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Volumn 16, Issue 5, 1996, Pages 2110-2118

Fos-jun dimerization promotes interaction of the basic region with TFIIE-34 and TFIIF

Author keywords

[No Author keywords available]

Indexed keywords

REGULATOR PROTEIN; RNA POLYMERASE II; TRANSCRIPTION FACTOR;

EID: 0029862609     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.16.5.2110     Document Type: Article
Times cited : (34)

References (80)
  • 1
    • 0025782826 scopus 로고
    • Transcriptional regulation by Fos and Jun in vitro: Interaction among multiple activator and regulatory domains
    • Abate, C., D. Luk, and T. Curran. 1991 Transcriptional regulation by Fos and Jun in vitro: interaction among multiple activator and regulatory domains Mol. Cell. Biol. 11:3624-3632.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3624-3632
    • Abate, C.1    Luk, D.2    Curran, T.3
  • 2
    • 0025123272 scopus 로고
    • Fos and Jun cooperate in transcriptional regulation via heterologous activation domains
    • Abate, C., D. Luk, E. Gagne, R. G. Reeder, and T. Curran. 1990. Fos and Jun cooperate in transcriptional regulation via heterologous activation domains. Mol. Cell. Biol. 10:5532-5535.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5532-5535
    • Abate, C.1    Luk, D.2    Gagne, E.3    Reeder, R.G.4    Curran, T.5
  • 3
    • 0025091890 scopus 로고
    • Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: Both Fos and Jun contact DNA directly
    • Abate, C., D. Luk, R. Gentz, F. J. Rauscher, and T. Curran. 1990. Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly. Proc. Natl. Acad. Sci. USA 87:1032-1036
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1032-1036
    • Abate, C.1    Luk, D.2    Gentz, R.3    Rauscher, F.J.4    Curran, T.5
  • 4
    • 0026357519 scopus 로고
    • Fos is phosphorylated by p34cdc2, cAMP-dependent protein kinase and protein kinase C at multiple sites clustered within regulatory regions
    • Abate, C., D. R. Marshak, and T. Curran. 1991. Fos is phosphorylated by p34cdc2, cAMP-dependent protein kinase and protein kinase C at multiple sites clustered within regulatory regions. Oncogene 6:2179-2185.
    • (1991) Oncogene , vol.6 , pp. 2179-2185
    • Abate, C.1    Marshak, D.R.2    Curran, T.3
  • 5
    • 0025251136 scopus 로고
    • Control of c-Jun activity by interaction of a cell-specific inhibitor with regulatory domain δ: Differences between v-and c-Jun
    • Baichwal, V. R., and R. Tjian. 1990. Control of c-Jun activity by interaction of a cell-specific inhibitor with regulatory domain δ: differences between v-and c-Jun. Cell 63:815-825.
    • (1990) Cell , vol.63 , pp. 815-825
    • Baichwal, V.R.1    Tjian, R.2
  • 6
    • 0026725899 scopus 로고
    • Jun is phosphorylated by several protein kinases at the same sites that are modified in serum-stimulated fibroblasts
    • Baker, S. J., T. K. Kerppola, D. Luk, M. T. Vandenberg, D. R. Marshak, T. Curran, and C. Abate. 1992. Jun is phosphorylated by several protein kinases at the same sites that are modified in serum-stimulated fibroblasts. Mol. Cell Biol. 12:4694-4705.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 4694-4705
    • Baker, S.J.1    Kerppola, T.K.2    Luk, D.3    Vandenberg, M.T.4    Marshak, D.R.5    Curran, T.6    Abate, C.7
  • 7
    • 0028243510 scopus 로고
    • Positive control mutations in the MyoD basic region fail to show cooperative DNA binding and transcriptional activation in vitro
    • Bengal, E., O. Flores, P. N. Rangarajan, A. Chen, H. Weintraub, and I. M. Verma. 1994. Positive control mutations in the MyoD basic region fail to show cooperative DNA binding and transcriptional activation in vitro. Proc. Natl Acad. Sci. USA 91:6221-6225.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6221-6225
    • Bengal, E.1    Flores, O.2    Rangarajan, P.N.3    Chen, A.4    Weintraub, H.5    Verma, I.M.6
  • 8
    • 0028291252 scopus 로고
    • The basics of basal transcription by RNA polymerase II
    • Buratowski, S. 1994. The basics of basal transcription by RNA polymerase II. Cell 77:1-3.
    • (1994) Cell , vol.77 , pp. 1-3
    • Buratowski, S.1
  • 9
    • 0027275111 scopus 로고
    • RAP30/74 (transcription factor IIF) is required for promoter escape by RNA polymerase II
    • Chang, C., C. F. Kostrub, and Z. F. Burton. 1993. RAP30/74 (transcription factor IIF) is required for promoter escape by RNA polymerase II. J. Biol. Chem. 268:20482-20489.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20482-20489
