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Volumn 63, Issue , 1998, Pages 301-309

Role of RNA polymerase II carboxy-terminal domain in coordinating transcription with RNA processing

Author keywords

[No Author keywords available]

Indexed keywords

RNA; RNA POLYMERASE II; ALPHA AMANITIN; CYCLIN DEPENDENT KINASE 7; CYCLIN H; GUANOSINE TRIPHOSPHATASE; METHYLTRANSFERASE; PREGNANCY SPECIFIC BETA1 GLYCOPROTEIN; PROTEIN VP16; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR GAL4; TRANSCRIPTION FACTOR IIH;

EID: 0032459207     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.1998.63.301     Document Type: Conference Paper
Times cited : (38)

References (61)
  • 1
    • 0029791943 scopus 로고    scopus 로고
    • Distinct activated and non-activated RNA polymerase II complexes in yeast
    • Akhtar A., Faye G., and Bentley D. 1996. Distinct activated and non-activated RNA polymerase II complexes in yeast. EMBO J. 15: 4654.
    • (1996) EMBO J. , vol.15 , pp. 4654
    • Akhtar, A.1    Faye, G.2    Bentley, D.3
  • 2
    • 0022132080 scopus 로고
    • Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases
    • Allison L.A., Moyle M., Shales M., and Ingles C.J. 1985. Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases. Cell 42: 599.
    • (1985) Cell , vol.42 , pp. 599
    • Allison, L.A.1    Moyle, M.2    Shales, M.3    Ingles, C.J.4
  • 3
    • 0023737652 scopus 로고
    • Genetic analysis of the repetitive carboxyl-terminal domain of the largest subunit of mouse RNA polymerase II
    • Bartolomei M.S., Halden N.F., Cullen C.R., and Corden J.L. 1988. Genetic analysis of the repetitive carboxyl-terminal domain of the largest subunit of mouse RNA polymerase II. Mol Cell. Biol. 8: 330.
    • (1988) Mol Cell. Biol. , vol.8 , pp. 330
    • Bartolomei, M.S.1    Halden, N.F.2    Cullen, C.R.3    Corden, J.L.4
  • 4
    • 0028969391 scopus 로고
    • Regulation of transcriptional elongation by RNA polymerase II
    • Bentley D. 1995. Regulation of transcriptional elongation by RNA polymerase II. Curr. Opin. Genet. Dev. 5: 210.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 210
    • Bentley, D.1
  • 6
    • 0028900584 scopus 로고
    • Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains
    • Bregman D.B., Du L., van der Zee S., and Warren S.L. 1995. Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains. J. Cell Biol. 129: 287.
    • (1995) J. Cell Biol. , vol.129 , pp. 287
    • Bregman, D.B.1    Du, L.2    Van Der Zee, S.3    Warren, S.L.4
  • 7
    • 0025885556 scopus 로고
    • Simian virus 40 late mRNA leader sequences involved in augmenting mRNA accumulation via multiple mechanisms, including increased polyadenylation efficiency
    • Chiou H.C., Dabrowski C., and Alwine J.C. 1991. Simian virus 40 late mRNA leader sequences involved in augmenting mRNA accumulation via multiple mechanisms, including increased polyadenylation efficiency. J. Virol. 65: 6677.
    • (1991) J. Virol. , vol.65 , pp. 6677
    • Chiou, H.C.1    Dabrowski, C.2    Alwine, J.C.3
  • 8
    • 0029909605 scopus 로고    scopus 로고
    • Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV 1
    • Chun R.F. and Jeang K.T. 1996. Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV 1. J. Biol. Chem. 271: 27888.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27888
    • Chun, R.F.1    Jeang, K.T.2
  • 9
    • 0023990221 scopus 로고
    • A functional mRNA polyadenylation signal is required for transcription termination by RNA polymerase II
    • Connelly S. and Manley J.L. 1988. A functional mRNA polyadenylation signal is required for transcription termination by RNA polymerase II. Genes Dev. 2: 440.
