메뉴 건너뛰기




Volumn 23, Issue 9, 2003, Pages 3186-3201

Structural and functional analysis of mutations along the crystallographic dimer interface of the yeast TATA binding protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DIMER; MUTANT PROTEIN; PROTEIN; TAF1 PROTEIN; TATA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0037405079     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.9.3186-3201.2003     Document Type: Article
Times cited : (14)

References (85)
  • 1
    • 0035853690 scopus 로고    scopus 로고
    • High affinity interaction of yeast transcriptional regulator, Mot1, with TATA box-binding protein (TBP)
    • Adamkewicz, J. I., K. E. Hansen, W. A. Prud'homme, J. L. Davis, and J. Thorner. 2001. High affinity interaction of yeast transcriptional regulator, Mot1, with TATA box-binding protein (TBP). J. Biol. Chem. 276:11883-11894.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11883-11894
    • Adamkewicz, J.I.1    Hansen, K.E.2    Prud'homme, W.A.3    Davis, J.L.4    Thorner, J.5
  • 2
    • 0032765083 scopus 로고    scopus 로고
    • Three-dimensional structure of the human TFIID-IIA-IIB complex
    • Andel, F., III, A. G. Ladurner, C. Inouye, R. Tjian, and E. Nogales. 1999. Three-dimensional structure of the human TFIID-IIA-IIB complex. Science 286:2153-2156.
    • (1999) Science , vol.286 , pp. 2153-2156
    • Andel F. III1    Ladurner, A.G.2    Inouye, C.3    Tjian, R.4    Nogales, E.5
  • 3
    • 0026711087 scopus 로고
    • Biochemical and genetic characterization of a yeast TFIID mutant that alters transcription in vivo and DNA binding in vitro
    • Arndt, K. M., S. L. Ricupero, D. M. Eisenmann, and F. Winston. 1992. Biochemical and genetic characterization of a yeast TFIID mutant that alters transcription in vivo and DNA binding in vitro. Mol. Cell. Biol. 12:2372-2382.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2372-2382
    • Arndt, K.M.1    Ricupero, S.L.2    Eisenmann, D.M.3    Winston, F.4
  • 4
    • 0028904881 scopus 로고
    • TBP mutants defective in activated transcription in vivo
    • Arndt, K. M., S. Ricupero-Hovasse, and F. Winston. 1995. TBP mutants defective in activated transcription in vivo. EMBO J. 14:1490-1497.
    • (1995) EMBO J. , vol.14 , pp. 1490-1497
    • Arndt, K.M.1    Ricupero-Hovasse, S.2    Winston, F.3
  • 5
    • 0028270659 scopus 로고
    • Equivalent mutations in the two repeats of yeast TATA-binding protein confer distinct TATA recognition specificities
    • Arndt, K. M., C. R. Wobbe, S. Ricupero-Hovasse, K. Struhl, and F. Winston. 1994. Equivalent mutations in the two repeats of yeast TATA-binding protein confer distinct TATA recognition specificities. Mol. Cell. Biol. 14:3719-3728.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3719-3728
    • Arndt, K.M.1    Wobbe, C.R.2    Ricupero-Hovasse, S.3    Struhl, K.4    Winston, F.5
  • 6
    • 0027191870 scopus 로고
    • An ATP-dependent inhibitor of TBP binding to DNA
    • Auble, D. T., and S. Hahn. 1993. An ATP-dependent inhibitor of TBP binding to DNA. Genes Dev. 7:844-856.
    • (1993) Genes Dev. , vol.7 , pp. 844-856
    • Auble, D.T.1    Hahn, S.2
  • 7
    • 0028038315 scopus 로고
    • Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism
    • Auble, D. T., K. E. Hansen, C. G. Mueller, W. S. Lane, J. Thorner, and S. Hahn. 1994. Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism. Genes Dev. 8:1920-1934.
    • (1994) Genes Dev. , vol.8 , pp. 1920-1934
    • Auble, D.T.1    Hansen, K.E.2    Mueller, C.G.3    Lane, W.S.4    Thorner, J.5    Hahn, S.6
  • 8
    • 0030835671 scopus 로고    scopus 로고
    • Molecular analysis of the SNF2/SWI2 protein family member MOT1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA
    • Auble, D. T., D. Wang, K. W. Post, and S. Hahn. 1997. Molecular analysis of the SNF2/SWI2 protein family member MOT1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA. Mol. Cell. Biol. 17:4842-4851.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4842-4851
    • Auble, D.T.1    Wang, D.2    Post, K.W.3    Hahn, S.4
  • 9
    • 0033911879 scopus 로고    scopus 로고
    • Functional interaction of CCR4-NOT proteins with TATAA-binding protein (TBP) and its associated factors in yeast
    • Badarinarayana, V., Y. C. Chiang, and C. L. Denis. 2000. Functional interaction of CCR4-NOT proteins with TATAA-binding protein (TBP) and its associated factors in yeast. Genetics 155:1045-1054.