    • Chang, C.1    Kostrub, C.F.2    Burton, Z.F.3
  • 10
    • 0028108925 scopus 로고
    • Assembly of recombinant TFIID reveals differential coactivator requirements for distinct transcriptional activators
    • Chen, J. L., L. D. Attardi, C. P. Verrijzer, K. Yokomori, and R. Tjian. 1994. Assembly of recombinant TFIID reveals differential coactivator requirements for distinct transcriptional activators. Cell 79:93-105.
    • (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
  • 11
    • 0027772890 scopus 로고
    • Eukaryotic activators function during multiple steps of preinitiation complex assembly
    • Choy, B., and M. R. Green. 1993. Eukaryotic activators function during multiple steps of preinitiation complex assembly. Nature (London) 366:531-536.
    • (1993) Nature (London) , vol.366 , pp. 531-536
    • Choy, B.1    Green, M.R.2
  • 12
    • 0028291063 scopus 로고
    • Mutations in the zinc-finger region of the yeast regulatory protein ADR1 affect both DNA binding and transcriptional activation
    • Cook, W. J., S. P. Mosley, D. C. Audino, U. L. Mullaney, A. Rovelli, G. Stewart, and C. L. Denis. 1994. Mutations in the zinc-finger region of the yeast regulatory protein ADR1 affect both DNA binding and transcriptional activation. J. Biol. Chem. 269:9374-9379.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9374-9379
    • Cook, W.J.1    Mosley, S.P.2    Audino, D.C.3    Mullaney, U.L.4    Rovelli, A.5    Stewart, G.6    Denis, C.L.7
  • 13
    • 0023798751 scopus 로고
    • Fos and Jun: The AP-1 connection
    • Curran, T., and B. Franza. 1988. Fos and Jun: the AP-1 connection. Cell 55:395-397.
    • (1988) Cell , vol.55 , pp. 395-397
    • Curran, T.1    Franza, B.2
  • 14
    • 0020037140 scopus 로고
    • Candidate product of the FBJ murine osteosarcoma virus oncogene: Characterization of a 55,000-dalton phosphoprotein
    • Curran, T., and N. M. Teich. 1982. Candidate product of the FBJ murine osteosarcoma virus oncogene: characterization of a 55,000-dalton phosphoprotein. J Virol. 42:114-122.
    • (1982) J Virol. , vol.42 , pp. 114-122
    • Curran, T.1    Teich, N.M.2
  • 15
    • 0001817670 scopus 로고
    • Dangerous liaisons: Fos and Jun, oncogenic transcription factors
    • S. L. McKnight and K. R. Yamamoto (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Curran, T., and P. K. Vogt. 1992. Dangerous liaisons: Fos and Jun, oncogenic transcription factors, p. 797-831. In S. L. McKnight and K. R. Yamamoto (ed.), Transcriptional regulation, vol. 2. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) Transcriptional Regulation , vol.2 , pp. 797-831
    • Curran, T.1    Vogt, P.K.2
  • 16
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983 Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res 11:1475-1489.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 18
    • 0024616057 scopus 로고
    • Multiple sequence elements in the c-fos promoter mediate induction by cAMP
    • Fisch, T. M., R. Prywes, M. C. Simon, and R. G. Roeder. 1989. Multiple sequence elements in the c-fos promoter mediate induction by cAMP. Genes Dev. 3:198-211.
    • (1989) Genes Dev. , vol.3 , pp. 198-211
    • Fisch, T.M.1    Prywes, R.2    Simon, M.C.3    Roeder, R.G.4
  • 20
    • 0028018945 scopus 로고
    • Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes
    • Ge, H., and R. G. Roeder. 1994. Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes. Cell 78:513-523.
    • (1994) Cell , vol.78 , pp. 513-523
    • Ge, H.1    Roeder, R.G.2
  • 21
    • 0024590007 scopus 로고
    • Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains
    • Gentz, R., F. J. Rauscher, C. Abate, and T. Curran. 1989. Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains Science 243:1695-1699.
    • (1989) Science , vol.243 , pp. 1695-1699
    • Gentz, R.1    Rauscher, F.J.2    Abate, C.3    Curran, T.4
  • 22
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover, J. N., and S. C. Harrison. 1995. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature (London) 373:257-261.
    • (1995) Nature (London) , vol.373 , pp. 257-261
    • Glover, J.N.1    Harrison, S.C.2
  • 23
    • 0027332365 scopus 로고
    • Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB
    • Goodrich, J. A., T. Hoey, C. J. Thut, A. Admon, and R. Tjian. 1993. Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB. Cell 75:519-530.
