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Volumn 18, Issue 9, 1998, Pages 5355-5363

A human RNA polymerase II complex containing factors that modify chromatin structure

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EID: 0031841947     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.9.5355     Document Type: Article
Times cited : (251)

References (82)
  • 2
    • 0023807922 scopus 로고
    • The C-terminal domain of the largest subunit of RNA polymerase II of Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: A conserved structure with an essential function
    • Allison, L., J. Wong, V. Fitzpatrick, M. Moyle, and J. Ingles. 1988. The C-terminal domain of the largest subunit of RNA polymerase II of Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved structure with an essential function. Mol. Cell. Biol. 8:321-329.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 321-329
    • Allison, L.1    Wong, J.2    Fitzpatrick, V.3    Moyle, M.4    Ingles, J.5
  • 3
    • 0030480969 scopus 로고    scopus 로고
    • The CBP-co-activator is a histone acetyltransferase
    • Bannister, A., and T. Kouzarides. 1996. The CBP-co-activator is a histone acetyltransferase. Nature (London) 384:641-643.
    • (1996) Nature (London) , vol.384 , pp. 641-643
    • Bannister, A.1    Kouzarides, T.2
  • 4
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J., J. Zhou, T. Ranalli, R. Kobayashi, D. Edmond son, S. Roth, and D. Allis. 1996. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84:843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmond Son, D.5    Roth, S.6    Allis, D.7
  • 6
    • 0030030611 scopus 로고    scopus 로고
    • Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5
    • Candau, R., P. Moore, L. Wang, N. Barlev, C. Ying, C. Rosen, and S. Berger. 1996. Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. Mol. Cell. Biol. 16:593-602.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 593-602
    • Candau, R.1    Moore, P.2    Wang, L.3    Barlev, N.4    Ying, C.5    Rosen, C.6    Berger, S.7
  • 7
    • 0031451166 scopus 로고    scopus 로고
    • Genetics of transcriptional regulation in yeast: Connections to the RNA polymerase II CTD
    • Carlson, M. 1997. Genetics of transcriptional regulation in yeast: connections to the RNA polymerase II CTD. Annu. Rev. Cell Dev. Biol. 13:1-23.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 1-23
    • Carlson, M.1
  • 8
    • 0031574071 scopus 로고    scopus 로고
    • A multiplicity of mediators: Alternative forms of transcription complexes communicate with transcriptional regulators
    • Chang, M., and J. Jaehning. 1997. A multiplicity of mediators: alternative forms of transcription complexes communicate with transcriptional regulators. Nucleic Acids Res. 25:4861-4865.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4861-4865
    • Chang, M.1    Jaehning, J.2
  • 10
    • 0026672986 scopus 로고
    • The interaction of RNA polymerase II with the adenovirus-2 major late promoter is precluded by phosphorylation of the C-terminal domain of subunit IIa
    • Chestnut, J., J. Stephens, and M. Dahmus. 1992. The interaction of RNA polymerase II with the adenovirus-2 major late promoter is precluded by phosphorylation of the C-terminal domain of subunit IIa. J. Biol. Chem. 267:10500-10506.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10500-10506
    • Chestnut, J.1    Stephens, J.2    Dahmus, M.3
  • 11
    • 0030936115 scopus 로고    scopus 로고
    • Affinity purification of a human RNA polymerase II complex using monoclonal antibodies against transcription factor IIF
    • Cho, H., E. Maldonado, and D. Reinberg. 1997. Affinity purification of a human RNA polymerase II complex using monoclonal antibodies against transcription factor IIF. J. Biol. Chem. 272:11495-11502.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11495-11502
    • Cho, H.1    Maldonado, E.2    Reinberg, D.3
  • 12
    • 0030901305 scopus 로고    scopus 로고
    • The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme
    • Cujec, T. P., H. Cho, E. Maldonado, J. Meyer, D. Reinberg, and B. M. Peterlin. 1997. The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. Mol. Cell. Biol. 17:1817-1823.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1817-1823
    • Cujec, T.P.1    Cho, H.2    Maldonado, E.3    Meyer, J.4    Reinberg, D.5    Peterlin, B.M.6
  • 13
    • 0031891003 scopus 로고    scopus 로고
    • NF-Y is associated with the histone acetyltransferases GCN5 and P/CAF
    • Currie, R. 1998. NF-Y is associated with the histone acetyltransferases GCN5 and P/CAF. J. Biol. Chem. 273:1430-1434.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1430-1434
    • Currie, R.1
  • 14
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus, M. 1996. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem. 271: 19009-19012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19009-19012
    • Dahmus, M.1
  • 15
    • 0025891809 scopus 로고
    • A mediator required for activation of RNA polymerase II transcription in vitro
    • Flanagan, P., R. kelleher, M. Sayre, H. Tshochner, and R. Kornberg. 1991. A mediator required for activation of RNA polymerase II transcription in vitro. Nature (London) 350:436-438.
