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Volumn 11, Issue 5, 2004, Pages 394-403

Structure and mechanism of the RNA polymerase II transcription machinery

Author keywords

[No Author keywords available]

Indexed keywords

RNA POLYMERASE II;

EID: 2542428546     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb763     Document Type: Review
Times cited : (393)

References (127)
  • 1
    • 0031840672 scopus 로고    scopus 로고
    • Molecular genetics of the RNA polymerase II general transcriptional machinery
    • Hampsey, M. Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol. Mol. Biol. Rev. 62, 465-503 (1998).
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 465-503
    • Hampsey, M.1
  • 2
    • 0034507632 scopus 로고    scopus 로고
    • Transcription of eukaryotic protein-coding genes
    • Lee, T.I. & Young, R.A. Transcription of eukaryotic protein-coding genes. Annu. Rev. Genet. 34, 77-137 (2000).
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 77-137
    • Lee, T.I.1    Young, R.A.2
  • 3
    • 0037154984 scopus 로고    scopus 로고
    • The RNA polymerase II machinery: Structure illuminates function
    • Woychik, N.A. & Hampsey, M. The RNA polymerase II machinery: structure illuminates function. Cell 108, 453-463 (2002).
    • (2002) Cell , vol.108 , pp. 453-463
    • Woychik, N.A.1    Hampsey, M.2
  • 4
    • 0038013991 scopus 로고    scopus 로고
    • RNA polymerase holoenzyme: Structure, function and biological implications
    • Borukhov, S. & Nudler, E. RNA polymerase holoenzyme: structure, function and biological implications. Curr. Opin. Microbiol. 6, 93-100 (2003).
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 93-100
    • Borukhov, S.1    Nudler, E.2
  • 6
    • 0141992120 scopus 로고    scopus 로고
    • Binding of TFIIB to RNA polymerase II: Mapping the binding site for the TFIIB zinc ribbon domain within the preinitiation complex
    • Chen, H.T. & Hahn, S. Binding of TFIIB to RNA polymerase II: mapping the binding site for the TFIIB zinc ribbon domain within the preinitiation complex. Mol. Cell 12, 437-447 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 437-447
    • Chen, H.T.1    Hahn, S.2
  • 7
    • 0242266617 scopus 로고    scopus 로고
    • RNA Polymerase II/TFIIF Structure and Conserved Organization of the Initiation Complex
    • Chung, W.H. et al. RNA Polymerase II/TFIIF Structure and Conserved Organization of the Initiation Complex. Mol. Cell 12, 1003-1013 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1003-1013
    • Chung, W.H.1
  • 8
    • 1142274214 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II-TFIIB cocrystal at 4.5 A
    • Bushnell, D.A., Westover, K.D., Davis, R.E. & Kornberg, R.D. Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 A. Science 303, 983-988 (2004).
    • (2004) Science , vol.303 , pp. 983-988
    • Bushnell, D.A.1    Westover, K.D.2    Davis, R.E.3    Kornberg, R.D.4
  • 10
    • 0034671288 scopus 로고    scopus 로고
    • RNA polymerase: Structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II
    • Ebright, R.H. RNA polymerase: structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II. J. Mol. Biol. 304, 687-698 (2000).
    • (2000) J. Mol. Biol. , vol.304 , pp. 687-698
    • Ebright, R.H.1
  • 11
    • 0037108150 scopus 로고    scopus 로고
    • Recruitment of RNA polymerase III to its target promoters
    • Schramm, L. & Hernandez, N. Recruitment of RNA polymerase III to its target promoters. Genes Dev. 16, 2593-2620 (2002).
    • (2002) Genes Dev , vol.16 , pp. 2593-2620
    • Schramm, L.1    Hernandez, N.2
  • 12
    • 0038506040 scopus 로고    scopus 로고
    • Life on a planet of its own: Regulation of RNA polymerase I transcription in the nucleolus
    • Grummt, I. Life on a planet of its own: regulation of RNA polymerase I transcription in the nucleolus. Genes Dev. 17, 1691-1702 (2003).
    • (2003) Genes Dev , vol.17 , pp. 1691-1702
    • Grummt, I.1
  • 13
    • 0004211673 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Ptashne, M. & Gann, A. Genes and Signals (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2002).
    • (2002) Genes and Signals
    • Ptashne, M.1    Gann, A.2
  • 14
    • 0036671407 scopus 로고    scopus 로고
    • Ordered recruitment: Gene-specific mechanism of transcription active-tion
    • Cosma, M.P. Ordered recruitment: gene-specific mechanism of transcription active-tion. Mol. Cell 10, 227-236 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 227-236
    • Cosma, M.P.1
  • 15
    • 0026577264 scopus 로고
    • Polymerase II promoter activation: Closed complex formation and ATP-driven start site opening
    • Wang, W., Carey, M. & Gralla, J.D. Polymerase II promoter activation: closed complex formation and ATP-driven start site opening. Science 255, 450-453 (1992).
    • (1992) Science , vol.255 , pp. 450-453
    • Wang, W.1    Carey, M.2    Gralla, J.D.3
  • 16
    • 0023645766 scopus 로고
    • Abortive initiation by RNA polymerase II in vitro at the adenovirus 2 major late promoter
    • Luse, D.S. & Jacob, G.A. Abortive initiation by RNA polymerase II in vitro at the adenovirus 2 major late promoter. J. Biol. Chem. 262, 14990-14997 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 14990-14997
    • Luse, D.S.1    Jacob, G.A.2
  • 17
    • 0031463993 scopus 로고    scopus 로고
    • Three transitions in the RNA polymerase II transcription complex during initiation
    • Holstege, F.C.P., Fiedler, U. & Timmers, H.T.M. Three transitions in the RNA polymerase II transcription complex during initiation. EMBO J. 16, 7468-7480 (1997).
