates for splicing or polyadenylation
    • Sisodia SS, Sollner WB, Cleveland DW: Specificity of RNA maturation pathways: RNAs transcribed by RNA polymerase III are not substrates for splicing or polyadenylation. Mol Cell Biol 1987, 7:3602-3612.
    • (1987) Mol Cell Biol , vol.7 , pp. 3602-3612
    • Sisodia, S.S.1    Sollner, W.B.2    Cleveland, D.W.3
  • 4
    • 0020522128 scopus 로고
    • Human beta-globin premRNA synthesized in vitro is accurately spliced in Xenopus oocyte nuclei
    • Green MR, Maniatis T, Melton DA: Human beta-globin premRNA synthesized in vitro is accurately spliced in Xenopus oocyte nuclei. Cell 1983, 32:681-694.
    • (1983) Cell , vol.32 , pp. 681-694
    • Green, M.R.1    Maniatis, T.2    Melton, D.A.3
  • 5
    • 0020731865 scopus 로고
    • Promoter-proximal pausing by RNA polymerase II in vitro: Transcripts shorter than 20 nucleotides are not capped
    • Coppola JA, Field AS, Luse DS: Promoter-proximal pausing by RNA polymerase II in vitro: Transcripts shorter than 20 nucleotides are not capped. Proc Natl Acad Sci USA 1983, 80:1251-1255.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1251-1255
    • Coppola, J.A.1    Field, A.S.2    Luse, D.S.3
  • 6
    • 0027166316 scopus 로고
    • In-vivo transcriptional pausing and cap formation on 3 Drosophila heat-shock genes
    • Rasmussen EB, Lis JT: In-vivo transcriptional pausing and cap formation on 3 Drosophila heat-shock genes. Proc Natl Acad Sci USA 1993, 90:7923-7927.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7923-7927
    • Rasmussen, E.B.1    Lis, J.T.2
  • 7
    • 0029870388 scopus 로고    scopus 로고
    • A nuclear capbinding complex binds balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export
    • Visa N, Izaurralde E, Ferreira J, Daneholt B, Mattaj IW: A nuclear capbinding complex binds balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export J Cell Biol 1996, 133:5-14.
    • (1996) J Cell Biol , vol.133 , pp. 5-14
    • Visa, N.1    Izaurralde, E.2    Ferreira, J.3    Daneholt, B.4    Mattaj, I.W.5
  • 8
    • 0030807902 scopus 로고    scopus 로고
    • An RNA 5′-triphosphatase related to the protein tyrosine phosphatases
    • Takagi T, Moore C, Diehn F, Buratowski S: An RNA 5′-triphosphatase related to the protein tyrosine phosphatases. Cell 1997, 89:867-873.
    • (1997) Cell , vol.89 , pp. 867-873
    • Takagi, T.1    Moore, C.2    Diehn, F.3    Buratowski, S.4
  • 9
    • 0031561370 scopus 로고    scopus 로고
    • Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability
    • Tsukamoto T, Shibagaki Y, Imajoh-Ohmi S, Murakoshi T, Suzuki M, Nakamura A, Gotoh H, Mizumoto K: Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability. Biochem Biophys Res Commun 1997, 239:116-122.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 116-122
    • Tsukamoto, T.1    Shibagaki, Y.2    Imajoh-Ohmi, S.3    Murakoshi, T.4    Suzuki, M.5    Nakamura, A.6    Gotoh, H.7    Mizumoto, K.8
  • 10
    • 3543026832 scopus 로고    scopus 로고
    • Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus
    • Ho CK, Schwer B, Shuman S: Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus. Mol Cell Biol 1998, 18:5189-5198.
    • (1998) Mol Cell Biol , vol.18 , pp. 5189-5198
    • Ho, C.K.1    Schwer, B.2    Shuman, S.3
  • 11
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus ME: Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J Biol Chem 1996, 271:19009-19012.
    • (1996) J Biol Chem , vol.271 , pp. 19009-19012
    • Dahmus, M.E.1
  • 12
    • 0028305843 scopus 로고
    • Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation
    • O'Brien T, Hardin S, Greenleaf A, Lis JT: Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation. Nature 1994, 370:75-77.