    • (1991) Nature (London) , vol.350 , pp. 436-438
    • Flanagan, P.1    Kelleher, R.2    Sayre, M.3    Tshochner, H.4    Kornberg, R.5
  • 16
    • 0030935280 scopus 로고    scopus 로고
    • RNA polymerase II holoenzyme recruitment is sufficient to remodel chromatin at the yeast PHO5 promoter
    • Gaudreau, L., A. Schmid, D. Blaschke, M. Ptashne, and W. Horz. 1997. RNA polymerase II holoenzyme recruitment is sufficient to remodel chromatin at the yeast PHO5 promoter. Cell 89:55-62.
    • (1997) Cell , vol.89 , pp. 55-62
    • Gaudreau, L.1    Schmid, A.2    Blaschke, D.3    Ptashne, M.4    Horz, W.5
  • 18
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. 1997. Histone acetylation in chromatin structure and transcription. Nature (London) 389:349-352.
    • (1997) Nature (London) , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 20
    • 0031840672 scopus 로고    scopus 로고
    • Molecular genetics of the RNA polymerase II general transcriptional machinery
    • Hampsey, M. 1998. Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol. Mol. Biol. Rev. 62:465-503.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 465-503
    • Hampsey, M.1
  • 21
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • Hassig, C., T. Fleischer, A. Billin, S. Schreiber, and D. Ayer. 1997. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89:341-347.
    • (1997) Cell , vol.89 , pp. 341-347
    • Hassig, C.1    Fleischer, T.2    Billin, A.3    Schreiber, S.4    Ayer, D.5
  • 22
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes, T., A. Clayton, A. Thorne, and C. Crane-Robinson. 1994. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7:1395-1402.
    • (1994) EMBO J. , vol.7 , pp. 1395-1402
    • Hebbes, T.1    Clayton, A.2    Thorne, A.3    Crane-Robinson, C.4
  • 24
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
    • Ito, T., M. Bulger, M. Pazin, R. Kobayashi, and J. Kadonaga. 1997. ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell 90:145-155.
    • (1997) Cell , vol.90 , pp. 145-155
    • Ito, T.1    Bulger, M.2    Pazin, M.3    Kobayashi, R.4    Kadonaga, J.5
  • 26
    • 0343924289 scopus 로고    scopus 로고
    • Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor Rpd3 histone deacetylase to target promoters
    • Kadosh, D., and K. Struhl. 1997. Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor Rpd3 histone deacetylase to target promoters. Cell 89:365-371.
    • (1997) Cell , vol.89 , pp. 365-371
    • Kadosh, D.1    Struhl, K.2
  • 27
    • 0025286261 scopus 로고
    • A novel mediator between activator proteins and the RNA polymerase II transcription apparatus
    • Kelleher, R., P. Flanagan, and R. Kornberg. 1990. A novel mediator between activator proteins and the RNA polymerase II transcription apparatus. Cell 61:1209-1215.