    • (1988) Genes Dev. , vol.2 , pp. 440
    • Connelly, S.1    Manley, J.L.2
  • 10
    • 0029982647 scopus 로고    scopus 로고
    • The cap and the 3′ splice site similarly affect polyadenylation efficiency
    • Cooke C. and Alwine J.C. 1996. The cap and the 3′ splice site similarly affect polyadenylation efficiency. Mol. Cell. Biol. 16: 2579.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2579
    • Cooke, C.1    Alwine, J.C.2
  • 11
    • 0020731865 scopus 로고
    • Promoter-proximal pausing by RNA polymerase II in vitro: Transcripts shorter than 20 nucleotides are not capped
    • Coppola J.A., Field A.S., and Luse D.S. 1983. Promoter-proximal pausing by RNA polymerase II in vitro: Transcripts shorter than 20 nucleotides are not capped. Proc. Natl. Acad. Sci. 80: 1251.
    • (1983) Proc. Natl. Acad. Sci. , vol.80 , pp. 1251
    • Coppola, J.A.1    Field, A.S.2    Luse, D.S.3
  • 12
    • 0002076846 scopus 로고
    • Carboxy-terminal domain of the largest subunit of eukaryotic RNA polymerase II
    • (ed. S.L. McKnight and K.R. Yamamoto), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Corden J.L. and Ingles C.J. 1992. Carboxy-terminal domain of the largest subunit of eukaryotic RNA polymerase II. In Transcriptional regulation (ed. S.L. McKnight and K.R. Yamamoto), p. 81. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1992) Transcriptional Regulation , pp. 81
    • Corden, J.L.1    Ingles, C.J.2
  • 13
    • 0009370184 scopus 로고
    • A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II
    • Corden J.L., Cadena D.L., Ahearn J.M., Jr., and Dahmus M.E. 1985. A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II. Proc. Natl. Acad. Sci. 82: 7934.
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 7934
    • Corden, J.L.1    Cadena, D.L.2    Ahearn Jr., J.M.3    Dahmus, M.E.4
  • 14
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus M.E. 1996. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem.271: 19009.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19009
    • Dahmus, M.E.1
  • 15
    • 0031032049 scopus 로고    scopus 로고
    • Functional interaction between the carboxy-terminal domain of RNA and pre-mRNA splicing
    • Du L. and Warren S.L. 1997. Functional interaction between the carboxy-terminal domain of RNA and pre-mRNA splicing. J. Cell Biol. 136: 5.
    • (1997) J. Cell Biol. , vol.136 , pp. 5
    • Du, L.1    Warren, S.L.2
  • 16
    • 0029030491 scopus 로고
    • An efficient strategy to isolate full-length cDNAs based on an mRNA cap retention procedure (CAPture)
    • Edery I., Chu L.L., Sonenberg N., and Pelletier J. 1995. An efficient strategy to isolate full-length cDNAs based on an mRNA cap retention procedure (CAPture). Mol. Cell. Biol. 15: 3363.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3363
    • Edery, I.1    Chu, L.L.2    Sonenberg, N.3    Pelletier, J.4
  • 17
    • 0039243885 scopus 로고    scopus 로고
    • Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription
    • Garcia-Martinez L.F., Mavankal G., Neveu J.M., Lane W.S., Ivanov D., and Gaynor R.B. 1997. Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription. EMBO J. 16: 2836.
    • (1997) EMBO J. , vol.16 , pp. 2836
    • Garcia-Martinez, L.F.1    Mavankal, G.2    Neveu, J.M.3    Lane, W.S.4    Ivanov, D.5    Gaynor, R.B.6
  • 19
    • 0032480229 scopus 로고    scopus 로고
    • RNA polymerase II is an essential mRNA polyadenylation factor
    • Hirose Y. and Manley J.L. 1998. RNA polymerase II is an essential mRNA polyadenylation factor. Nature 395: 93.
    • (1998) Nature , vol.395 , pp. 93
    • Hirose, Y.1    Manley, J.L.2
  • 20
    • 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 C.K., Sriskanda V., McCracken S., Bentley D., Schwer B., and Shuman S. 1998. The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 273: 9577.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9577
    • Ho, C.K.1    Sriskanda, V.2    McCracken, S.3    Bentley, D.4    Schwer, B.5    Shuman, S.6
  • 21
    • 0023654017 scopus 로고
    • Messenger RNA guanylyltransferase from Saccharomyces cere-visiae. Large scale purification, subunit functions, and subcellular localization
    • Itoh N., Yamada H., Kaziro Y., and Mizumoto K. 1987. Messenger RNA guanylyltransferase from Saccharomyces cere-visiae. Large scale purification, subunit functions, and subcellular localization. J. Biol. Chem. 262: 1989.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1989
    • Itoh, N.1    Yamada, H.2    Kaziro, Y.3    Mizumoto, K.4
  • 23
    • 0023513563 scopus 로고
    • Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product
    • Kao S.Y., Calman A.F., Luciw P.A., and Peterlin B.M. 1987. Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product. Nature 330: 489.