    • (1994) Nature , vol.370 , pp. 75-77
    • O'Brien, T.1    Hardin, S.2    Greenleaf, A.3    Lis, J.T.4
  • 13
    • 15644372864 scopus 로고    scopus 로고
    • 5′-capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II
    • McCracken S, Fong N, Rosonina E, Yankulov K, Brothers G, Siderovski D, Hessel A, Foster S, Amgen Est Program, Shuman S, Bentley D: 5′-capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II. Genes Dev 1997, 11:3306-3318. This study shows that capping in vivo is an RNA polymerase II CTD dependent processing step and that two of the capping enzymes bind the phosphorylated CTD in vitro.
    • (1997) Genes Dev , vol.11 , pp. 3306-3318
    • McCracken, S.1    Fong, N.2    Rosonina, E.3    Yankulov, K.4    Brothers, G.5    Siderovski, D.6    Hessel, A.7    Foster, S.8    Shuman, S.9    Bentley, D.10
  • 14
    • 0031453408 scopus 로고    scopus 로고
    • mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Cho EJ, Takagi T, Moore CR, Buratowski S: mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev 1997, 11:3319-3326. The authors report the important result that yeast guanylyltransferase associates with ternary complexes of DNA, RNA transcript and phosphorylated RNA pol II. They also demonstrate a genetic interaction between the pol II CTD and yeast guanylyltransferase.
    • (1997) Genes Dev , vol.11 , pp. 3319-3326
    • Cho, E.J.1    Takagi, T.2    Moore, C.R.3    Buratowski, S.4
  • 15
    • 0030660264 scopus 로고    scopus 로고
    • Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA pol II
    • Yue Z, Maldonado E, Pilluta R, Cho H, Reinberg D, Shatkin A: Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA pol II. Proc Natl Acad Sci USA 1997, 94:12898-12903. Demonstrates binding of mammalian capping enzyme to elongating (phosphorylated) RNA pol II but not the initiating (nonphosphorylated) form.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12898-12903
    • Yue, Z.1    Maldonado, E.2    Pilluta, R.3    Cho, H.4    Reinberg, D.5    Shatkin, A.6
  • 16
    • 0032540231 scopus 로고    scopus 로고
    • The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Ho CK, Sriskanda V, McCracken S, Bentley D, Schwer B, Shuman S: The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II. J Biol Chem 1998, 273:9577-9585.
    • (1998) J Biol Chem , vol.273 , pp. 9577-9585
    • Ho, C.K.1    Sriskanda, V.2    McCracken, S.3    Bentley, D.4    Schwer, B.5    Shuman, S.6
  • 17
    • 0032533898 scopus 로고    scopus 로고
    • Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain
    • Cho EJ, Rodriguez CR, Takagi T, Buratowski S: Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain. Genes Dev 1998, 12:3482-3487. Shows for the first time regulation of the activity of a processing factor, yeast guanylyltransferase, by its interaction with the RNA pol II CTD.
    • (1998) Genes Dev , vol.12 , pp. 3482-3487
    • Cho, E.J.1    Rodriguez, C.R.2    Takagi, T.3    Buratowski, S.4
  • 18
    • 0033105827 scopus 로고    scopus 로고
    • Distinct effector roles for Ser2 and Ser5 phosphorylation of the RNA polymerase II CTD in the recruitment and allosteric activation of mammalian capping enzyme
    • Ho C, Shuman S: Distinct effector roles for Ser2 and Ser5 phosphorylation of the RNA polymerase II CTD in the recruitment and allosteric activation of mammalian capping enzyme. Mol Cell 1999, 3:405-411. The authors show that a peptide with only four CTD heptad repeats not only binds mammalian guanylyltransferase but also activates it. Activation is dependent on a particular phosphorylated serine residue (Ser5) in the RNA pol II CTD repeat.