    • (2000) Genetics , vol.155 , pp. 1045-1054
    • Badarinarayana, V.1    Chiang, Y.C.2    Denis, C.L.3
  • 10
    • 0030987325 scopus 로고    scopus 로고
    • Structure-function analysis of TAF130: Identification and characterization of a high-affinity TATA-binding protein interaction domain in the N terminus of yeast TAF(II)130
    • Bai, Y., G. M. Perez, J. M. Beechem, and P. A. Weil. 1997. Structure-function analysis of TAF130: identification and characterization of a high-affinity TATA-binding protein interaction domain in the N terminus of yeast TAF(II)130. Mol. Cell. Biol. 17:3081-3093.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3081-3093
    • Bai, Y.1    Perez, G.M.2    Beechem, J.M.3    Weil, P.A.4
  • 11
    • 0035966126 scopus 로고    scopus 로고
    • Fluorescence-based analyses of the effects of full-length recombinant TAF130p on the interaction of TATA box-binding protein with TATA box DNA
    • Banik, U., J. M. Beechem, E. Klebanow, S. Schroeder, and P. A. Weil. 2001. Fluorescence-based analyses of the effects of full-length recombinant TAF130p on the interaction of TATA box-binding protein with TATA box DNA. J. Biol. Chem. 276:49100-49109.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49100-49109
    • Banik, U.1    Beechem, J.M.2    Klebanow, E.3    Schroeder, S.4    Weil, P.A.5
  • 12
    • 0033957403 scopus 로고    scopus 로고
    • Inhibition of TATA-binding protein function by SAGA subunits Spt3 and Spt8 at Gcn4-activated promoters
    • Belotserkovskaya, R., D. E. Sterner, M. Deng, M. H. Sayre, P. M. Lieberman, and S. L. Berger. 2000. Inhibition of TATA-binding protein function by SAGA subunits Spt3 and Spt8 at Gcn4-activated promoters. Mol. Cell. Biol. 20:634-647.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 634-647
    • Belotserkovskaya, R.1    Sterner, D.E.2    Deng, M.3    Sayre, M.H.4    Lieberman, P.M.5    Berger, S.L.6
  • 13
    • 0036838096 scopus 로고    scopus 로고
    • Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo
    • Bhaumik, S. R., and M. R. Green. 2002. Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo. Mol. Cell. Biol. 22:7365-7371.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7365-7371
    • Bhaumik, S.R.1    Green, M.R.2
  • 14
    • 0035423749 scopus 로고    scopus 로고
    • SAGA is an essential in vivo target of the yeast acidic activator Gal4p
    • Bhaumik, S. R., and M. R. Green. 2001. SAGA is an essential in vivo target of the yeast acidic activator Gal4p. Genes Dev. 15:1935-1945.
    • (2001) Genes Dev. , vol.15 , pp. 1935-1945
    • Bhaumik, S.R.1    Green, M.R.2
  • 15
    • 0030907242 scopus 로고    scopus 로고
    • A yeast TATA-binding protein mutant that selectively enhances gene expression from weak RNA polymerase II promoters
    • Blair, W. S., and B. R. Cullen. 1997. A yeast TATA-binding protein mutant that selectively enhances gene expression from weak RNA polymerase II promoters. Mol. Cell. Biol. 17:2888-2896.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2888-2896
    • Blair, W.S.1    Cullen, B.R.2
  • 16
    • 0032589574 scopus 로고    scopus 로고
    • Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC
    • Brand, M., C. Leurent, V. Mallouh, L. Tora, and P. Schultz. 1999. Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC. Science 286:2151-2153.
    • (1999) Science , vol.286 , pp. 2151-2153
    • Brand, M.1    Leurent, C.2    Mallouh, V.3    Tora, L.4    Schultz, P.5
  • 17
    • 0029802124 scopus 로고    scopus 로고
    • Radical mutations reveal TATA-box binding protein surfaces required for activated transcription in vivo
    • Bryant, G. O., L. S. Martel, S. K. Burley, and A. J. Berk. 1996. Radical mutations reveal TATA-box binding protein surfaces required for activated transcription in vivo. Genes Dev. 10:2491-2504.