    • (1997) EMBO J , vol.16 , pp. 7468-7480
    • Holstege, F.C.P.1    Fiedler, U.2    Timmers, H.T.M.3
  • 18
    • 0036591882 scopus 로고    scopus 로고
    • The mRNA assembly line: Transcription and processing machines in the same factory
    • Bentley, D. The mRNA assembly line: transcription and processing machines in the same factory. Curr. Opin. Cell Biol. 14, 336-342 (2002).
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 336-342
    • Bentley, D.1
  • 19
    • 0034626731 scopus 로고    scopus 로고
    • A transcription reinitiation intermediate that is stabilized by activator
    • Yudkovsky, N., Ranish, J.A. & Hahn, S. A transcription reinitiation intermediate that is stabilized by activator. Nature 408, 225-229 (2000).
    • (2000) Nature , vol.408 , pp. 225-229
    • Yudkovsky, N.1    Ranish, J.A.2    Hahn, S.3
  • 20
    • 0043269205 scopus 로고    scopus 로고
    • The RNA polymerase II core promoter
    • Smale, S.T. & Kadonaga, J.T. The RNA polymerase II core promoter. Annu. Rev. Biochem. 72, 449-479 (2003).
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 449-479
    • Smale, S.T.1    Kadonaga, J.T.2
  • 21
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA- box complex
    • Kim, Y., Geiger, J.H., Hahn, S. & Sigler, P.B. Crystal structure of a yeast TBP/TATA- box complex. Nature 365, 512-520 (1993).
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 22
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim, J.L., Nikolov, D.B. & Burley, S.K. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365, 520-527 (1993).
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 23
    • 0031456020 scopus 로고    scopus 로고
    • Bidirectional binding of the TATA box binding protein to the TATA box
    • Cox, J.M. et al. Bidirectional binding of the TATA box binding protein to the TATA box. Proc. Natl. Acad. Sci. USA 94, 13475-13480 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13475-13480
    • Cox, J.M.1
  • 24
    • 0031882652 scopus 로고    scopus 로고
    • New core promoter element in RNA polymerase II-dependent transcription: Sequence-specific DNA binding by transcription factor IIB
    • Lagrange, T., Kapanidis, A.N., Tang, H., Reinberg, D. & Ebright, R.H. New core promoter element in RNA polymerase II-dependent transcription: sequence-specific DNA binding by transcription factor IIB. Genes Dev. 12, 34-44 (1998).
    • (1998) Genes Dev , vol.12 , pp. 34-44
    • Lagrange, T.1    Kapanidis, A.N.2    Tang, H.3    Reinberg, D.4    Ebright, R.H.5
  • 25
    • 0031990302 scopus 로고    scopus 로고
    • Sequence-specific DNA binding by the S. Shibatae TFIIB homolog, TFB, and its effect on promoter strength
    • Qureshi, S.A. & Jackson, S.P. Sequence-specific DNA binding by the S. shibatae TFIIB homolog, TFB, and its effect on promoter strength. Mol. Cell 1, 389-400 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 389-400
    • Qureshi, S.A.1    Jackson, S.P.2
  • 27
    • 0033598826 scopus 로고    scopus 로고
    • The structural basis for the oriented assembly of a TBP/TFB/promoter complex
    • Littlefield, O., Korkhin, Y. & Sigler, P.B. The structural basis for the oriented assembly of a TBP/TFB/promoter complex. Proc. Natl. Acad. Sci. USA 96, 13668-13673 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13668-13673
    • Littlefield, O.1    Korkhin, Y.2    Sigler, P.B.3
  • 28
    • 0033200098 scopus 로고    scopus 로고
    • DNA binding site selection by RNA polymerase II TAFs: A TAF(II)250-TAF(II) 150 complex recognizes the initiator
    • Chalkley, G.E. & Verrijzer, C.P. DNA binding site selection by RNA polymerase II TAFs: a TAF(II)250-TAF(II) 150 complex recognizes the initiator. EMBO J. 18, 4835-4845 (1999).
    • (1999) EMBO J , vol.18 , pp. 4835-4845
    • Chalkley, G.E.1    Verrijzer, C.P.2
  • 29
    • 0029808220 scopus 로고    scopus 로고
    • Topology and reorganization of a human TFIID-promoter complex
    • Oelgeschlager, T., Chiang, C.-M. & Roeder, R.G. Topology and reorganization of a human TFIID-promoter complex. Nature 382, 735-738 (1996).
    • (1996) Nature , vol.382 , pp. 735-738
    • Oelgeschlager, T.1    Chiang, C.-M.2    Roeder, R.G.3
  • 30
    • 0030669466 scopus 로고    scopus 로고
    • The downstream core promoter element, DPE, is conserved from Drosophilato humans and is recognized by TAFII60 of Drosophila
    • Burke, T.W. & Kadonaga, J.T. The downstream core promoter element, DPE, is conserved from Drosophilato humans and is recognized by TAFII60 of Drosophila. Genes Dev. 11, 3020-3031 (1997).
    • (1997) Genes Dev , vol.11 , pp. 3020-3031
    • Burke, T.W.1    Kadonaga, J.T.2
  • 31
    • 0035477093 scopus 로고    scopus 로고
    • Enhancer-promoter specificity mediated by DPE or TATA core promoter motifs
    • Butler, J.E. & Kadonaga, J.T. Enhancer-promoter specificity mediated by DPE or TATA core promoter motifs. Genes Dev. 15, 2515-2519 (2001).
    • (2001) Genes Dev , vol.15 , pp. 2515-2519
    • Butler, J.E.1    Kadonaga, J.T.2
  • 32
    • 0012253746 scopus 로고    scopus 로고
    • Computational analysis of core promoters in the Drosophilagenome. Genome Biol
    • Ohler, U., Liao, G.C., Niemann, H. & Rubin, G.M. Computational analysis of core promoters in the Drosophilagenome. Genome Biol. 3, 0087.1-0087.12 (2002).