    • (1990) Cell , vol.61 , pp. 1209-1215
    • Kelleher, R.1    Flanagan, P.2    Kornberg, R.3
  • 28
    • 0026540659 scopus 로고
    • Yeast and human TFIIDs are interchangeable for the response to acidic transcriptional activators in vitro
    • Kelleher, R., P. Flanagan, D. Chasman, A. Ponticelli, K. Struhl, and R. Kornberg. 1992. Yeast and human TFIIDs are interchangeable for the response to acidic transcriptional activators in vitro. Genes Dev. 6:296-304.
    • (1992) Genes Dev. , vol.6 , pp. 296-304
    • Kelleher, R.1    Flanagan, P.2    Chasman, D.3    Ponticelli, A.4    Struhl, K.5    Kornberg, R.6
  • 29
    • 0028282551 scopus 로고
    • A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II
    • Kim, Y., S. Bjorklund, Y. Li, M. Sayre, and R. Kornberg. 1994. A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II. Cell 77:599-608.
    • (1994) Cell , vol.77 , pp. 599-608
    • Kim, Y.1    Bjorklund, S.2    Li, Y.3    Sayre, M.4    Kornberg, R.5
  • 30
    • 0029917840 scopus 로고    scopus 로고
    • Repression and activation by multiprotein complexes that alter chromatin structure
    • Kingston, R., C. Bunker, and A. Imbalzano. 1996. Repression and activation by multiprotein complexes that alter chromatin structure. Genes Dev. 10:905-920.
    • (1996) Genes Dev. , vol.10 , pp. 905-920
    • Kingston, R.1    Bunker, C.2    Imbalzano, A.3
  • 31
    • 0028347674 scopus 로고
    • An RNA polymerase II holoenzyme responsive to activators
    • Koleske, A., and R. Young. 1994, An RNA polymerase II holoenzyme responsive to activators. Nature (London) 368:466-469.
    • (1994) Nature (London) , vol.368 , pp. 466-469
    • Koleske, A.1    Young, R.2
  • 32
    • 0017331464 scopus 로고
    • Structure of chromatin
    • Kornberg, R. 1977. Structure of chromatin. Annu. Rev. Biochem. 46:931-954.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 931-954
    • Kornberg, R.1
  • 33
    • 0029038690 scopus 로고
    • Cyclin-dependent protein kinase and cyclin homologs SSN3 and SSN8 contribute to transcriptional control in yeast
    • Kuchin, S., P. Yeghiayan, and M. Carlson. 1995. Cyclin-dependent protein kinase and cyclin homologs SSN3 and SSN8 contribute to transcriptional control in yeast. Proc. Natl. Acad. Sci. USA 92:4006-4010.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4006-4010
    • Kuchin, S.1    Yeghiayan, P.2    Carlson, M.3
  • 34
    • 0028093378 scopus 로고
    • Nucleosome disruption and enhancement of activator binding by a human SWI/SNF complex
    • Kwon, H., A. Imbalzano, P. Khavari, R. Kingston, and M. Green. 1994. Nucleosome disruption and enhancement of activator binding by a human SWI/SNF complex. Nature (London) 370:477-481.