    • (1999) Mol Cell , vol.3 , pp. 405-411
    • Ho, C.1    Shuman, S.2
  • 20
    • 0031882755 scopus 로고    scopus 로고
    • RNA polymerase i-promoted HIS4 expression yields uncapped, polyadenylated mRNA that is unstable and inefficiently translated in Saccharomyces cerevisiae
    • Lo HJ, Huang HK, Donahue TF: RNA polymerase i-promoted HIS4 expression yields uncapped, polyadenylated mRNA that is unstable and inefficiently translated in Saccharomyces cerevisiae. Mol Cell Biol 1998, 18:665-675.
    • (1998) Mol Cell Biol , vol.18 , pp. 665-675
    • Lo, H.J.1    Huang, H.K.2    Donahue, T.F.3
  • 21
    • 0031037856 scopus 로고    scopus 로고
    • The C-terminal domain of RNA polymerase II couples messenger RNA processing to transcription
    • McCracken S, Fong N, Yankulov K, Ballantyne S, Pan GH, Greenblatt J, Patterson SD, Wickens M, Bentley DL: The C-terminal domain of RNA polymerase II couples messenger RNA processing to transcription. Nature 1997, 385:357-361. This study shows that splicing, 3′-end processing and termination of pol II transcription are abrogated in transfected cells by deletion of the RNA pol II CTD. Interaction of the polyadenylation factors CstF and CPSF with RNA pol II is demonstrated.
    • (1997) Nature , vol.385 , pp. 357-361
    • McCracken, S.1    Fong, N.2    Yankulov, K.3    Ballantyne, S.4    Pan, G.H.5    Greenblatt, J.6    Patterson, S.D.7    Wickens, M.8    Bentley, D.L.9
  • 22
    • 0032529164 scopus 로고    scopus 로고
    • Activated transcription independent of the RNA polymerase II holoenzyme in budding yeast
    • McNeil JB, Agah H, Bentley D: Activated transcription independent of the RNA polymerase II holoenzyme in budding yeast. Genes Dev 1998, 12:2510-2521.
    • (1998) Genes Dev , vol.12 , pp. 2510-2521
    • McNeil, J.B.1    Agah, H.2    Bentley, D.3
  • 23
    • 0032480229 scopus 로고    scopus 로고
    • RNA polymerase II is an essential mRNA polyadenylation factor
    • Hirose Y, Manley JL: RNA polymerase II is an essential mRNA polyadenylation factor. Nature 1998, 395:93-96. This important study shows for the first time that the RNA pol II CTD can stimulate the transcript cleavage reaction independent of transcription. It may therefore function as a bona fide processing factor.
    • (1998) Nature , vol.395 , pp. 93-96
    • Hirose, Y.1    Manley, J.L.2
  • 24
    • 0030798246 scopus 로고    scopus 로고
    • Transcription factor TFIID recruits factor CPSF for formation of 3′ end of mRNA
    • Dantonel JC, Murthy KG, Manley JL, Tora L: Transcription factor TFIID recruits factor CPSF for formation of 3′ end of mRNA. Nature 1997, 389:399-402. The authors sequenced polypeptides of the basal transcription factor TFIID, and found, to everyone's surprise, that they include three subunits of the polyadenylation factor CPSF. They provide evidence for a handover of CPSF from TFIID to pol II when transcription starts.
    • (1997) Nature , vol.389 , pp. 399-402
    • Dantonel, J.C.1    Murthy, K.G.2    Manley, J.L.3    Tora, L.4
  • 25
    • 0024562757 scopus 로고
    • How RNA polymerase II terminates transcription in higher eukaryotes
    • Proudfoot NJ: How RNA polymerase II terminates transcription in higher eukaryotes. Trends Biochem Sci 1989, 14:105-110.
    • (1989) Trends Biochem Sci , vol.14 , pp. 105-110
    • Proudfoot, N.J.1
  • 26
    • 0032502825 scopus 로고    scopus 로고
    • Coupling termination of transcription to messenger RNA maturation in yeast
    • Birse CE, Minvielle-Sebastia L, Lee BA, Keller W, Proudfoot NJ: Coupling termination of transcription to messenger RNA maturation in yeast. Science 1998, 280:298-301. An elegant dissection of which components of the polyadenylation machinery are necessary for coupled termination. The authors demonstrate that the cleavage factor 1A is important but not the polyadenylation factor PF1.