    • (2002) , vol.3 , pp. 87.1-87.12
    • Ohler, U.1    Liao, G.C.2    Niemann, H.3    Rubin, G.M.4
  • 33
    • 0033573008 scopus 로고    scopus 로고
    • TATA element recognition by the TATA box-binding protein has been conserved throughout evolution
    • Patikoglou, G.A. et al. TATA element recognition by the TATA box-binding protein has been conserved throughout evolution. Genes Dev. 13, 3217-3230 (1999).
    • (1999) Genes Dev , vol.13 , pp. 3217-3230
    • Patikoglou, G.A.1
  • 34
    • 0025309524 scopus 로고
    • Yeast and human TATA-binding proteins have nearly identical DNA sequence requirements for transcription in vitro
    • Wobbe, C.R. & Struhl, K. Yeast and human TATA-binding proteins have nearly identical DNA sequence requirements for transcription in vitro. Mol. Cell. Biol. 10, 3859-3867 (1990).
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3859-3867
    • Wobbe, C.R.1    Struhl, K.2
  • 35
    • 0032900980 scopus 로고    scopus 로고
    • Intermediates in formation and activity of the RNA polymerase II preinitiation complex: Holoenzyme recruitment and a postrecruit- ment role for the TATA box and TFIIB
    • Ranish, J.A., Yudkovsky, N. & Hahn, S. Intermediates in formation and activity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruit- ment role for the TATA box and TFIIB. Genes Dev. 13, 49-63 (1999).
    • (1999) Genes Dev , vol.13 , pp. 49-63
    • Ranish, J.A.1    Yudkovsky, N.2    Hahn, S.3
  • 36
    • 0029610077 scopus 로고
    • Core promoter-specific function of a mutant transcription factor TFIID defective in TATA-box binding
    • Martinez, E. et al. Core promoter-specific function of a mutant transcription factor TFIID defective in TATA-box binding. Proc. Natl. Acad. Sci. USA 92, 11864-11868 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11864-11868
    • Martinez, E.1
  • 37
    • 0037948267 scopus 로고    scopus 로고
    • Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression
    • Hochheimer, A. & Tjian, R. Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression. Genes Dev. 17, 1309-1320 (2003).
    • (2003) Genes Dev , vol.17 , pp. 1309-1320
    • Hochheimer, A.1    Tjian, R.2
  • 38
    • 0038148651 scopus 로고    scopus 로고
    • The genetics of TBP and TBP-related factors
    • Davidson, I. The genetics of TBP and TBP-related factors. Trends Biochem. Sci. 28, 391-398 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 391-398
    • Davidson, I.1
  • 39
    • 0034608084 scopus 로고    scopus 로고
    • Promoter-selective properties of the TBP-related factor TRF1
    • Holmes, M.C. & Tjian, R. Promoter-selective properties of the TBP-related factor TRF1. Science 288, 867-870 (2000).
    • (2000) Science , vol.288 , pp. 867-870
    • Holmes, M.C.1    Tjian, R.2
  • 40
    • 0034716931 scopus 로고    scopus 로고
    • A TRF1:BRF complex directs Drosophila RNA polymerase III transcription
    • Takada, S., Lis, J.T., Zhou, S. & Tjian, R. A TRF1:BRF complex directs Drosophila RNA polymerase III transcription. Cell 101, 459-469 (2000).
    • (2000) Cell , vol.101 , pp. 459-469
    • Takada, S.1    Lis, J.T.2    Zhou, S.3    Tjian, R.4
  • 41
    • 0028978670 scopus 로고
    • Crystal structure of a TFIIB-TBP-TATA-element ternary complex
    • Nikolov, D.B. et al. Crystal structure of a TFIIB-TBP-TATA-element ternary complex. Nature 377, 119-128 (1995).
    • (1995) Nature , vol.377 , pp. 119-128
    • Nikolov, D.B.1
  • 42
    • 0029930779 scopus 로고    scopus 로고
    • Crystal structure of the yeast TFIIA/TBP/DNA complex
    • Geiger, J.H., Hahn, S., Lee, S. & Sigler, P.B. Crystal structure of the yeast TFIIA/TBP/DNA complex. Science 272, 830-836 (1996).
    • (1996) Science , vol.272 , pp. 830-836
    • Geiger, J.H.1    Hahn, S.2    Lee, S.3    Sigler, P.B.4
  • 43
    • 0029870514 scopus 로고    scopus 로고
    • Crystal structure of a yeast TFIIA/TBP/DNA complex
    • Tan, S., Hunziker, Y., Sargent, D.F. & Richmond, T.J. Crystal structure of a yeast TFIIA/TBP/DNA complex. Nature 381, 127-134 (1996).
    • (1996) Nature , vol.381 , pp. 127-134
    • Tan, S.1    Hunziker, Y.2    Sargent, D.F.3    Richmond, T.J.4
  • 44
    • 0031559556 scopus 로고    scopus 로고
    • Dynamic interplay of TFIIA, TBP, and TATA DNA
    • Weideman, C.A. et al. Dynamic interplay of TFIIA, TBP, and TATA DNA. J. Mol. Biol. 271, 61-75 (1997).
    • (1997) J. Mol. Biol. , vol.271 , pp. 61-75
    • Weideman, C.A.1
  • 45
    • 0031883573 scopus 로고    scopus 로고
    • The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein
    • Kokubo, T., Swanson, M.J., Nishikawa, J.I., Hinnebusch, A.G. & Nakatani, Y. The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein. Mol. Cell. Biol. 18, 1003-1012 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1003-1012
    • Kokubo, T.1    Swanson, M.J.2    Nishikawa, J.I.3    Hinnebusch, A.G.4    Nakatani, Y.5
  • 46
    • 0032483558 scopus 로고    scopus 로고
    • Solution structure of a TBP-TAF(II)230 complex: Protein mimicry of the minor groove surface of the TATA box unwound by TBP
    • Liu, D. et al. Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. Cell 94, 573-583 (1998).