    • (1994) Nature (London) , vol.370 , pp. 477-481
    • Kwon, H.1    Imbalzano, A.2    Khavari, P.3    Kingston, R.4    Green, M.5
  • 35
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • Lai, J.-S., and W. Herr. 1992. Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc. Natl. Acad. Sci. USA 89:6958-6962.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6958-6962
    • Lai, J.-S.1    Herr, W.2
  • 36
    • 0001448546 scopus 로고    scopus 로고
    • A transcriptional mediator protein that is required for activation of many RNA polymerase II promoters and is conserved from yeast to humans
    • Lee, Y. C., S. Min, B. S. Gim, and Y.-J. Kim. 1997. A transcriptional mediator protein that is required for activation of many RNA polymerase II promoters and is conserved from yeast to humans. Mol. Cell. Biol. 17:4622-4632.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4622-4632
    • Lee, Y.C.1    Min, S.2    Gim, B.S.3    Kim, Y.-J.4
  • 37
    • 0028826925 scopus 로고
    • Yeast global transcriptional regulators Sin4 and Rgr1 are components of mediator complex/RNA polymerase II holoenzyme
    • Li, Y., S. Bjorklund, Y. Jiang, Y.-J. Kim, W. Lane. D. Stillman, and R. Kornberg. 1995. Yeast global transcriptional regulators Sin4 and Rgr1 are components of mediator complex/RNA polymerase II holoenzyme. Proc. Natl. Acad. Sci. USA 92:10864-10868.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10864-10868
    • Li, Y.1    Bjorklund, S.2    Jiang, Y.3    Kim, Y.-J.4    Lane, W.5    Stillman, D.6    Kornberg, R.7
  • 39
    • 0025790439 scopus 로고
    • The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex
    • Lu, H., O. Flores, R. Weinman, and D. Reinberg. 1991. The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex. Proc. Natl. Acad. Sci. USA 88:10004-10008.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10004-10008
    • Lu, H.1    Flores, O.2    Weinman, R.3    Reinberg, D.4
  • 41
    • 0029806764 scopus 로고    scopus 로고
    • Purification of human RNA polymerase II and general transcription factors
    • Maldonado, E., R. Drapkin, and D. Reinberg. 1996. Purification of human RNA polymerase II and general transcription factors. Methods Enzymol. 174:72-100.
    • (1996) Methods Enzymol. , vol.174 , pp. 72-100
    • Maldonado, E.1    Drapkin, R.2    Reinberg, D.3
  • 42
    • 0027948984 scopus 로고
    • Functional similarities and physical association between Gcn5 and Ada2putative transcriptional adaptors
    • Marcus, G., N. Silverman, S. Berger, J. Horiuchi, and L. Guarente. 1994. Functional similarities and physical association between Gcn5 and Ada2putative transcriptional adaptors. EMBO J. 13:4807-4815.
    • (1994) EMBO J. , vol.13 , pp. 4807-4815
    • Marcus, G.1    Silverman, N.2    Berger, S.3    Horiuchi, J.4    Guarente, L.5
  • 46
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression is mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • Nagy, L., H.-Y. Kao, D. Chakravarti, R. Lin, C. Hassig, D. Ayer, S. Schreiber, and R. Evans. 1997. Nuclear receptor repression is mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89:373-380.
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.-Y.2    Chakravarti, D.3    Lin, R.4    Hassig, C.5    Ayer, D.6    Schreiber, S.7    Evans, R.8
  • 47
    • 0030902507 scopus 로고    scopus 로고
    • Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcription induction via signal-dependent factors
    • Nakajima, T., C. Uchida, S. Anderson, J. Parvin, and M. Montminy. 1997. Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcription induction via signal-dependent factors. Genes Dev. 11:738-747.
    • (1997) Genes Dev. , vol.11 , pp. 738-747
    • Nakajima, T.1    Uchida, C.2    Anderson, S.3    Parvin, J.4    Montminy, M.5
  • 49
    • 0021715020 scopus 로고
    • Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae
    • Neigeborn, L., and M. Carlson. 1984. Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae. Genetics 108:845-858.
    • (1984) Genetics , vol.108 , pp. 845-858
    • Neigeborn, L.1    Carlson, M.2
  • 50
    • 0032004591 scopus 로고    scopus 로고
    • Factors associated with the mammalian RNA polymerase II holoenzyme
    • Neish, A., S. Anderson, B. S. W. Wei, and J. Parvin. 1998. Factors associated with the mammalian RNA polymerase II holoenzyme. Nucleic Acids Res. 26:847-853.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 847-853
    • Neish, A.1    Anderson, S.2    Wei, B.S.W.3    Parvin, J.4
  • 51
    • 0031466322 scopus 로고    scopus 로고
    • Transcription units as RNA processing units
    • Neugebauer, K., and M. Roth. 1997. Transcription units as RNA processing units. Genes Dev. 11:3279-3285.