    • (1996) Genes Dev. , vol.10 , pp. 2491-2504
    • Bryant, G.O.1    Martel, L.S.2    Burley, S.K.3    Berk, A.J.4
  • 18
    • 0026507091 scopus 로고
    • Transcription factor IID mutants defective for interaction with transcription factor IIA
    • Buratowski, S., and H. Zhou. 1992. Transcription factor IID mutants defective for interaction with transcription factor IIA. Science 255:1130-1132.
    • (1992) Science , vol.255 , pp. 1130-1132
    • Buratowski, S.1    Zhou, H.2
  • 19
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID (TFIID)
    • Burley, S. K., and R. G. Roeder. 1996. Biochemistry and structural biology of transcription factor IID (TFIID). Annu. Rev. Biochem. 65:769-799.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 769-799
    • Burley, S.K.1    Roeder, R.G.2
  • 20
    • 0034646399 scopus 로고    scopus 로고
    • Reevaluation of transcriptional regulation by TATA-binding protein oligomerization: Predominance of monomers
    • Campbell, K. M., R. T. Ranallo, L. A. Stargell, and K. J. Lumb. 2000. Reevaluation of transcriptional regulation by TATA-binding protein oligomerization: predominance of monomers. Biochemistry 39:2633-2638.
    • (2000) Biochemistry , vol.39 , pp. 2633-2638
    • Campbell, K.M.1    Ranallo, R.T.2    Stargell, L.A.3    Lumb, K.J.4
  • 21
    • 0033486113 scopus 로고    scopus 로고
    • A new regulatory domain on the TATA-binding protein
    • Cang, Y., D. T. Auble, and G. Prelich. 1999. A new regulatory domain on the TATA-binding protein. EMBO J. 18:6662-6671.
    • (1999) EMBO J. , vol.18 , pp. 6662-6671
    • Cang, Y.1    Auble, D.T.2    Prelich, G.3
  • 22
    • 0027250617 scopus 로고
    • Crystal structure of yeast TATA-binding protein and model for interaction with DNA
    • Chasman, D. I., K. M. Flaherty, P. A. Sharp, and R. D. Kornberg. 1993. Crystal structure of yeast TATA-binding protein and model for interaction with DNA. Proc. Natl. Acad. Sci. USA 90:8174-8178.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8174-8178
    • Chasman, D.I.1    Flaherty, K.M.2    Sharp, P.A.3    Kornberg, R.D.4
  • 23
    • 0031935594 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1
    • Chicca, J. J., II, D. T. Auble, and B. F. Pugh. 1998. Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1. Mol. Cell. Biol. 18:1701-1710.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1701-1710
    • Chicca J.J. II1    Auble, D.T.2    Pugh, B.F.3
  • 24
    • 0036810412 scopus 로고    scopus 로고
    • Interplay of TBP inhibitors in global transcriptional control
    • Chitikila, C., K. L. Huisinga, J. D. Irvin, M. Mitra, and B. F. Pugh. 2002. Interplay of TBP inhibitors in global transcriptional control. Mol. Cell 10: 871-882.
    • (2002) Mol. Cell , vol.10 , pp. 871-882
    • Chitikila, C.1    Huisinga, K.L.2    Irvin, J.D.3    Mitra, M.4    Pugh, B.F.5
  • 25
    • 0030795734 scopus 로고    scopus 로고
    • Slow dimer dissociation of the TATA binding protein dictates the kinetics of DNA binding
    • Coleman, R. A., and B. F. Pugh. 1997. Slow dimer dissociation of the TATA binding protein dictates the kinetics of DNA binding. Proc. Natl. Acad. Sci. USA 94:7221-7226.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7221-7226
    • Coleman, R.A.1    Pugh, B.F.2
  • 28
    • 0029860453 scopus 로고    scopus 로고
    • The NOT, SPT3, and MOT1 genes functionally interact to regulate transcription at core promoters
    • Collart, M. A. 1996. The NOT, SPT3, and MOT1 genes functionally interact to regulate transcription at core promoters. Mol. Cell. Biol. 16:6668-6676.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6668-6676
    • Collart, M.A.1
  • 29
    • 0025818453 scopus 로고
    • Functional differences between yeast and human TFIID are localized to the highly conserved region
    • Cormack, B. P., M. Strubin, A. S. Ponticelli, and K. Struhl. 1991. Functional differences between yeast and human TFIID are localized to the highly conserved region. Cell 65:341-348.