    • (1998) Cell , vol.94 , pp. 573-583
    • Liu, D.1
  • 47
    • 0036318573 scopus 로고    scopus 로고
    • Molecular characterization of Saccharomyces cerevisiaeTFIID
    • Sanders, S.L., Garbett, K.A. & Weil, P.A. Molecular characterization of Saccharomyces cerevisiaeTFIID. Mol. Cell. Biol. 22, 6000-6013 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6000-6013
    • Sanders, S.L.1    Garbett, K.A.2    Weil, P.A.3
  • 48
    • 0029045553 scopus 로고
    • A general mechanism for transcrip- tional synergy by eukaryotic activators
    • Chi, T., Lieberman, P., Ellwood, K. & Carey, M. A general mechanism for transcrip- tional synergy by eukaryotic activators. Nature 377, 254-257 (1995).
    • (1995) Nature , vol.377 , pp. 254-257
    • Chi, T.1    Lieberman, P.2    Ellwood, K.3    Carey, M.4
  • 49
    • 0032504245 scopus 로고    scopus 로고
    • The N-terminal region of yeast TFIIB contains two adjacent functional domains involved in stable RNA polymerase II binding and transcription start site selection
    • Pardee, T.S., Bangur, C.S. & Ponticelli, A.S. The N-terminal region of yeast TFIIB contains two adjacent functional domains involved in stable RNA polymerase II binding and transcription start site selection. J. Biol. Chem. 273, 17859-17864 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 17859-17864
    • Pardee, T.S.1    Bangur, C.S.2    Ponticelli, A.S.3
  • 50
    • 0034653666 scopus 로고    scopus 로고
    • The zinc ribbon domains of the general transcription factors TFIIB and Brf: Conserved functional surfaces but different roles in transcription initiation
    • Hahn, S. & Roberts, S. The zinc ribbon domains of the general transcription factors TFIIB and Brf: conserved functional surfaces but different roles in transcription initiation. Genes Dev. 14, 719-730 (2000).
    • (2000) Genes Dev , vol.14 , pp. 719-730
    • Hahn, S.1    Roberts, S.2
  • 51
    • 0033969766 scopus 로고    scopus 로고
    • TAFs revisited: More data reveal new twists and confirm old ideas
    • Albright, S.R. & Tjian, R. TAFs revisited: more data reveal new twists and confirm old ideas. Gene 242, 1-13 (2000).
    • (2000) Gene , vol.242 , pp. 1-13
    • Albright, S.R.1    Tjian, R.2
  • 52
    • 0033964073 scopus 로고    scopus 로고
    • TBP-associated factors (TAFIIs): Multiple, selective transcriptional mediators in common complexes
    • Green, M.R. TBP-associated factors (TAFIIs): multiple, selective transcriptional mediators in common complexes. Trends Biochem. Sci. 25, 59-63 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 59-63
    • Green, M.R.1
  • 53
    • 0037087628 scopus 로고    scopus 로고
    • A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription
    • Tora, L. A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription. Genes Dev. 16, 673-675 (2002).
    • (2002) Genes Dev , vol.16 , pp. 673-675
    • Tora, L.1
  • 54
    • 0028108925 scopus 로고
    • Assembly of recombinant TFIID reveals differential coactivator requirements for distinct transcriptional activators
    • Chen, J.-L., Attardi, L.D., Verrijzer, C.P., Yokomori, K. & Tjian, R. Assembly of recombinant TFIID reveals differential coactivator requirements for distinct transcriptional activators. Cell 79, 93-105 (1994).
    • (1994) Cell , vol.79 , pp. 93-105
    • Chen, J.-L.1    Attardi, L.D.2    Verrijzer, C.P.3    Yokomori, K.4    Tjian, R.5
  • 56
    • 0034839274 scopus 로고    scopus 로고
    • TAF(II)250: A transcription toolbox
    • Wassarman, D.A. & Sauer, F. TAF(II)250: a transcription toolbox. J. Cell Sci. 114, 2895-2902 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 2895-2902
    • Wassarman, D.A.1    Sauer, F.2
  • 57
    • 0032765083 scopus 로고    scopus 로고
    • Three-dimensional structure of the human TFIID-IIA-IIB complex
    • Andel, F. 3rd, Ladurner, A.G., Inouye, C., Tjian, R. & Nogales, E. Three-dimensional structure of the human TFIID-IIA-IIB complex. Science 286, 2153-2156 (1999).
    • (1999) Science , vol.286 , pp. 2153-2156
    • Andel, F.1    Ladurner, A.G.2    Inouye, C.3    Tjian, R.4    Nogales, E.5
  • 58
    • 0032589574 scopus 로고    scopus 로고
    • Three-dimensional struc-tures of the TAFII-containing complexes TFIID and TFTC
    • Brand, M., Leurent, C., Mallouh, V., Tora, L. & Schultz, P. Three-dimensional struc-tures of the TAFII-containing complexes TFIID and TFTC. Science 286, 2151-2153 (1999).
    • (1999) Science , vol.286 , pp. 2151-2153
    • Brand, M.1    Leurent, C.2    Mallouh, V.3    Tora, L.4    Schultz, P.5
  • 59
    • 0029869460 scopus 로고    scopus 로고
    • Structural similarity between TAFs and the heterotetrameric core of the histone octamer
    • Xie, X. et al. Structural similarity between TAFs and the heterotetrameric core of the histone octamer. Nature 380, 316-322 (1996).
    • (1996) Nature , vol.380 , pp. 316-322
    • Xie, X.1
  • 60
    • 0037160103 scopus 로고    scopus 로고
    • Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (HTAF(II)135) and hTAF12 (hTAF(II)20)
    • Werten, S. et al. Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20). J. Biol. Chem. 277, 45502-45509 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 45502-45509
    • Werten, S.1
  • 62
    • 0036646106 scopus 로고    scopus 로고
    • Mapping histone fold TAFs within yeast TFIID
    • Leurent, C. et al. Mapping histone fold TAFs within yeast TFIID. EMBO J. 21, 3424-3433 (2002).
    • (2002) EMBO J , vol.21 , pp. 3424-3433
    • Leurent, C.1
  • 63
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.9A resolution
    • Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F. & Richmond, T.J. Crystal structure of the nucleosome core particle at 2.9A resolution. Nature 389, 251-260 (1997).
