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Volumn 14, Issue 8, 2007, Pages 696-703

The positions of TFIIF and TFIIE in the RNA polymerase II transcription preinitiation complex

Author keywords

[No Author keywords available]

Indexed keywords

RNA POLYMERASE II; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR II E; TRANSCRIPTION FACTOR II F; UNCLASSIFIED DRUG;

EID: 34547683177     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1272     Document Type: Article
Times cited : (144)

References (44)
  • 1
    • 2542428546 scopus 로고    scopus 로고
    • Structure and mechanism of the RNA polymerase II transcription machinery
    • Hahn, S. Structure and mechanism of the RNA polymerase II transcription machinery. Nat. Struct. Mol. Biol. 11, 394-403 (2004).
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 394-403
    • Hahn, S.1
  • 2
    • 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
  • 3
    • 0028019848 scopus 로고
    • Characterization of sua7 mutations defines a domain of TFIIB involved in transcription start site selection in yeast
    • Pinto, I., Wu, W.H., Na, J.G. & Hampsey, M. Characterization of sua7 mutations defines a domain of TFIIB involved in transcription start site selection in yeast. J. Biol. Chem. 269, 30569-30573 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 30569-30573
    • Pinto, I.1    Wu, W.H.2    Na, J.G.3    Hampsey, M.4
  • 4
    • 0028921452 scopus 로고
    • Identification of the gene (SSU71/TFG1) encoding the largest subunit of transcription factor TFIIF as a suppressor of a TFIIB mutation in Saccharomyces cerevisiae
    • Sun, Z.W. & Hampsey, M. Identification of the gene (SSU71/TFG1) encoding the largest subunit of transcription factor TFIIF as a suppressor of a TFIIB mutation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 92, 3127-3131 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3127-3131
    • Sun, Z.W.1    Hampsey, M.2
  • 5
    • 1942422184 scopus 로고    scopus 로고
    • Functional interaction between TFIIB and the Rpb2 subunit of RNA polymerase II: Implications for the mechanism of transcription initiation
    • Chen, B.S. & Hampsey, M. Functional interaction between TFIIB and the Rpb2 subunit of RNA polymerase II: implications for the mechanism of transcription initiation. Mol. Cell. Biol. 24, 3983-3991 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3983-3991
    • Chen, B.S.1    Hampsey, M.2
  • 6
    • 10044250105 scopus 로고    scopus 로고
    • Amino acid substitutions in yeast TFIIF confer upstream shifts in transcription initiation and altered interaction with RNA polymerase II
    • Ghazy, M.A., Brodie, S.A., Ammerman, M.L., Ziegler, L.M. & Ponticelli, A.S. Amino acid substitutions in yeast TFIIF confer upstream shifts in transcription initiation and altered interaction with RNA polymerase II. Mol. Cell. Biol. 24, 10975-10985 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 10975-10985
    • Ghazy, M.A.1    Brodie, S.A.2    Ammerman, M.L.3    Ziegler, L.M.4    Ponticelli, A.S.5
  • 7
    • 24944549150 scopus 로고    scopus 로고
    • Evidence that the Tfg1/Tfg2 dimer interface of TFIIF lies near the active center of the RNA polymerase II initiation complex
    • Freire-Picos, M.A., Krishnamurthy, S., Sun, Z.W. & Hampsey, M. Evidence that the Tfg1/Tfg2 dimer interface of TFIIF lies near the active center of the RNA polymerase II initiation complex. Nucleic Acids Res. 33, 5045-5052 (2005).
    • (2005) Nucleic Acids Res , vol.33 , pp. 5045-5052
    • Freire-Picos, M.A.1    Krishnamurthy, S.2    Sun, Z.W.3    Hampsey, M.4
  • 8
    • 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
  • 9
    • 5444275331 scopus 로고    scopus 로고
    • Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: A model for the structure of the PIC
    • Chen, H.T. & Hahn, S. Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: a model for the structure of the PIC. Cell 119, 169-180 (2004).
    • (2004) Cell , vol.119 , pp. 169-180
    • Chen, H.T.1    Hahn, S.2
  • 10
    • 1142274214 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms
    • 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 Angstroms. 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
  • 11
    • 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
  • 12
    • 1542676413 scopus 로고    scopus 로고
    • Yeast RNA polymerase II lacking the Rpb9 subunit is impaired for interaction with transcription factor IIF
    • Ziegler, L.M., Khaperskyy, D.A., Ammerman, M.L. & Ponticelli, A.S. Yeast RNA polymerase II lacking the Rpb9 subunit is impaired for interaction with transcription factor IIF. J. Biol. Chem. 278, 48950-48956 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 48950-48956
    • Ziegler, L.M.1    Khaperskyy, D.A.2    Ammerman, M.L.3    Ponticelli, A.S.4
  • 13
    • 0031463993 scopus 로고    scopus 로고
    • Three transitions in the RNA polymerase II transcription complex during initiation
    • Holstege, F.C., Fiedler, U. & Timmers, H.T. 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.1    Fiedler, U.2    Timmers, H.T.3
  • 14
    • 0037073047 scopus 로고    scopus 로고
    • Promoter escape by RNA polymerase II
    • Dvir, A. Promoter escape by RNA polymerase II. Biochim. Biophys. Acta 1577, 208-223 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 208-223
    • Dvir, A.1
  • 15
    • 21244484548 scopus 로고    scopus 로고
    • The role of the transcription bubble and TFIIB in promoter clearance by RNA polymerase II
    • Pal, M., Ponticelli, A.S. & Luse, D.S. The role of the transcription bubble and TFIIB in promoter clearance by RNA polymerase II. Mol. Cell 19, 101-110 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 101-110
    • Pal, M.1    Ponticelli, A.S.2    Luse, D.S.3
  • 16
    • 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
  • 17
    • 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
  • 18
    • 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
  • 19
    • 33745842952 scopus 로고    scopus 로고
    • DNA-tethered cleavage probe reveals the path for promoter DNA in the yeast preinitiation complex
    • Miller, G. & Hahn, S. A DNA-tethered cleavage probe reveals the path for promoter DNA in the yeast preinitiation complex. Nat. Struct. Mol. Biol. 13, 603-610 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 603-610
    • Miller, G.1    Hahn, S.A.2
  • 20
    • 0030730281 scopus 로고    scopus 로고
    • Trajectory of DNA in the RNA polymerase II transcription preinitiation complex
    • Kim, T.K. et al. Trajectory of DNA in the RNA polymerase II transcription preinitiation 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
  • 21
    • 0032161845 scopus 로고    scopus 로고
    • Wrapping of promoter DNA around the RNA polymerase II initiation complex induced by TFIIF
    • Robert, F. et al. Wrapping of promoter DNA around the RNA polymerase II initiation complex induced by TFIIF. Mol. Cell 2, 341-351 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 341-351
    • Robert, F.1
  • 22
    • 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
  • 23
    • 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
  • 24
    • 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
  • 25
    • 0041520960 scopus 로고    scopus 로고
    • An expanded eukaryotic genetic code
    • Chin, J.W. et al. An expanded eukaryotic genetic code. Science 301, 964-967 (2003).
    • (2003) Science , vol.301 , pp. 964-967
    • Chin, J.W.1
  • 26
    • 0023006043 scopus 로고
    • p-Benzoyl-L-phenylalanine, a new photoreactive amino acid. Photolabeling of calmodulin with a synthetic calmodulin-binding peptide
    • Kauer, J.C., Erickson-Viitanen, S., Wolfe, H.R. Jr. & DeGrado, W.F. p-Benzoyl-L-phenylalanine, a new photoreactive amino acid. Photolabeling of calmodulin with a synthetic calmodulin-binding peptide. J. Biol. Chem. 261, 10695-10700 (1986).
    • (1986) J. Biol. Chem , vol.261 , pp. 10695-10700
    • Kauer, J.C.1    Erickson-Viitanen, S.2    Wolfe Jr., H.R.3    DeGrado, W.F.4
  • 27
    • 0141680555 scopus 로고    scopus 로고
    • A composite upstream sequence motif potentiates tRNA gene transcription in yeast
    • Giuliodori, S. et al. A composite upstream sequence motif potentiates tRNA gene transcription in yeast. J. Mol. Biol. 333, 1-20 (2003).