    • (1987) Nature , vol.330 , pp. 489
    • Kao, S.Y.1    Calman, A.F.2    Luciw, P.A.3    Peterlin, B.M.4
  • 24
    • 0028924386 scopus 로고
    • Promoter-proximal pausing of RNA polymerase II defines a general rate-limiting step after transcription initiation
    • Krumm A., Hickey L., and Groudine M. 1995. Promoter-proximal pausing of RNA polymerase II defines a general rate-limiting step after transcription initiation. Genes Dev. 9: 559.
    • (1995) Genes Dev. , vol.9 , pp. 559
    • Krumm, A.1    Hickey, L.2    Groudine, M.3
  • 25
    • 0027674020 scopus 로고
    • Common mechanisms for the control of eukaryotic transcriptional elongation
    • Krumm A., Meulia T., and Groudine M. 1993. Common mechanisms for the control of eukaryotic transcriptional elongation. BioEssays 15: 659.
    • (1993) BioEssays , vol.15 , pp. 659
    • Krumm, A.1    Meulia, T.2    Groudine, M.3
  • 26
    • 0023478621 scopus 로고
    • A poly(A) addition site and a downstream termination region are required for efficient cessation of transcription by RNA polymerase II in the mouse beta maj-globin gene
    • Logan J., Falck-Pedersen E., Darnell J.E., Jr., and Shenk T. 1987. A poly(A) addition site and a downstream termination region are required for efficient cessation of transcription by RNA polymerase II in the mouse beta maj-globin gene. Proc. Natl. Acad. Sci. 84: 8306.
    • (1987) Proc. Natl. Acad. Sci. , vol.84 , pp. 8306
    • Logan, J.1    Falck-Pedersen, E.2    Darnell Jr., J.E.3    Shenk, T.4
  • 28
    • 0029001790 scopus 로고
    • Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene
    • Mao X., Schwer B., and Shuman S. 1995. Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene. Mol. Cell. Biol. 15: 4167.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4167
    • Mao, X.1    Schwer, B.2    Shuman, S.3
  • 29
    • 0026064723 scopus 로고
    • HIV-1 Tat protein promotes formation of more-processive elongation complexes
    • Marciniak R.A. and Sharp P.A. 1991. HIV-1 Tat protein promotes formation of more-processive elongation complexes. EMBO J. 10:4189.
    • (1991) EMBO J. , vol.10 , pp. 4189
    • Marciniak, R.A.1    Sharp, P.A.2
  • 30
    • 0026725368 scopus 로고
    • Control of formation of two distinct classes of RNA polymerase II elongation complexes
    • Marshall N.F. and Price D.H. 1992. Control of formation of two distinct classes of RNA polymerase II elongation complexes. Mol. Cell. Biol. 12: 2078.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2078
    • Marshall, N.F.1    Price, D.H.2
  • 31
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall N.F., Peng J.M., Xie Z., and Price D.H. 1996. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271: 27176.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176
    • Marshall, N.F.1    Peng, J.M.2    Xie, Z.3    Price, D.H.4
  • 34
    • 0032529164 scopus 로고    scopus 로고
    • Activated transcription independent of the RNA polymerase II holoenzyme in budding yeast
    • McNeil J.B., Agah H., and Bentley D. 1998. Activated transcription independent of the RNA polymerase II holoenzyme in budding yeast. Genes Dev. 12: 2510.
    • (1998) Genes Dev. , vol.12 , pp. 2510
    • McNeil, J.B.1    Agah, H.2    Bentley, D.3
  • 35
    • 0025935848 scopus 로고
    • Mutation of the AAUAAA polyadenylation signal depresses in vitro splicing of proximal but not distal introns
    • Niwa M. and Berget S.M. 1991. Mutation of the AAUAAA polyadenylation signal depresses in vitro splicing of proximal but not distal introns. Genes Dev. 5: 2086.