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 64
    • 0035860472 scopus 로고    scopus 로고
    • Requirement of tissue-selective TBP-associated factor TAFII105 in ovarian development
    • Freiman, R.N. et al. Requirement of tissue-selective TBP-associated factor TAFII105 in ovarian development. Science 293, 2084-2087 (2001).
    • (2001) Science , vol.293 , pp. 2084-2087
    • Freiman, R.N.1
  • 65
    • 0035871354 scopus 로고    scopus 로고
    • Developmental regulation of transcription by a tissue-specific TAF homolog
    • Hiller, M.A., Lin, T.Y., Wood, C. & Fuller, M.T. Developmental regulation of transcription by a tissue-specific TAF homolog. Genes Dev. 15, 1021-1030 (2001).
    • (2001) Genes Dev , vol.15 , pp. 1021-1030
    • Hiller, M.A.1    Lin, T.Y.2    Wood, C.3    Fuller, M.T.4
  • 66
    • 0038601937 scopus 로고    scopus 로고
    • Systematic analysis of essential yeast TAFs in genome-wide transcription and preinitiation complex assembly
    • Shen, W.C. et al. Systematic analysis of essential yeast TAFs in genome-wide transcription and preinitiation complex assembly. EMBO J. 22, 3395-3402 (2003).
    • (2003) EMBO J , vol.22 , pp. 3395-3402
    • Shen, W.C.1
  • 67
    • 0034686037 scopus 로고    scopus 로고
    • TAF-containing and TAF-independent forms of transcriptionally active TBP in vivo
    • Kuras, L., Kosa, P., Mencia, M. & Struhl, K. TAF-containing and TAF-independent forms of transcriptionally active TBP in vivo. Science 288, 1244-1248 (2000).
    • (2000) Science , vol.288 , pp. 1244-1248
    • Kuras, L.1    Kosa, P.2    Mencia, M.3    Struhl, K.4
  • 68
    • 0034686001 scopus 로고    scopus 로고
    • Distinct classes of yeast promoters revealed by differential TAF recruitment
    • Li, X.Y., Bhaumik, S.R. & Green, M.R. Distinct classes of yeast promoters revealed by differential TAF recruitment. Science 288, 1242-1244 (2000).
    • (2000) Science , vol.288 , pp. 1242-1244
    • Li, X.Y.1    Bhaumik, S.R.2    Green, M.R.3
  • 69
    • 0001262663 scopus 로고    scopus 로고
    • Redundant roles for the TFIID and SAGA complexes in global transcription
    • Lee, T.I. et al. Redundant roles for the TFIID and SAGA complexes in global transcription. Nature 405, 701-704 (2000).
    • (2000) Nature , vol.405 , pp. 701-704
    • Lee, T.I.1
  • 70
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution
    • Zhang, G. et al. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 98, 811-824 (1999).
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1
  • 71
    • 0034724953 scopus 로고    scopus 로고
    • Architecture of RNA polymerase II and implications for the transcription mechanism
    • Cramer, P. et al. Architecture of RNA polymerase II and implications for the transcription mechanism. Science 288, 640-649 (2000).
    • (2000) Science , vol.288 , pp. 640-649
    • Cramer, P.1
  • 72
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 A resolution
    • Cramer, P., Bushnell, D.A. & Kornberg, R.D. Structural basis of transcription: RNA polymerase II at 2.8 A resolution. Science 292, 1863-1876 (2001).
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 73
    • 0043244877 scopus 로고    scopus 로고
    • Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase
    • Opalka, N. et al. Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase. Cell 114, 335-345 (2003).
    • (2003) Cell , vol.114 , pp. 335-345
    • Opalka, N.1
  • 74
    • 18344371347 scopus 로고    scopus 로고
    • Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase-promoter open complex
    • Mekler, V. et al. Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase-promoter open complex. Cell 108, 599-614 (2002).
    • (2002) Cell , vol.108 , pp. 599-614
    • Mekler, V.1
  • 75
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution
    • Murakami, K.S., Masuda, S. & Darst, S.A. Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution. Science 296, 1280-1284 (2002).
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 76
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution
    • Vassylyev, D.G. et al. Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution. Nature 417, 712-719 (2002).
    • (2002) Nature , vol.417 , pp. 712-719
    • Vassylyev, D.G.1
  • 77
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami, K.S., Masuda, S., Campbell, E.A., Muzzin, O. & Darst, S.A. Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science 296, 1285-1290 (2002).
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 78
    • 0037495037 scopus 로고    scopus 로고
    • Architecture of initiation-competent 12-subunit RNA polymerase II
    • Armache, K.J., Kettenberger, H. & Cramer, P. Architecture of initiation-competent 12-subunit RNA polymerase II. Proc. Natl. Acad. Sci. USA 100, 6964-6968 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6964-6968
    • Armache, K.J.1    Kettenberger, H.2    Cramer, P.3
  • 79
    • 0037832543 scopus 로고    scopus 로고
    • Complete, 12-subunit RNA polymerase II at 4.1-A resolution: Implications for the initiation of transcription
    • Bushnell, D.A. & Kornberg, R.D. Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription. Proc. Natl. Acad. Sci. USA 100, 6969-6973 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6969-6973
    • Bushnell, D.A.1    Kornberg, R.D.2
  • 80
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 A resolution
    • Gnatt, A.L., Cramer, P., Fu, J., Bushnell, D.A. & Kornberg, R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science 292, 1876-1882 (2001).
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 81
    • 1142310578 scopus 로고    scopus 로고
    • Structural basis of transcription: Separation of RNA from DNA by RNA polymerase II
    • Westover, K.D., Bushnell, D.A. & Kornberg, R.D. Structural basis of transcription: separation of RNA from DNA by RNA polymerase II. Science 303, 1014-1016 (2004).
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 82
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • Kettenberger, H., Armache, K.J. & Cramer, P. Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Cell 114, 347-357 (2003).