    • (2003) J. Mol. Biol , vol.333 , pp. 1-20
    • Giuliodori, S.1
  • 28
    • 2442630488 scopus 로고    scopus 로고
    • Positive and negative functions of the SAGA complex mediated through interaction of Spt8 with TBP and the N-terminal domain of TFIIA
    • Warfield, L., Ranish, J.A. & Hahn, S. Positive and negative functions of the SAGA complex mediated through interaction of Spt8 with TBP and the N-terminal domain of TFIIA. Genes Dev. 18, 1022-1034 (2004).
    • (2004) Genes Dev , vol.18 , pp. 1022-1034
    • Warfield, L.1    Ranish, J.A.2    Hahn, S.3
  • 29
    • 18944364218 scopus 로고    scopus 로고
    • Function of a eukaryotic transcription activator during the transcription cycle
    • Fishburn, J., Mohibullah, N. & Hahn, S. Function of a eukaryotic transcription activator during the transcription cycle. Mol. Cell 18, 369-378 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 369-378
    • Fishburn, J.1    Mohibullah, N.2    Hahn, S.3
  • 30
    • 26444507919 scopus 로고    scopus 로고
    • Targets of the Gal4 transcription activator in functional transcription complexes
    • Reeves, W.M. & Hahn, S. Targets of the Gal4 transcription activator in functional transcription complexes. Mol. Cell. Biol. 25, 9092-9102 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 9092-9102
    • Reeves, W.M.1    Hahn, S.2
  • 31
    • 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
  • 32
    • 0034602843 scopus 로고    scopus 로고
    • Structural basis of preinitiation complex assembly on human pol II promoters
    • Tsai, F.T. & Sigler, P.B. Structural basis of preinitiation complex assembly on human pol II promoters. EMBO J. 19, 25-36 (2000).
    • (2000) EMBO J , vol.19 , pp. 25-36
    • Tsai, F.T.1    Sigler, P.B.2
  • 33
    • 0025993771 scopus 로고
    • Mutations in a conserved region of RNA polymerase II influence the accuracy of mRNA start site selection
    • Hekmatpanah, D.S. & Young, R.A. Mutations in a conserved region of RNA polymerase 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
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 37
    • 0029807310 scopus 로고    scopus 로고
    • A minimal set of RNA polymerase II transcription protein interactions
    • Bushnell, D.A., Bamdad, C. & Kornberg, R.D. A minimal set of RNA polymerase 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
  • 38
    • 0028115840 scopus 로고
    • The sua8 suppressors of Saccharomyces cerevisiae encode replacements of conserved residues within the largest subunit of RNA polymerase II and affect transcription start site selection similarly to sua7 (TFIIB) mutations
    • Berroteran, R.W., Ware, D.E. & Hampsey, M. The sua8 suppressors of Saccharomyces cerevisiae encode replacements of conserved residues within the largest subunit of RNA polymerase 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
  • 39
    • 33751212468 scopus 로고    scopus 로고
    • Initial transcription by RNA polymerase proceeds through a DNA-scrunching mechanism
    • Kapanidis, A.N. et al. Initial transcription by RNA polymerase proceeds through a DNA-scrunching mechanism. Science 314, 1144-1147 (2006).
    • (2006) Science , vol.314 , pp. 1144-1147
    • Kapanidis, A.N.1
  • 40
    • 33751218319 scopus 로고    scopus 로고
    • Abortive initiation and productive initiation by RNA polymerase involve DNA scrunching
    • Revyakin, A., Liu, C., Ebright, R.H. & Strick, T.R. Abortive initiation and productive initiation by RNA polymerase involve DNA scrunching. Science 314, 1139-1143 (2006).
    • (2006) Science , vol.314 , pp. 1139-1143
    • Revyakin, A.1    Liu, C.2    Ebright, R.H.3    Strick, T.R.4
  • 41
    • 0032900980 scopus 로고    scopus 로고
    • Intermediates in formation and activity of the RNA polymerase II preinitiation complex: Holoenzyme recruitment and a postrecruitment 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 postrecruitment 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
  • 43
    • 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
  • 44
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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