    • (1991) Genes Dev. , vol.5 , pp. 2086
    • Niwa, M.1    Berget, S.M.2
  • 36
    • 0024988383 scopus 로고
    • In vitro polyadenylation is stimulated by the presence of an upstream intron
    • Niwa M., Rose S.D., and Berget S.M. 1990. In vitro polyadenylation is stimulated by the presence of an upstream intron. Genes Dev. 4: 1552.
    • (1990) Genes Dev. , vol.4 , pp. 1552
    • Niwa, M.1    Rose, S.D.2    Berget, S.M.3
  • 37
    • 0023651270 scopus 로고
    • Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II
    • Nonet M., Sweetser D., and Young R.A. 1987. Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II. Cell 50: 909.
    • (1987) Cell , vol.50 , pp. 909
    • Nonet, M.1    Sweetser, D.2    Young, R.A.3
  • 38
    • 0028305843 scopus 로고
    • Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation
    • O'Brien T., Hardin S., Greenleaf A., and Lis J.T. 1994. Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation. Nature 370: 75.
    • (1994) Nature , vol.370 , pp. 75
    • O'Brien, T.1    Hardin, S.2    Greenleaf, A.3    Lis, J.T.4
  • 39
    • 0029969105 scopus 로고    scopus 로고
    • Trans-activation by human immunodeficiency virus tat protein requires the C-terminal domain of RNA polymerase II
    • Okamoto H., Sheline C.T., Corden J.L., Jones K.A., and Peterlin B.M. 1996. Trans-activation by human immunodeficiency virus tat protein requires the C-terminal domain of RNA polymerase II. Proc. Natl. Acad. Sci. 93: 11575.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 11575
    • Okamoto, H.1    Sheline, C.T.2    Corden, J.L.3    Jones, K.A.4    Peterlin, B.M.5
  • 40
    • 0030776835 scopus 로고    scopus 로고
    • Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators
    • Pan G., Aso T., and Greenblatt J. 1997. Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators. J. Biol. Chem. 272: 24563.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24563
    • Pan, G.1    Aso, T.2    Greenblatt, J.3
  • 41
    • 0029956642 scopus 로고    scopus 로고
    • Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain
    • Parada C.A. and Roeder R.G. 1996. Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. Nature 384: 375.
    • (1996) Nature , vol.384 , pp. 375
    • Parada, C.A.1    Roeder, R.G.2
  • 43
    • 0027166316 scopus 로고
    • In-vivo transcriptional pausing and cap formation on 3 Drosophila heat-shock genes
    • Rasmussen E.B. and Lis J.T. 1993. In-vivo transcriptional pausing and cap formation on 3 Drosophila heat-shock genes. Proc. Natl. Acad. Sci. 90: 7923.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 7923
    • Rasmussen, E.B.1    Lis, J.T.2
  • 45
    • 0027428934 scopus 로고
    • A phage T7 class-III promoter functions as a polymerase II promoter in mammalian cells
    • Sandig V., Lieber A., Bahring S., and Strauss M. 1993. A phage T7 class-III promoter functions as a polymerase II promoter in mammalian cells. Gene 131: 255.
    • (1993) Gene , vol.131 , pp. 255
    • Sandig, V.1    Lieber, A.2    Bahring, S.3    Strauss, M.4
  • 46
    • 0025027915 scopus 로고
    • RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals
    • Scafe C., Chao D., Lopes J., Hirsch J.P., Henry S., and Young R.A. 1990. RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals. Nature 347:491.
    • (1990) Nature , vol.347 , pp. 491
    • Scafe, C.1    Chao, D.2    Lopes, J.3    Hirsch, J.P.4    Henry, S.5    Young, R.A.6
  • 47
    • 0028211258 scopus 로고
    • Mutational analysis of yeast mRNA capping enzyme
    • Schwer B. and Shuman S. 1994. Mutational analysis of yeast mRNA capping enzyme. Proc. Natl. Acad. Sci. 91: 4328.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 4328
    • Schwer, B.1    Shuman, S.2
  • 48
    • 0029902842 scopus 로고    scopus 로고
    • Conditional inactivation of mRNA capping enzyme affects yeast pre-mRNA splicing in vivo
    • _. 1996. Conditional inactivation of mRNA capping enzyme affects yeast pre-mRNA splicing in vivo. RNA 2: 574.