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 83
    • 0036671095 scopus 로고    scopus 로고
    • Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction
    • Davis, J.A., Takagi, Y., Kornberg, R.D. & Asturias, F.A. Structure of the yeast RNA polymerase II holoenzyme: mediator conformation and polymerase interaction. Mol. Cell 10, 409-415 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 409-415
    • Davis, J.A.1    Takagi, Y.2    Kornberg, R.D.3    Asturias, F.A.4
  • 84
    • 0842347413 scopus 로고    scopus 로고
    • Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex
    • Liu, Y. et al. Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex. Mol. Cell. Biol. 24, 1721-1735 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1721-1735
    • Liu, Y.1
  • 85
    • 1542334001 scopus 로고    scopus 로고
    • Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing
    • Ahn, S.H., Kim, M. & Buratowski, S. Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing. Mol. Cell 13, 67-76 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 67-76
    • Ahn, S.H.1    Kim, M.2    Buratowski, S.3
  • 86
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T. & Noel, J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7, 639-643 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 87
    • 0038094496 scopus 로고    scopus 로고
    • Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II
    • Fabrega, C., Shen, V., Shuman, S. & Lima, C.D. Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II. Mol. Cell 11, 1549-1561 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1549-1561
    • Fabrega, C.1    Shen, V.2    Shuman, S.3    Lima, C.D.4
  • 88
    • 0023923585 scopus 로고
    • Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein
    • Hope, I.A., Mahadevan, S. & Struhl, K. Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein. Nature 333, 635-640 (1988).
    • (1988) Nature , vol.333 , pp. 635-640
    • Hope, I.A.1    Mahadevan, S.2    Struhl, K.3
  • 89
    • 0026086914 scopus 로고
    • Critical structural elements of the VP16 transcrip- tional activation domain
    • Cress, W.D. & Triezenberg, S.J. Critical structural elements of the VP16 transcrip- tional activation domain. Science 251, 87-90 (1991).
    • (1991) Science , vol.251 , pp. 87-90
    • Cress, W.D.1    Triezenberg, S.J.2
  • 90
    • 0029791550 scopus 로고    scopus 로고
    • Identification of seven hydrophobic clusters in GCN4 making redundant contributions to transcrip- tional activation
    • Jackson, B.M., Drysdale, C.M., Natarajan, K. & Hinnebusch, A.G. Identification of seven hydrophobic clusters in GCN4 making redundant contributions to transcrip- tional activation. Mol. Cell. Biol. 16, 5557-5571 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5557-5571
    • Jackson, B.M.1    Drysdale, C.M.2    Natarajan, K.3    Hinnebusch, A.G.4
  • 91
    • 0034212441 scopus 로고    scopus 로고
    • Transcriptional regulation through mediator-like coactiva- tors in yeast and metazoan cells
    • Malik, S. & Roeder, R.G. Transcriptional regulation through mediator-like coactiva- tors in yeast and metazoan cells. Trends Biochem. Sci. 25, 277-283 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 277-283
    • Malik, S.1    Roeder, R.G.2
  • 92
    • 0037178788 scopus 로고    scopus 로고
    • Evidence for a mediator of RNA polymerase II transcriptional regulation conserved from yeast to man
    • Boube, M., Joulia, L., Cribbs, D.L. & Bourbon, H.M. Evidence for a mediator of RNA polymerase II transcriptional regulation conserved from yeast to man. Cell 110, 143-151 (2002).
    • (2002) Cell , vol.110 , pp. 143-151
    • Boube, M.1    Joulia, L.2    Cribbs, D.L.3    Bourbon, H.M.4
  • 93
    • 0033617334 scopus 로고    scopus 로고
    • Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter
    • Cosma, M.P., Tanaka, T. & Nasmyth, K. Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell 97, 299-311 (1999).
    • (1999) Cell , vol.97 , pp. 299-311
    • Cosma, M.P.1    Tanaka, T.2    Nasmyth, K.3
  • 94
    • 0842304212 scopus 로고    scopus 로고
    • RNA polymerase II (Pol II)-TFIIF and Pol II-medi- ator complexes: The major stable Pol II complexes and their activity in transcription initiation and reinitiation
    • Rani, P.G., Ranish, J.A. & Hahn, S. RNA polymerase II (Pol II)-TFIIF and Pol II-medi- ator complexes: the major stable Pol II complexes and their activity in transcription initiation and reinitiation. Mol. Cell. Biol. 24, 1709-1720 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1709-1720
    • Rani, P.G.1    Ranish, J.A.2    Hahn, S.3
  • 95
    • 0035834772 scopus 로고    scopus 로고
    • The structural and functional organization of the yeast mediator complex
    • Kang, J.S. et al. The structural and functional organization of the yeast mediator complex. J. Biol. Chem. 276, 42003-42010 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 42003-42010
    • Kang, J.S.1
  • 96
    • 0030825269 scopus 로고    scopus 로고
    • RAP74 induces promoter contacts by RNA polymerase II upstream and downstream of a DNA bend centered on the TATA box
    • Forget, D. et al. RAP74 induces promoter contacts by RNA polymerase II upstream and downstream of a DNA bend centered on the TATA box. Proc. Natl. Acad. Sci. USA 94, 7150-7155 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7150-7155
    • Forget, D.1
  • 97
    • 0030730281 scopus 로고    scopus 로고
    • Trajectory of DNA in the RNA polymerase II transcription preinitia- tion complex
    • Kim, T.-K. et al. Trajectory of DNA in the RNA polymerase II transcription preinitia- tion complex. Proc. Natl. Acad. Sci. USA 94, 12268-12273 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12268-12273
    • Kim, T.-K.1
  • 98
    • 0034717308 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent promoter melting by transcription factor IIH
    • Kim, T.K., Ebright, R.H. & Reinberg, D. Mechanism of ATP-dependent promoter melting by transcription factor IIH. Science 288, 1418-1422 (2000).