    • (1991) Cell , vol.65 , pp. 341-348
    • Cormack, B.P.1    Strubin, M.2    Ponticelli, A.S.3    Struhl, K.4
  • 30
    • 0033613911 scopus 로고    scopus 로고
    • The TATA-binding protein from Saccharomyces cerevisiae oligomerizes in solution at micromolar concentrations to form tetramers and octamers
    • Daugherty, M. A., M. Brenowitz, and M. G. Fried. 1999. The TATA-binding protein from Saccharomyces cerevisiae oligomerizes in solution at micromolar concentrations to form tetramers and octamers. J. Mol. Biol. 285:1389-1399.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1389-1399
    • Daugherty, M.A.1    Brenowitz, M.2    Fried, M.G.3
  • 32
    • 0032710459 scopus 로고    scopus 로고
    • The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo
    • Dudley, A. M., C. Rougeulle, and F. Winston. 1999. The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo. Genes Dev. 13:2940-2945.
    • (1999) Genes Dev. , vol.13 , pp. 2940-2945
    • Dudley, A.M.1    Rougeulle, C.2    Winston, F.3
  • 34
    • 0026764896 scopus 로고
    • SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae
    • Eisenmann, D. M., K. M. Arndt, S. L. Ricupero, J. W. Rooney, and F. Winston. 1992. SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae. Genes Dev. 6:1319-1331.
    • (1992) Genes Dev. , vol.6 , pp. 1319-1331
    • Eisenmann, D.M.1    Arndt, K.M.2    Ricupero, S.L.3    Rooney, J.W.4    Winston, F.5
  • 35
    • 0028233352 scopus 로고
    • The Saccharomyces cerevisiae SPT8 gene encodes a very acidic protein that is functionally related to SPT3 and TATA-binding protein
    • Eisenmann, D. M., C. Chapon, S. M. Roberts, C. Dollard, and F. Winston. 1994. The Saccharomyces cerevisiae SPT8 gene encodes a very acidic protein that is functionally related to SPT3 and TATA-binding protein. Genetics 137:647-657.
    • (1994) Genetics , vol.137 , pp. 647-657
    • Eisenmann, D.M.1    Chapon, C.2    Roberts, S.M.3    Dollard, C.4    Winston, F.5
  • 36
    • 0033961273 scopus 로고    scopus 로고
    • TATA-binding protein mutants that increase transcription from enhancerless and repressed promoters in vivo
    • Geisberg, J. V., and K. Struhl. 2000. TATA-binding protein mutants that increase transcription from enhancerless and repressed promoters in vivo. Mol. Cell. Biol. 20:1478-1488.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1478-1488
    • Geisberg, J.V.1    Struhl, K.2
  • 38
    • 0029907837 scopus 로고    scopus 로고
    • Characterization of the basal inhibitor of class II transcription NC2 from Saccharomyces cerevisiae
    • Goppelt, A., and M. Meisterernst. 1996. Characterization of the basal inhibitor of class II transcription NC2 from Saccharomyces cerevisiae. Nucleic Acids Res. 24:4450-4455.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4450-4455
    • Goppelt, A.1    Meisterernst, M.2
  • 40
    • 0032504104 scopus 로고    scopus 로고
    • A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation
    • Grant, P. A., D. Schieltz, M. G. Pray-Grant, D. J. Steger, J. C. Reese, J. R. Yates III, and J. L. Workman. 1998. A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation. Cell 94:45-53.
    • (1998) Cell , vol.94 , pp. 45-53
    • Grant, P.A.1    Schieltz, D.2    Pray-Grant, M.G.3    Steger, D.J.4    Reese, J.C.5    Yates J.R. III6    Workman, J.L.7
  • 41
    • 0026752598 scopus 로고
    • The human cytomegalovirus 80-kilodalton but not the 72-kilodalton immediate-early protein transactivates heterologous promoters in a TATA box-dependent mechanism and interacts directly with TFIID
    • Hagemeier, C., S. Walker, R. Caswell, T. Kouzarides, and J. Sinclair. 1992. The human cytomegalovirus 80-kilodalton but not the 72-kilodalton immediate-early protein transactivates heterologous promoters in a TATA box-dependent mechanism and interacts directly with TFIID. J. Virol. 66:4452-4456.