    • (1996) RNA , vol.2 , pp. 574
  • 49
    • 0029107231 scopus 로고
    • Capping enzyme in eukaryotic mRNA synthesis
    • Shuman S. 1995. Capping enzyme in eukaryotic mRNA synthesis. Prog. Nucleic Acid Res. Mol. Biol. 50: 101.
    • (1995) Prog. Nucleic Acid Res. Mol. Biol. , vol.50 , pp. 101
    • Shuman, S.1
  • 50
    • 0029928677 scopus 로고    scopus 로고
    • Interallelic complementation at the suppressor of forked locus of Drosophila reveals complementation between suppressor of forked proteins mutated in different regions
    • Simonelig M., Elliott K., Mitchelson A., and O'Hare K. 1996. Interallelic complementation at the suppressor of forked locus of Drosophila reveals complementation between suppressor of forked proteins mutated in different regions. Genetics 142: 1225.
    • (1996) Genetics , vol.142 , pp. 1225
    • Simonelig, M.1    Elliott, K.2    Mitchelson, A.3    O'Hare, K.4
  • 52
    • 0027169855 scopus 로고
    • Transcriptional activation by the acidic domain of Vmw65 requires the integrity of the domain and involves additional determinants distinct from those necessary for TFIIB binding
    • Walker S., Greaves R., and O'Hare P. 1993. Transcriptional activation by the acidic domain of Vmw65 requires the integrity of the domain and involves additional determinants distinct from those necessary for TFIIB binding. Mol. Cell. Biol.; 13: 5233.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5233
    • Walker, S.1    Greaves, R.2    O'Hare, P.3
  • 53
    • 0000643270 scopus 로고    scopus 로고
    • Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae
    • Wang S.P. and Shuman S. 1997. Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae. J.Biol. Chem. 272: 14683.
    • (1997) J.Biol. Chem. , vol.272 , pp. 14683
    • Wang, S.P.1    Shuman, S.2
  • 54
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei P., Garber M.E., Fang S.M., Fischer W.H., and Jones K.A. 1998. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92: 451.
    • (1998) Cell , vol.92 , pp. 451
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3    Fischer, W.H.4    Jones, K.A.5
  • 55
    • 0022819015 scopus 로고
    • Alpha-thalassaemia caused by a poly(A) site mutation reveals that transcriptional termination is linked to 3′ end processing in the human alpha 2 globin gene
    • Whitelaw E. and Proudfoot N. 1986. Alpha-thalassaemia caused by a poly(A) site mutation reveals that transcriptional termination is linked to 3′ end processing in the human alpha 2 globin gene. EMBO J. 5: 2915.
    • (1986) EMBO J. , vol.5 , pp. 2915
    • Whitelaw, E.1    Proudfoot, N.2
  • 57
    • 0029943536 scopus 로고    scopus 로고
    • The human immunodeficiency virus tat proteins specifically associate with tak in vivo and require the carboxy-terminal domain of RNA polymerase II for function
    • Yang X.Z., Herrmann C.H., and Rice A.P. 1996. The human immunodeficiency virus tat proteins specifically associate with tak in vivo and require the carboxy-terminal domain of RNA polymerase II for function. J. Virol. 70: 4576.
    • (1996) J. Virol. , vol.70 , pp. 4576
    • Yang, X.Z.1    Herrmann, C.H.2    Rice, A.P.3
  • 58
    • 0028236808 scopus 로고
    • Transcriptional elongation by RNA polymerase II is stimulated by transactivators
    • Yankulov K., Blau J., Purton T., Roberts S., and Bentley D. 1994. Transcriptional elongation by RNA polymerase II is stimulated by transactivators. Cell 77: 749.
    • (1994) Cell , vol.77 , pp. 749
    • Yankulov, K.1    Blau, J.2    Purton, T.3    Roberts, S.4    Bentley, D.5
  • 59
    • 0029942906 scopus 로고    scopus 로고
    • TFIIH functions in regulating transcriptional elongation by RNA-polymerase II in Xenopus oocytes
    • Yankulov K.Y., Pandes M., McCracken S., Bouchard D., and Bentley D.L. 1996. TFIIH functions in regulating transcriptional elongation by RNA-polymerase II in Xenopus oocytes. Mol. Cell. Biol. 16:3291.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3291
    • Yankulov, K.Y.1    Pandes, M.2    McCracken, S.3    Bouchard, D.4    Bentley, D.L.5


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