    • (1998) Science , vol.280 , pp. 298-301
    • Birse, C.E.1    Minvielle-Sebastia, L.2    Lee, B.A.3    Keller, W.4    Proudfoot, N.J.5
  • 27
    • 0033106189 scopus 로고    scopus 로고
    • EM visualization of transcription by RNA polymerase II: Downstream termination requires a poly(A) signal but not transcript cleavage
    • Osheim Y, Proudfoot N, Beyer A: EM visualization of transcription by RNA polymerase II: Downstream termination requires a poly(A) signal but not transcript cleavage. Mol Cell 1999, 3:379-387. A graphic demonstration that RNA transcript cleavage is not a necessary pre-requisite for termination of transcription by RNA pol II.
    • (1999) Mol Cell , vol.3 , pp. 379-387
    • Osheim, Y.1    Proudfoot, N.2    Beyer, A.3
  • 28
    • 0033105008 scopus 로고    scopus 로고
    • Terminal exon definition occurs cotranscriptionally and promotes termination of RNA polymerase II
    • Dye M, Proudfoot N: Terminal exon definition occurs cotranscriptionally and promotes termination of RNA polymerase II. Mol Cell 1999, 3:371-378. This study uses a novel nuclear run-on method to show that transcripts elongated in isolated nuclei can extend far beyond the poly(A) site without being cleaved. It also reports that splicing of the terminal intron is coupled to termination.
    • (1999) Mol Cell , vol.3 , pp. 371-378
    • Dye, M.1    Proudfoot, N.2
  • 29
    • 0032167935 scopus 로고    scopus 로고
    • Transcriptional termination in the balbiani ring 1 gene is closely coupled to 3′-end formation and excision of the 3′-terminal intron
    • Bauren G, Belikov S, Wieslander L: Transcriptional termination in the balbiani ring 1 gene is closely coupled to 3′-end formation and excision of the 3′-terminal intron. Genes Dev 1998, 12:2759-2769. A tour de force, probably the most thorough analysis ever of events at the 3′-end of an RNA pol II transcription unit. The authors demonstrate that closely coupled cleavage, polyadenylation, termination, and splicing of the last intron occur when the polymerase reaches a point 600 bases downstream of the poly(A) site.
    • (1998) Genes Dev , vol.12 , pp. 2759-2769
    • Bauren, G.1    Belikov, S.2    Wieslander, L.3
  • 30
    • 0024988383 scopus 로고
    • In vitro polyadenylation is stimulated by the presence of an upstream intron
    • Niwa M, Rose SD, Berget SM: In vitro polyadenylation is stimulated by the presence of an upstream intron. Genes Dev 1990, 4:1552-1559.
    • (1990) Genes Dev , vol.4 , pp. 1552-1559
    • Niwa, M.1    Rose, S.D.2    Berget, S.M.3
  • 31
    • 0027175493 scopus 로고
    • Sequences within the last intron function in RNA 3′-end formation in cultured cells
    • Nesic D, Cheng J, Maquat LE: Sequences within the last intron function in RNA 3′-end formation in cultured cells. Mol Cell Biol 1993, 13:3359-3369.
    • (1993) Mol Cell Biol , vol.13 , pp. 3359-3369
    • Nesic, D.1    Cheng, J.2    Maquat, L.E.3
  • 33
    • 0031815767 scopus 로고    scopus 로고
    • A subset of poly(A) polymerase is concentrated at sites of RNA synthesis and is associated with domains enriched in splicing factors and poly(A) RNA
    • Schul W, van Driel R, de Jong L: A subset of poly(A) polymerase is concentrated at sites of RNA synthesis and is associated with domains enriched in splicing factors and poly(A) RNA. Exp Cell Res 1998, 238:1-12. A thorough quantitative study of the co-localisation of sites of pol II transcription with RNA processing factors in the nucleoplasm.