    • (1992) J. Virol. , vol.66 , pp. 4452-4456
    • Hagemeier, C.1    Walker, S.2    Caswell, R.3    Kouzarides, T.4    Sinclair, J.5
  • 42
    • 0027276508 scopus 로고
    • Binding activity of the human transcription factor TFIID
    • Icard-Liepkalns, C. 1993. Binding activity of the human transcription factor TFIID. Biochem. Biophys. Res. Commun. 193:453-459.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 453-459
    • Icard-Liepkalns, C.1
  • 43
    • 0028068714 scopus 로고
    • Facilitated binding of TATA-binding protein to nucleosomal DNA
    • Imbalzano, A. N., H. Kwon, M. R. Green, and R. E. Kingston. 1994. Facilitated binding of TATA-binding protein to nucleosomal DNA. Nature 370: 481-485.
    • (1994) Nature , vol.370 , pp. 481-485
    • Imbalzano, A.N.1    Kwon, H.2    Green, M.R.3    Kingston, R.E.4
  • 45
    • 0033152140 scopus 로고    scopus 로고
    • A role for TBP dimerization in preventing unregulated gene expression
    • Jackson-Fisher, A. J., C. Chitikila, M. Mitra, and B. F. Pugh. 1999. A role for TBP dimerization in preventing unregulated gene expression. Mol. Cell 3:717-727.
    • (1999) Mol. Cell , vol.3 , pp. 717-727
    • Jackson-Fisher, A.J.1    Chitikila, C.2    Mitra, M.3    Pugh, B.F.4
  • 47
    • 0028223755 scopus 로고
    • Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain
    • Kato, K., Y. Makino, T. Kishimoto, J. Yamauchi, S. Kato, M. Muramatsu, and T. Tamura. 1994. Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain. Nucleic Acids Res. 22: 1179-1185.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1179-1185
    • Kato, K.1    Makino, Y.2    Kishimoto, T.3    Yamauchi, J.4    Kato, S.5    Muramatsu, M.6    Tamura, T.7
  • 48
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim, J. L., D. B. Nikolov, and S. K. Burley. 1993. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365:520-527.
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 49
    • 0031037248 scopus 로고    scopus 로고
    • The Dr1/DRAP1 heterodimer is a global repressor of transcription in vivo
    • Kim, S., J. G. Na, M. Hampsey, and D. Reinberg. 1997. The Dr1/DRAP1 heterodimer is a global repressor of transcription in vivo. Proc. Natl. Acad. Sci. USA 94:820-825.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 820-825
    • Kim, S.1    Na, J.G.2    Hampsey, M.3    Reinberg, D.4
  • 50
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim, Y., J. H. Geiger, S. Hahn, and P. B. Sigler. 1993. Crystal structure of a yeast TBP/TATA-box complex. Nature 365:512-520.
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 51
    • 0035808448 scopus 로고    scopus 로고
    • Mutations in the TATA-binding protein, affecting transcriptional activation, show synthetic lethality with the TAF145 gene lacking the TAF N-terminal domain in Saccharomyces cerevisiae
    • Kobayashi, A., T. Miyake, Y. Ohyama, M. Kawaichi, and T. Kokubo. 2001. Mutations in the TATA-binding protein, affecting transcriptional activation, show synthetic lethality with the TAF145 gene lacking the TAF N-terminal domain in Saccharomyces cerevisiae. J. Biol. Chem. 276:395-405.
    • (2001) J. Biol. Chem. , vol.276 , pp. 395-405
    • Kobayashi, A.1    Miyake, T.2    Ohyama, Y.3    Kawaichi, M.4    Kokubo, T.5
  • 52
    • 0031883573 scopus 로고    scopus 로고
    • The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein
    • Kokubo, T., M. J. Swanson, J. I. Nishikawa, A. G. Hinnebusch, and Y. Nakatani. 1998. The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein. Mol. Cell. Biol. 18:1003-1012.