    • (1997) Genes Dev. , vol.11 , pp. 3279-3285
    • Neugebauer, K.1    Roth, M.2
  • 52
    • 0024354605 scopus 로고
    • Intragenic and extragenic suppressors of mutations in the heptapeptide repeat domain of Saccharomyces cerevisiae RNA polymerase II
    • Nonet, M., and R. Young. 1989. Intragenic and extragenic suppressors of mutations in the heptapeptide repeat domain of Saccharomyces cerevisiae RNA polymerase II. Genetics 123:715-724.
    • (1989) Genetics , vol.123 , pp. 715-724
    • Nonet, M.1    Young, R.2
  • 53
    • 0028305843 scopus 로고
    • Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation
    • O'Brien, T., S. Hardin, A. Greenleaf, and J. Lis. 1994. Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation. Nature (London) 370:75-77.
    • (1994) Nature (London) , vol.370 , pp. 75-77
    • O'Brien, T.1    Hardin, S.2    Greenleaf, A.3    Lis, J.4
  • 54
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V., L. Schiltz, V. Russanova, B. Howard, and Y. Nakatani. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.1    Schiltz, L.2    Russanova, V.3    Howard, B.4    Nakatani, Y.5
  • 55
    • 0029846871 scopus 로고    scopus 로고
    • The general transcription factors of RNA polymerase II
    • Orphanides, G., T. Lagrange, and D. Reinberg. 1996. The general transcription factors of RNA polymerase II. Genes Dev. 10:2657-2683.
    • (1996) Genes Dev. , vol.10 , pp. 2657-2683
    • Orphanides, G.1    Lagrange, T.2    Reinberg, D.3
  • 56
    • 0032498273 scopus 로고    scopus 로고
    • FACT, a factor that facilitates transcript elongation through nucleosomes
    • Orphanides, G., G. LeRoy, C. Chang, D. Luse, and D. Reinberg. 1998. FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 92:105-116.
    • (1998) Cell , vol.92 , pp. 105-116
    • Orphanides, G.1    Leroy, G.2    Chang, C.3    Luse, D.4    Reinberg, D.5
  • 57
    • 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., T. Aso, and J. Greenblatt. 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. 272:24563-24571.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24563-24571
    • Pan, G.1    Aso, T.2    Greenblatt, J.3
  • 58
    • 0024408630 scopus 로고
    • The transition of RNA polymerase II from initiation to elongation is associated with phosphoryla tion of the carboxyl-terminal domain of subunit IIa
    • Payne, J., P. Laybourn, and M. Dahmus. 1989. The transition of RNA polymerase II from initiation to elongation is associated with phosphoryla tion of the carboxyl-terminal domain of subunit IIa. J. Biol. Chem. 264: 19621-19629.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19621-19629
    • Laybourn, P.1    Dahmus, M.2
  • 59
    • 0028987268 scopus 로고
    • The SWI-SNF complex: A chromatin remodeling machine?
    • Peterson, C., and J. Tamkun. 1995. The SWI-SNF complex: a chromatin remodeling machine? Trends Biochem. Sci. 20:143-146.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 143-146
    • Peterson, C.1    Tamkun, J.2
  • 60
    • 0029741343 scopus 로고    scopus 로고
    • Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases
    • Reifsnyder, C., J. Lowell, A. Clarke, and L. Pillus. 1996. Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases. Nat. Genet. 14:42-49.
    • (1996) Nat. Genet. , vol.14 , pp. 42-49
    • Reifsnyder, C.1    Lowell, J.2    Clarke, A.3    Pillus, L.4
  • 61
    • 0029948789 scopus 로고    scopus 로고
    • Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase II
    • Rickert, P., W. Seghezzi, F. Shanahan, H. Cho, and E. Lees. 1996. Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase II. Oncogene 12:2631-2640.