    • (2000) Science , vol.288 , pp. 1418-1422
    • Kim, T.K.1    Ebright, R.H.2    Reinberg, D.3
  • 99
    • 1642540256 scopus 로고    scopus 로고
    • Photo-cross-linking of a purified preinitiation complex reveals central roles for the RNA polymerase II mobile clamp and TFIIE in initiation mechanisms
    • Forget, D., Langelier, M.-F., Therien, C., Trinh, V. & Coulombe, B. Photo-cross-linking of a purified preinitiation complex reveals central roles for the RNA polymerase II mobile clamp and TFIIE in initiation mechanisms. Mol. Cell. Biol. 24, 1122-1131 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1122-1131
    • Forget, D.1    Langelier, M.-F.2    Therien, C.3    Trinh, V.4    Coulombe, B.5
  • 100
    • 1242339612 scopus 로고    scopus 로고
    • Topography of the euryarchaeal transcription initiation complex
    • Bartlett, M.S., Thomm, M. & Geiduschek, E.P. Topography of the euryarchaeal transcription initiation complex. J. Biol. Chem. 279, 5894-5903 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 5894-5903
    • Bartlett, M.S.1    Thomm, M.2    Geiduschek, E.P.3
  • 101
    • 1642453651 scopus 로고    scopus 로고
    • Transcription factor B contacts promoter DNA near the transcription start site of the archaeal transcription initiation complex
    • Renfrow, M.B. et al. Transcription factor B contacts promoter DNA near the transcription start site of the archaeal transcription initiation complex. J. Biol. Chem. 279, 2825-2831 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 2825-2831
    • Renfrow, M.B.1
  • 102
    • 0034613012 scopus 로고    scopus 로고
    • Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution
    • Gaiser, F., Tan, S. & Richmond, T.J. Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution. J. Mol. Biol. 302, 1119-1127 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 1119-1127
    • Gaiser, F.1    Tan, S.2    Richmond, T.J.3
  • 103
    • 0345701300 scopus 로고    scopus 로고
    • Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF
    • Kamada, K., Roeder, R.G. & Burley, S.K. Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF. Proc. Natl. Acad. Sci. USA 100, 2296-2299 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2296-2299
    • Kamada, K.1    Roeder, R.G.2    Burley, S.K.3
  • 104
    • 0038286151 scopus 로고    scopus 로고
    • NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1
    • Nguyen, B.D. et al. NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1. Proc. Natl. Acad. Sci. USA 100, 5688-5693 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5688-5693
    • Nguyen, B.D.1
  • 105
    • 0024470368 scopus 로고
    • Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II
    • Sopta, M., Burton, Z.F. & Greenblatt, J. Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II. Nature 341, 410-414 (1989).
    • (1989) Nature , vol.341 , pp. 410-414
    • Sopta, M.1    Burton, Z.F.2    Greenblatt, J.3
  • 106
    • 0028171310 scopus 로고
    • TFIIF-TAF-RNA polymerase II connection
    • Henry, N.L. et al. TFIIF-TAF-RNA polymerase II connection. Genes Dev. 8, 2868-2878 (1994).
    • (1994) Genes Dev , vol.8 , pp. 2868-2878
    • Henry, N.L.1
  • 107
    • 0029807310 scopus 로고    scopus 로고
    • A minimal set of RNA Pol II transcription protein interactions
    • Bushnell, D.A., Bamdad, C. & Kornberg, R.D. A minimal set of RNA Pol II transcription protein interactions. J. Biol. Chem. 271, 20170-20174 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 20170-20174
    • Bushnell, D.A.1    Bamdad, C.2    Kornberg, R.D.3
  • 108
    • 0030753149 scopus 로고    scopus 로고
    • Multiple functions of general transcription factors TFIIE and TFIIH in transcription: Possible points of regulation by trans-acting factors
    • Ohkuma, Y. Multiple functions of general transcription factors TFIIE and TFIIH in transcription: possible points of regulation by trans-acting factors. J. Biochem. 122, 481-489 (1997).
    • (1997) J. Biochem. , vol.122 , pp. 481-489
    • Ohkuma, Y.1
  • 109
    • 0026463076 scopus 로고
    • Purification and properties of S. Cere- visiae RNA polymerase II general initiation factor a
    • Sayre, M.H., Tschochner, H. & Kornberg, R.D. Purification and properties of S. cere- visiae RNA polymerase II general initiation factor a. J. Biol. Chem. 267, 23383-23387 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 23383-23387
    • Sayre, M.H.1    Tschochner, H.2    Kornberg, R.D.3
  • 110
    • 0030014797 scopus 로고    scopus 로고
    • Two-dimensional crystallography of TFIIB- and IIE-RNA polymerase II complexes: Implications for start site selection and initiation complex formation
    • Leuther, K.K., Bushnell, D.A. & Kornberg, R.D. Two-dimensional crystallography of TFIIB- and IIE-RNA polymerase II complexes: implications for start site selection and initiation complex formation. Cell 85, 773-779 (1996).
    • (1996) Cell , vol.85 , pp. 773-779
    • Leuther, K.K.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 111
    • 0034653424 scopus 로고    scopus 로고
    • Structure of the central core domain of TFIIEp with a novel double- stranded DNA-binding surface
    • Okuda, M. et al. Structure of the central core domain of TFIIEp with a novel double- stranded DNA-binding surface. EMBO J. 19, 1346-1356 (2000).
    • (2000) EMBO J , vol.19 , pp. 1346-1356
    • Okuda, M.1
  • 113
    • 0242498477 scopus 로고    scopus 로고
    • Revised subunit structure of yeast TFIIH and reconciliation with human TFIIH
    • Takagi, Y. et al. Revised subunit structure of yeast TFIIH and reconciliation with human TFIIH. J. Biol. Chem. 278, 43897-43900 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 43897-43900
    • Takagi, Y.1
  • 114
    • 0038094503 scopus 로고    scopus 로고
    • Basal transcription defect discriminates between xeroderma pig- mentosum and trichothiodystrophy in XPD patients
    • Dubaele, S. et al. Basal transcription defect discriminates between xeroderma pig- mentosum and trichothiodystrophy in XPD patients. Mol. Cell 11, 1635-1646 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1635-1646
    • Dubaele, S.1
  • 115
    • 0034268691 scopus 로고    scopus 로고
    • Molecular structure of human TFIIH
    • Schultz, P. et al. Molecular structure of human TFIIH. Cell 102, 599-607 (2000).