    • (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
  • 53
    • 0034691184 scopus 로고    scopus 로고
    • A role of transcriptional activators as antirepressors for the autoinhibitory activity of TATA box binding of transcription factor IID
    • Kotani, T., K. Banno, M. Ikura, A. G. Hinnebusch, Y. Nakatani, M. Kawaichi, and T. Kokubo. 2000. A role of transcriptional activators as antirepressors for the autoinhibitory activity of TATA box binding of transcription factor IID. Proc. Natl. Acad. Sci. USA 97:7178-7183.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7178-7183
    • Kotani, T.1    Banno, K.2    Ikura, M.3    Hinnebusch, A.G.4    Nakatani, Y.5    Kawaichi, M.6    Kokubo, T.7
  • 54
    • 0033610789 scopus 로고    scopus 로고
    • Identification of highly conserved amino-terminal segments of dTAFII230 and yTAFII145 that are functionally interchangeable for inhibiting TBP-DNA interactions in vitro and in promoting yeast cell growth in vivo
    • Kotani, T., T. Miyake, Y. Tsukihashi, A. G. Hinnebusch, Y. Nakatani, M. Kawaichi, and T. Kokubo. 1998. Identification of highly conserved amino-terminal segments of dTAFII230 and yTAFII145 that are functionally interchangeable for inhibiting TBP-DNA interactions in vitro and in promoting yeast cell growth in vivo. J. Biol. Chem. 273:32254-32264.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32254-32264
    • Kotani, T.1    Miyake, T.2    Tsukihashi, Y.3    Hinnebusch, A.G.4    Nakatani, Y.5    Kawaichi, M.6    Kokubo, T.7
  • 55
    • 0027298879 scopus 로고
    • Effect of the non-conserved N-terminus on the DNA binding activity of the yeast TATA binding protein
    • Kuddus, R., and M. C. Schmidt. 1993. Effect of the non-conserved N-terminus on the DNA binding activity of the yeast TATA binding protein. Nucleic Acids Res. 21:1789-1796.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1789-1796
    • Kuddus, R.1    Schmidt, M.C.2
  • 56
    • 0034686037 scopus 로고    scopus 로고
    • TAF-containing and TAF-independent forms of transcriptionally active TBP in vivo
    • Kuras, L., P. Kosa, M. Mencia, and K. Struhl. 2000. TAF-containing and TAF-independent forms of transcriptionally active TBP in vivo. Science 288:1244-1248.
    • (2000) Science , vol.288 , pp. 1244-1248
    • Kuras, L.1    Kosa, P.2    Mencia, M.3    Struhl, K.4
  • 57
    • 0033542436 scopus 로고    scopus 로고
    • Binding of TBP to promoters in vivo is stimulated by activators and requires Pol II holoenzyme
    • Kuras, L., and K. Struhl. 1999. Binding of TBP to promoters in vivo is stimulated by activators and requires Pol II holoenzyme. Nature 399:609-613.
    • (1999) Nature , vol.399 , pp. 609-613
    • Kuras, L.1    Struhl, K.2
  • 58
    • 0035425099 scopus 로고    scopus 로고
    • The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4
    • Larschan, E., and F. Winston. 2001. The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4. Genes Dev. 15:1946-1956.
    • (2001) Genes Dev. , vol.15 , pp. 1946-1956
    • Larschan, E.1    Winston, F.2
  • 59
    • 0026646052 scopus 로고
    • TFIIA induces conformational changes in TFIID via interactions with the basic repeat
    • Lee, D. K., J. DeJong, S. Hashimoto, M. Horikoshi, and R. G. Roeder. 1992. TFIIA induces conformational changes in TFIID via interactions with the basic repeat. Mol. Cell. Biol. 12:5189-5196.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5189-5196
    • Lee, D.K.1    DeJong, J.2    Hashimoto, S.3    Horikoshi, M.4    Roeder, R.G.5
  • 60
    • 0035024076 scopus 로고    scopus 로고
    • Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein
    • Lee, M., and K. Struhl. 2001. Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein. Genetics 158:87-93.
    • (2001) Genetics , vol.158 , pp. 87-93
    • Lee, M.1    Struhl, K.2
  • 61
    • 0029129287 scopus 로고
    • Mutations on the DNA-binding surface of TATA-binding protein can specifically impair the response to acidic activators in vivo
    • Lee, M., and K. Struhl. 1995. Mutations on the DNA-binding surface of TATA-binding protein can specifically impair the response to acidic activators in vivo. Mol. Cell. Biol. 15:5461-5469.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5461-5469
    • Lee, M.1    Struhl, K.2
  • 63
    • 0033542484 scopus 로고    scopus 로고
    • Enhancement of TBP binding by activators and general transcription factors
    • Li, X.-Y., A. Virbasius, X. Zhu, and M. Green. 1999. Enhancement of TBP binding by activators and general transcription factors. Nature 399:605-609.