    • (1996) Oncogene , vol.12 , pp. 2631-2640
    • Rickert, P.1    Seghezzi, W.2    Shanahan, F.3    Cho, H.4    Lees, E.5
  • 62
    • 0000647604 scopus 로고
    • Factors involved in specific transcription by human RNA polymerase II: Analysis by a rapid and quantitative in vitro assay
    • Sawadogo, M., and R. Roeder. 1985. Factors involved in specific transcription by human RNA polymerase II: analysis by a rapid and quantitative in vitro assay. Proc. Natl. Acad. Sci. USA 82:4394-4398.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4394-4398
    • Sawadogo, M.1    Roeder, R.2
  • 64
    • 0031027465 scopus 로고    scopus 로고
    • Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex from the Srbp-containing holoenzyme
    • Shi, X., M. Chang, A. Wolf, C. Chang, A. Frazer-Abel, P. Wade, Z. Burton, and J. Jaehning. 1997. Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex from the Srbp-containing holoenzyme. Mol. Cell. Biol. 17:1160-1169.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1160-1169
    • Shi, X.1    Chang, M.2    Wolf, A.3    Chang, C.4    Frazer-Abel, A.5    Wade, P.6    Burton, Z.7    Jaehning, J.8
  • 65
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama, N., J. Lyon, and N. LaThangue. 1997. The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol. 7:232-236.
    • (1997) Trends Cell Biol. , vol.7 , pp. 232-236
    • Shikama, N.1    Lyon, J.2    Lathangue, N.3
  • 66
    • 0030680252 scopus 로고    scopus 로고
    • Origins of mRNA identity: Capping enzymes bind to the phosphorylated C-terminal domain of the RNA polymerase II
    • Shuman, S. 1997. Origins of mRNA identity: capping enzymes bind to the phosphorylated C-terminal domain of the RNA polymerase II. Proc. Natl. Acad. Sci. USA 94:12758-12760.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12758-12760
    • Shuman, S.1
  • 67
    • 0029655780 scopus 로고    scopus 로고
    • SSN genes that affect transcriptional repression in Saccharomyces cerevisiae encode SIN4, ROX3, and SRB proteins associated with RNA polymerase II
    • Song, W., I. Treich, N. Qian, S. Kuchin, and M. Carlson. 1996. SSN genes that affect transcriptional repression in Saccharomyces cerevisiae encode SIN4, ROX3, and SRB proteins associated with RNA polymerase II. Mol. Cell. Biol. 16:115-120.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 115-120
    • Song, W.1    Treich, I.2    Qian, N.3    Kuchin, S.4    Carlson, M.5
  • 69
    • 85038537232 scopus 로고    scopus 로고
    • NAT, a human complex Srb polypeptides that functions as a negative regulator of activated transcription
    • in press
    • Sun, X., Y. Zhang, H. Cho, P. Rickert, E. Lees, W. Lane, and D. Reinberg. NAT, a human complex Srb polypeptides that functions as a negative regulator of activated transcription. Mol. Cell, in press.
    • Mol. Cell
    • Sun, X.1    Zhang, Y.2    Cho, H.3    Rickert, P.4    Lees, E.5    Lane, W.6    Reinberg, D.7
  • 70
    • 1842287996 scopus 로고    scopus 로고
    • CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription
    • Sune, C., T. Hayashi, Y. Liu, W. Lane, R. Young, and M. Garcia-Blanco. 1997. CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription. Mol. Cell. Biol. 17:6029-6039.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6029-6039
    • Sune, C.1    Hayashi, T.2    Liu, Y.3    Lane, W.4    Young, R.5    Garcia-Blanco, M.6
  • 71
    • 0029562736 scopus 로고
    • Purification and properties of an ATP-dependent nucleosome remodeling factor
    • Tsukiyama, T., and C. Wu. 1995. Purification and properties of an ATP-dependent nucleosome remodeling factor. Cell 83:1011-1020.