    • (1998) Exp Cell Res , vol.238 , pp. 1-12
    • Schul, W.1    Van Driel, R.2    De Jong, L.3
  • 34
    • 0029931320 scopus 로고    scopus 로고
    • The RNA 3′ cleavage factors CstF 64 kDa and CPSF 100 kDa are concentrated in nuclear domains closely associated with coiled bodies and newly synthesized RNA
    • Schul W, Groenhout B, KOberna K, Takagaki Y, Jenny A, Manders E, Raska I, van Driel R, de Jong L: The RNA 3′ cleavage factors CstF 64 kDa and CPSF 100 kDa are concentrated in nuclear domains closely associated with coiled bodies and newly synthesized RNA. EMBO J 1996, 15:2883-2892.
    • (1996) EMBO J , vol.15 , pp. 2883-2892
    • Schul, W.1    Groenhout, B.2    Koberna, K.3    Takagaki, Y.4    Jenny, A.5    Manders, E.6    Raska, I.7    Van Driel, R.8    De Jong, L.9
  • 35
    • 0024021747 scopus 로고
    • Splice site selection, rate of splicing, and alternative splicing on nascent transcripts
    • Beyer AL, Osheim YN: Splice site selection, rate of splicing, and alternative splicing on nascent transcripts. Genes Dev 1988, 2:754-765.
    • (1988) Genes Dev , vol.2 , pp. 754-765
    • Beyer, A.L.1    Osheim, Y.N.2
  • 36
    • 0027957779 scopus 로고
    • Splicing of balbiani ring 1 gene pre-mRNA occurs simultaneously with transcription
    • Bauren G, Wieslander L: Splicing of balbiani ring 1 gene pre-mRNA occurs simultaneously with transcription. Cell 1994, 76:183-192.
    • (1994) Cell , vol.76 , pp. 183-192
    • Bauren, G.1    Wieslander, L.2
  • 38
    • 0031032049 scopus 로고    scopus 로고
    • Functional interaction between the carboxy terminal domain of RNA polymerase II and pre-messenger RNA splicing
    • Du L, Warren SL: Functional interaction between the carboxy terminal domain of RNA polymerase II and pre-messenger RNA splicing. J Cell Biol 1997, 136:5-18. Some of the first evidence of a functional role of the RNA pol II CTD in splicing in vivo. Demonstrates that CTD overexpression inhibits splicing.
    • (1997) J Cell Biol , vol.136 , pp. 5-18
    • Du, L.1    Warren, S.L.2
  • 39
    • 0031022189 scopus 로고    scopus 로고
    • Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-messenger RNA
    • Kim E, Du L, Bregman DB, Warren SL: Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-messenger RNA. J Cell Biol 1997, 136:19-28. This study provides some of the best evidence for biochemical interactions between splicing factors and phosphorylated RNA pol II.
    • (1997) J Cell Biol , vol.136 , pp. 19-28
    • Kim, E.1    Du, L.2    Bregman, D.B.3    Warren, S.L.4
  • 41
    • 0029822049 scopus 로고    scopus 로고
    • The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes
    • Vincent M, Lauriault P, Dubois MF, Lavoie S, Bensaude O, Chabot B: The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes. Nucleic Acids Res 1996, 24:4649-4652.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4649-4652
    • Vincent, M.1    Lauriault, P.2    Dubois, M.F.3    Lavoie, S.4    Bensaude, O.5    Chabot, B.6
  • 42
    • 0031923752 scopus 로고    scopus 로고
    • A nuclear matrix protein interacts with the phosphorylated C-terminal domain of RNA polymerase II
    • Patturajan M, Wei X, Berezney R, Corden JL: A nuclear matrix protein interacts with the phosphorylated C-terminal domain of RNA polymerase II. Mol Cell Biol 1998, 18:2406-2415. This study characterises a member of a family of nuclear matrix associated proteins, SCAFs, with SR-rich domains and a conserved domain that binds strongly to phosphorylated RNA pol II CTD.
    • (1998) Mol Cell Biol , vol.18 , pp. 2406-2415
    • Patturajan, M.1    Wei, X.2    Berezney, R.3    Corden, J.L.4
  • 43
    • 0030670094 scopus 로고    scopus 로고
    • A CTD function linking transcription to splicing
    • Corden JL, Patturajan M: A CTD function linking transcription to splicing. Trends Biochem Sci 1997, 22:413-416.