    • (1999) Nature , vol.399 , pp. 605-609
    • Li, X.-Y.1    Virbasius, A.2    Zhu, X.3    Green, M.4
  • 64
    • 0034686001 scopus 로고    scopus 로고
    • Distinct classes of yeast promoters revealed by differential TAF recruitment
    • Li, X. Y., S. R. Bhaumik, and M. R. Green. 2000. Distinct classes of yeast promoters revealed by differential TAF recruitment. Science 288:1242-1244.
    • (2000) Science , vol.288 , pp. 1242-1244
    • Li, X.Y.1    Bhaumik, S.R.2    Green, M.R.3
  • 65
    • 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., R. Ishima, K. I. Tong, S. Bagby, T. Kokubo, D. R. Muhandiram, L. E. Kay, Y. Nakatani, and M. Ikura. 1998. 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) Cell , vol.94 , pp. 573-583
    • Liu, D.1    Ishima, R.2    Tong, K.I.3    Bagby, S.4    Kokubo, T.5    Muhandiram, D.R.6    Kay, L.E.7    Nakatani, Y.8    Ikura, M.9
  • 66
    • 0034692875 scopus 로고    scopus 로고
    • The essential function of Notl lies within the Ccr4-Not complex
    • Maillet, L., C. Tu, Y. K. Hong, E. O. Shuster, and M. A. Collart. 2000. The essential function of Notl lies within the Ccr4-Not complex. J. Mol. Biol. 303:131-143.
    • (2000) J. Mol. Biol. , vol.303 , pp. 131-143
    • Maillet, L.1    Tu, C.2    Hong, Y.K.3    Shuster, E.O.4    Collart, M.A.5
  • 68
    • 0032911185 scopus 로고    scopus 로고
    • MOT1 can activate basal transcription in vitro by regulating the distribution of TATA binding protein between promoter and nonpromoter sites
    • Muldrow, T. A., A. M. Campbell, P. A. Weil, and D. T. Auble. 1999. MOT1 can activate basal transcription in vitro by regulating the distribution of TATA binding protein between promoter and nonpromoter sites. Mol. Cell. Biol. 19:2835-2845.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2835-2845
    • Muldrow, T.A.1    Campbell, A.M.2    Weil, P.A.3    Auble, D.T.4
  • 70
    • 0031024494 scopus 로고    scopus 로고
    • Drosophila TAF(II)230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein
    • Nishikawa, J., T. Kokubo, M. Horikoshi, R. G. Roeder, and Y. Nakatani. 1997. Drosophila TAF(II)230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein. Proc. Natl. Acad. Sci. USA 94:85-90.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 85-90
    • Nishikawa, J.1    Kokubo, T.2    Horikoshi, M.3    Roeder, R.G.4    Nakatani, Y.5
  • 71
    • 0034785593 scopus 로고    scopus 로고
    • TAF(II)170 interacts with the concave surface of TATA-binding protein to inhibit its DNA binding activity
    • Pereira, L. A., J. A. van der Knaap, V. van den Boom, F. A. van den Heuvel, and H. T. Timmers. 2001. TAF(II)170 interacts with the concave surface of TATA-binding protein to inhibit its DNA binding activity. Mol. Cell. Biol. 21:7523-7534.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7523-7534
    • Pereira, L.A.1    Van der Knaap, J.A.2    Van den Boom, V.3    Van den Heuvel, F.A.4    Timmers, H.T.5
  • 72
    • 0029008807 scopus 로고
    • Yeast TATA binding protein interaction with DNA: Fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics
    • Perez-Howard, G. M., P. A. Weil, and J. M. Beechem. 1995. Yeast TATA binding protein interaction with DNA: fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics. Biochemistry 34:8005-8017.
    • (1995) Biochemistry , vol.34 , pp. 8005-8017
    • Perez-Howard, G.M.1    Weil, P.A.2    Beechem, J.M.3
  • 73
    • 0028070378 scopus 로고
    • Yeast TAF170 is encoded by MOT1 and exists in a TATA box-binding protein (TBP)-TBP-associated factor complex distinct from transcription factor IID
    • Poon, D., A. M. Campbell, Y. Bai, and P. A. Weil. 1994. Yeast TAF170 is encoded by MOT1 and exists in a TATA box-binding protein (TBP)-TBP-associated factor complex distinct from transcription factor IID. J. Biol. Chem. 269:23135-23140.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23135-23140
    • Poon, D.1    Campbell, A.M.2    Bai, Y.3    Weil, P.A.4
  • 74
    • 0025996772 scopus 로고
    • The conserved carboxy-terminal domain of Saccharomyces cerevisiae TFIID is sufficient to support normal cell growth
    • Poon, D., S. Schroeder, C. K. Wang, T. Yamamoto, M. Horikoshi, R. G. Roeder, and P. A. Weil. 1991. The conserved carboxy-terminal domain of Saccharomyces cerevisiae TFIID is sufficient to support normal cell growth. Mol. Cell. Biol. 11:4809-4821.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4809-4821
    • Poon, D.1    Schroeder, S.2    Wang, C.K.3    Yamamoto, T.4    Horikoshi, M.5    Roeder, R.G.6    Weil, P.A.7
  • 75
    • 0034609446 scopus 로고    scopus 로고
    • Control of gene expression through regulation of the TATA binding protein
    • Pugh, B. F. 2000. Control of gene expression through regulation of the TATA binding protein. Gene 255:1-14.