    • (1995) Cell , vol.83 , pp. 1011-1020
    • Tsukiyama, T.1    Wu, C.2
  • 72
    • 0031009397 scopus 로고    scopus 로고
    • Chromatin remodelling and transcription
    • Tsukiyama, T., and C. Wu. 1997. Chromatin remodelling and transcription. Curr. Opin. Genet. Dev. 7:182-191.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 182-191
    • Tsukiyama, T.1    Wu, C.2
  • 73
    • 0030826732 scopus 로고    scopus 로고
    • The Cockayne syndrome B protein, involved in transcription-coupled DNA repair, resides in an RNA polymerase II-containing complex
    • van Gool, A., E. Citterio, S. Rademakers, R. Os, W. Vermeulen, A. Constantinou, J.-M. Egly, D. Bootsma, and H. Hoejmakers. 1997. The Cockayne syndrome B protein, involved in transcription-coupled DNA repair, resides in an RNA polymerase II-containing complex. EMBO J. 16:5955-5965.
    • (1997) EMBO J. , vol.16 , pp. 5955-5965
    • Gool, A.1    Citterio, E.2    Rademakers, S.3    Os, R.4    Vermeulen, W.5    Constantinou, A.6    Egly, J.-M.7    Bootsma, D.8    Hoejmakers, H.9
  • 74
    • 0030839857 scopus 로고    scopus 로고
    • Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
    • Varga-Weisz, P., M. Wilm, E. Bonte, K. Dumas, M. Mann, and P. Becker. 1997. Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II. Nature (London) 388:598-602.
    • (1997) Nature (London) , vol.388 , pp. 598-602
    • Varga-Weisz, P.1    Wilm, M.2    Bonte, E.3    Dumas, K.4    Mann, M.5    Becker, P.6
  • 75
    • 0030940298 scopus 로고    scopus 로고
    • Histone acetylation: Chromatin in action
    • Wade, P., D. Pruss, and A. Wolffe. 1997. Histone acetylation: chromatin in action. Trends Biochem. Sci. 22:128-132.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 128-132
    • Wade, P.1    Pruss, D.2    Wolffe, A.3
  • 77
    • 0030033699 scopus 로고    scopus 로고
    • RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodelling
    • Wilson, C., D. Chao, A. Imbalzano, G. Schnitzler, R. Kingston, and R. Young. 1996. RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodelling. Cell 84:235-244.
    • (1996) Cell , vol.84 , pp. 235-244
    • Wilson, C.1    Chao, D.2    Imbalzano, A.3    Schnitzler, G.4    Kingston, R.5    Young, R.6
  • 78
    • 0023692115 scopus 로고
    • Transcriptional regulation by the immediate early promoter of pseudorabies virus during in vitro nucleosome assembly
    • Workman, J., S. Abmayr, W. Cromlish, and R. Roeder. 1988. Transcriptional regulation by the immediate early promoter of pseudorabies virus during in vitro nucleosome assembly. Cell 55:211-219.
    • (1988) Cell , vol.55 , pp. 211-219
    • Workman, J.1    Abmayr, S.2    Cromlish, W.3    Roeder, R.4
  • 79
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X.-J., V. Ogryzko, J. Nishikawa, B. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature (London) 382:319-324.
    • (1996) Nature (London) , vol.382 , pp. 319-324
    • Yang, X.-J.1    Ogryzko, V.2    Nishikawa, J.3    Howard, B.4    Nakatani, Y.5
  • 80
    • 0025739871 scopus 로고
    • RNA polymerase II
    • Young, R. 1991. RNA polymerase II. Annu. Rev. Biochem. 60:689-715.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 689-715
    • Young, R.1
  • 81
    • 0024022636 scopus 로고
    • The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription in vitro
    • Zehring, W., J. Lee, J. Weeks, R. Jokerst, and A. Greenleaf. 1988. The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription in vitro. Proc. Natl. Acad. Sci. USA 85:3698-3702.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3698-3702
    • Zehring, W.1    Lee, J.2    Weeks, J.3    Jokerst, R.4    Greenleaf, A.5
  • 82
    • 0030916729 scopus 로고    scopus 로고
    • Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
    • Zhang, Y., R. Iratni, H. Erdjument-Bromage, P. Tempst, and D. Reinberg. 1997. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89:357-364.
    • (1997) Cell , vol.89 , pp. 357-364
    • Zhang, Y.1    Iratni, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5


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