    • (1997) Trends Biochem Sci , vol.22 , pp. 413-416
    • Corden, J.L.1    Patturajan, M.2
  • 44
    • 0030844256 scopus 로고    scopus 로고
    • A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II
    • Bourquin JP, Stagljar I, Meier P, Moosmann P, Silke J, Baechi T, Georgiev O, Schaffner W: A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II. Nucleic Acids Res 1997, 25:2055-2061. Describes a new RNA pol II CTD binding protein with an SR-rich domain and a peptidyl-prolyl isomerase domain.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2055-2061
    • Bourquin, J.P.1    Stagljar, I.2    Meier, P.3    Moosmann, P.4    Silke, J.5    Baechi, T.6    Georgiev, O.7    Schaffner, W.8
  • 45
    • 0030761276 scopus 로고    scopus 로고
    • Functional association between promoter structure and transcripts alternative splicing
    • Cramer P, Pesce C, Baralle F, Kornblihtt A: Functional association between promoter structure and transcripts alternative splicing. Proc Natl Acad Sci USA 1997, 94:11456-11460. This paper documents a role of the promoter in the control of splicing. Mutation of two discrete promoter elements altered the frequency of inclusion of an alternative fibronectin exon which depends on an exonic splicing enhancer.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11456-11460
    • Cramer, P.1    Pesce, C.2    Baralle, F.3    Kornblihtt, A.4
  • 46
    • 0027143943 scopus 로고
    • A splicing enhancer in the human fibronectin alternate ED1 exon interacts with SR proteins and stimulates U2 snRNP binding
    • Lavigueur A, La Branche H, Kornblihtt AR, Chabot B: A splicing enhancer in the human fibronectin alternate ED1 exon interacts with SR proteins and stimulates U2 snRNP binding. Genes Dev 1993, 7:2405-2417.
    • (1993) Genes Dev , vol.7 , pp. 2405-2417
    • Lavigueur, A.1    La Branche, H.2    Kornblihtt, A.R.3    Chabot, B.4
  • 47
    • 0029064220 scopus 로고
    • The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities
    • Tacke R, Manley JL: The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities. EMBO J 1995, 14:3540-3551.
    • (1995) EMBO J , vol.14 , pp. 3540-3551
    • Tacke, R.1    Manley, J.L.2
  • 48
    • 0032538795 scopus 로고    scopus 로고
    • Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation
    • Ge H, Si Y, Roeder RG: Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation. EMBO J 1998, 17:6723-6729.
    • (1998) EMBO J , vol.17 , pp. 6723-6729
    • Ge, H.1    Si, Y.2    Roeder, R.G.3
  • 49
    • 0032239750 scopus 로고    scopus 로고
    • A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2
    • Ge H, Si Y, Wolffe AP: A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2. Mol Cell 1998, 2:751-759. This study reports the remarkable finding that a co-activator of RNA pol II transcription in vitro binds to and functionally synergises with the splicing factor ASF/SF2.
    • (1998) Mol Cell , vol.2 , pp. 751-759
    • Ge, H.1    Si, Y.2    Wolffe, A.P.3
  • 50
    • 0029961361 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Rev function requires continued synthesis of its target mRNA
    • Iacampo S, Cochrane A: Human immunodeficiency virus type 1 Rev function requires continued synthesis of its target mRNA. J Virol 1996, 70:8332-8339.
    • (1996) J Virol , vol.70 , pp. 8332-8339
    • Iacampo, S.1    Cochrane, A.2
  • 51
    • 0030034421 scopus 로고    scopus 로고
    • A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes
    • Visa N, Alzhanova EA, Sun X, Kiseleva E, BJoerkroth B, Wurtz T, Daneholt B: A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes. Cell 1996, 84:253-264.
    • (1996) Cell , vol.84 , pp. 253-264
    • Visa, N.1    Alzhanova, E.A.2    Sun, X.3    Kiseleva, E.4    Bjoerkroth, B.5    Wurtz, T.6    Daneholt, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.