    • (2000) Gene , vol.255 , pp. 1-14
    • Pugh, B.F.1
  • 76
    • 0025848742 scopus 로고
    • Dominant negative mutations in yeast TFIID define a bipartite DNA-binding region
    • Reddy, P., and S. Hahn. 1991. Dominant negative mutations in yeast TFIID define a bipartite DNA-binding region. Cell 65:349-357.
    • (1991) Cell , vol.65 , pp. 349-357
    • Reddy, P.1    Hahn, S.2
  • 77
    • 0028169339 scopus 로고
    • Yeast TAFIIS in a multisubunit complex required for activated transcription
    • Reese, J. C., L. Apone, S. S. Walker, L. A. Griffin, and M. R. Green. 1994. Yeast TAFIIS in a multisubunit complex required for activated transcription. Nature 371:523-527.
    • (1994) Nature , vol.371 , pp. 523-527
    • Reese, J.C.1    Apone, L.2    Walker, S.S.3    Griffin, L.A.4    Green, M.R.5
  • 78
    • 0036318573 scopus 로고    scopus 로고
    • Molecular characterization of Saccharomyces cerevisiae TFIID
    • Sanders, S. L., K. A. Garbett, and P. A. Weil. 2002. Molecular characterization of Saccharomyces cerevisiae TFIID. Mol. Cell. Biol. 22:6000-6013.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6000-6013
    • Sanders, S.L.1    Garbett, K.A.2    Weil, P.A.3
  • 79
    • 0026566106 scopus 로고
    • Yeast and human TFIID with altered DNA-binding specificity for TATA elements
    • Strubin, M., and K. Struhl. 1992. Yeast and human TFIID with altered DNA-binding specificity for TATA elements. Cell 68:721-730.
    • (1992) Cell , vol.68 , pp. 721-730
    • Strubin, M.1    Struhl, K.2
  • 80
    • 0033538531 scopus 로고    scopus 로고
    • Fundamentally different logic of gene regulation in eukaryotes and prokaryotes
    • Struhl, K. 1999. Fundamentally different logic of gene regulation in eukaryotes and prokaryotes. Cell 98:1-4.
    • (1999) Cell , vol.98 , pp. 1-4
    • Struhl, K.1
  • 81
    • 0029896209 scopus 로고    scopus 로고
    • Dimerization of TFIID when not bound to DNA
    • Taggart, A. K., and B. F. Pugh. 1996. Dimerization of TFIID when not bound to DNA. Science 272:1331-1333.
    • (1996) Science , vol.272 , pp. 1331-1333
    • Taggart, A.K.1    Pugh, B.F.2
  • 82
    • 0021749263 scopus 로고
    • The SPT3 gene is required for normal transcription of Ty elements in S. cerevisiae
    • Winston, F., K. J. Durbin, and G. R. Fink. 1984. The SPT3 gene is required for normal transcription of Ty elements in S. cerevisiae. Cell 39:675-682.
    • (1984) Cell , vol.39 , pp. 675-682
    • Winston, F.1    Durbin, K.J.2    Fink, G.R.3
  • 85
    • 0025859999 scopus 로고
    • Requirement for acidic amino acid residues immediately N-terminal to the conserved domain of Saccharomyces cerevisiae TFIID
    • Zhou, Q. A., M. C. Schmidt, and A. J. Berk. 1991. Requirement for acidic amino acid residues immediately N-terminal to the conserved domain of Saccharomyces cerevisiae TFIID. EMBO J. 10:1843-1852.
    • (1991) EMBO J. , vol.10 , pp. 1843-1852
    • Zhou, Q.A.1    Schmidt, M.C.2    Berk, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.