    • (2000) Cell , vol.102 , pp. 599-607
    • Schultz, P.1
  • 116
    • 0034264910 scopus 로고    scopus 로고
    • Electron crystal structure of the transcription factor and DNA repair complex, core TFIIH
    • Chang, W.H. & Kornberg, R.D. Electron crystal structure of the transcription factor and DNA repair complex, core TFIIH. Cell 102, 609-613 (2000).
    • (2000) Cell , vol.102 , pp. 609-613
    • Chang, W.H.1    Kornberg, R.D.2
  • 118
    • 0036303536 scopus 로고    scopus 로고
    • In vitro transcription and start site selection in Schizosaccharomycespombe
    • Choi, W.S., Yan, M., Nusinow, D. & Gralla, J.D. In vitro transcription and start site selection in Schizosaccharomycespombe. J. Mol. Biol. 319, 1005-1013 (2002).
    • (2002) J. Mol. Biol , vol.319 , pp. 1005-1013
    • Choi, W.S.1    Yan, M.2    Nusinow, D.3    Gralla, J.D.4
  • 119
    • 0025993771 scopus 로고
    • Mutations in a conserved region of RNA poly- merase II influence the accuracy of mRNA start site selection
    • Hekmatpanah, D.S. & Young, R.A. Mutations in a conserved region of RNA poly- merase II influence the accuracy of mRNA start site selection. Mol. Cell. Biol. 11, 5781-5791 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5781-5791
    • Hekmatpanah, D.S.1    Young, R.A.2
  • 120
    • 0028115840 scopus 로고
    • The sua8 suppressors of S. Cerevisiae encode replacements of conserved residues within the largest subunit of RNA poly- merase II and affect transcription start site selection similarly to sua7 (TFIIB) mutations
    • Berroteran, R.W., Ware, D.E. & Hampsey, M. The sua8 suppressors of S. cerevisiae encode replacements of conserved residues within the largest subunit of RNA poly- merase II and affect transcription start site selection similarly to sua7 (TFIIB) mutations. Mol. Cell. Biol. 14, 226-237 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 226-237
    • Berroteran, R.W.1    Ware, D.E.2    Hampsey, M.3
  • 121
    • 0026559077 scopus 로고
    • The yeast SUA7 gene encodes a homolog of human transcription factor TFIIB and is required for normal start site selection in vivo
    • Pinto, I., Ware, D.E. & Hampsey, M. The yeast SUA7 gene encodes a homolog of human transcription factor TFIIB and is required for normal start site selection in vivo. Cell 68, 977-988 (1992).
    • (1992) Cell , vol.68 , pp. 977-988
    • Pinto, I.1    Ware, D.E.2    Hampsey, M.3
  • 122
    • 0034960967 scopus 로고    scopus 로고
    • Promoter-specific shifts in transcription initiation conferred by yeast TFIIB mutations are determined by the sequence in the immediate vicinity of the start sites
    • Faitar, S.L., Brodie, S.A. & Ponticelli, A.S. Promoter-specific shifts in transcription initiation conferred by yeast TFIIB mutations are determined by the sequence in the immediate vicinity of the start sites. Mol. Cell. Biol. 21, 4427-4440 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4427-4440
    • Faitar, S.L.1    Brodie, S.A.2    Ponticelli, A.S.3
  • 123
    • 0029989059 scopus 로고    scopus 로고
    • Functional interaction between TFIIB and the Rpb9 (Ssu73) subunit of RNA polymerase II in Saccharomyces cerevisiae
    • Sun, Z.W., Tessmer, A. & Hampsey, M. Functional interaction between TFIIB and the Rpb9 (Ssu73) subunit of RNA polymerase II in Saccharomyces cerevisiae. Nucleic Acids Res. 24, 2560-2566 (1996).
    • (1996) Nucleic Acids Res , vol.24 , pp. 2560-2566
    • Sun, Z.W.1    Tessmer, A.2    Hampsey, M.3
  • 124
    • 0027197863 scopus 로고
    • DNA melting on yeast RNA polymerase II promoters
    • Giardina, C. & Lis, J.T. DNA melting on yeast RNA polymerase II promoters. Science 261, 759-762 (1993).
    • (1993) Science , vol.261 , pp. 759-762
    • Giardina, C.1    Lis, J.T.2
  • 125
    • 0033626545 scopus 로고    scopus 로고
    • Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription
    • Chen, H.T., Legault, P., Glushka, J., Omichinski, J.G. & Scott, R.A. Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription. Protein Sci. 9, 1743-1752 (2000).
    • (2000) Protein Sci , vol.9 , pp. 1743-1752
    • Chen, H.T.1    Legault, P.2    Glushka, J.3    Omichinski, J.G.4    Scott, R.A.5
  • 126
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: A-amanitin-RNA polymerase II cocrystal at 2.8 A resolution
    • Bushnell, D.A., Cramer, P. & Kornberg, R.D. Structural basis of transcription: a-amanitin-RNA polymerase II cocrystal at 2.8 A resolution. Proc. Natl. Acad. Sci. USA 99, 1218-1222 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1218-1222
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 127
    • 0033781448 scopus 로고    scopus 로고
    • Mechanism of promoter melting by the xeroderma pigmentosum complementation group B helicase of transcription factor IIH revealed by protein- DNA photo-cross-linking
    • Douziech, M. et al. Mechanism of promoter melting by the xeroderma pigmentosum complementation group B helicase of transcription factor IIH revealed by protein- DNA photo-cross-linking. Mol. Cell. Biol. 20, 8168-8177 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8168-8177
    • Douziech, M.1


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