    • (1993) Cell , vol.75 , pp. 519-530
    • Goodrich, J.A.1    Hoey, T.2    Thut, C.J.3    Admon, A.4    Tjian, R.5
  • 24
    • 0028352861 scopus 로고
    • Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II
    • Goodrich, J. A., and R. Tjian. 1994. Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II. Cell 77: 145-156.
    • (1994) Cell , vol.77 , pp. 145-156
    • Goodrich, J.A.1    Tjian, R.2
  • 26
    • 0025820544 scopus 로고
    • Cloning of a human gene encoding the general transcription factor TFIIB
    • Ha, I., W. Lane, and D. Reinberg. 1991. Cloning of a human gene encoding the general transcription factor TFIIB. Nature (London) 352:689-695.
    • (1991) Nature (London) , vol.352 , pp. 689-695
    • Ha, I.1    Lane, W.2    Reinberg, D.3
  • 27
    • 0025878233 scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Hai, T., and T. Curran. 1991. Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc. Natl. Acad Sci. USA 88:3720-3724
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 3720-3724
    • Hai, T.1    Curran, T.2
  • 28
    • 0027242180 scopus 로고
    • c-Jun is essential for normal mouse development and hepatogenesis
    • Hilberg, F., A. Aguzzi, N. Howells, and E. F. Wagner. 1993. c-Jun is essential for normal mouse development and hepatogenesis. Nature (London) 365: 179-181
    • (1993) Nature (London) , vol.365 , pp. 179-181
    • Hilberg, F.1    Aguzzi, A.2    Howells, N.3    Wagner, E.F.4
  • 29
    • 0027406964 scopus 로고
    • Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators
    • Hoey, T., R. O. J. Weinzierl, G. Gill, J.-L. Chen, B. D. Dynlacht, and R. Tjian. 1993. Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators. Cell 72:247-260
    • (1993) Cell , vol.72 , pp. 247-260
    • Hoey, T.1    Weinzierl, R.O.J.2    Gill, G.3    Chen, J.-L.4    Dynlacht, B.D.5    Tjian, R.6
  • 30
    • 0028964168 scopus 로고
    • The requirement for the basal transcription factor IIE is determined by the helical stability of the promoter DNA
    • Holstege, F. C. P., D. Tantin, M. Carey, P. C. van der Vliet, and H. T. M. Timmers. 1995. The requirement for the basal transcription factor IIE is determined by the helical stability of the promoter DNA EMBO J. 14:810-819.
    • (1995) EMBO J. , vol.14 , pp. 810-819
    • Holstege, F.C.P.1    Tantin, D.2    Carey, M.3    Van Der Vliet, P.C.4    Timmers, H.T.M.5
  • 33
    • 0023322681 scopus 로고
    • Identification of a rat liver nuclear protein that binds to the enhancer core element of three animal viruses
    • Johnson, P. F., W. H. Landschulz, B. J. Graves, and S. L. McKnight. 1987. Identification of a rat liver nuclear protein that binds to the enhancer core element of three animal viruses Genes Dev. 1:133-146.
    • (1987) Genes Dev. , vol.1 , pp. 133-146
    • Johnson, P.F.1    Landschulz, W.H.2    Graves, B.J.3    McKnight, S.L.4
  • 34
    • 0028821599 scopus 로고
    • Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor
    • Joliot, V., M. Demma, and R. Prywes. 1995. Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor. Nature (London) 373:632-635.
    • (1995) Nature (London) , vol.373 , pp. 632-635
    • Joliot, V.1    Demma, M.2    Prywes, R.3
  • 35
    • 0028986047 scopus 로고
    • Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor
    • Kataoka, K., K. Igarashi, K. Itoh, K. T. Fujiwara, M. Noda, M. Yamamoto, and M. Nishizawa. 1995 Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. Mol. Cell. Biol. 15:2180-2190.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2180-2190
    • Kataoka, K.1    Igarashi, K.2    Itoh, K.3    Fujiwara, K.T.4    Noda, M.5    Yamamoto, M.6    Nishizawa, M.7
  • 36
    • 0028053782 scopus 로고
    • A conserved region adjacent to the basic domain is required for recognition of an extended DNA binding site by Maf/Nrl family proteins
    • Kerppola, T. K., and T. Curran. 1994. A conserved region adjacent to the basic domain is required for recognition of an extended DNA binding site by Maf/Nrl family proteins. Oncogene 9:3149-3158.
    • (1994) Oncogene , vol.9 , pp. 3149-3158
    • Kerppola, T.K.1    Curran, T.2
  • 37
    • 0028154038 scopus 로고
    • Maf and Nrl can bind to AP-1 sites and form heterodimers with Fos and Jun
    • Kerppola, T. K., and T. Curran. 1994. Maf and Nrl can bind to AP-1 sites and form heterodimers with Fos and Jun. Oncogene 9:675-684
    • (1994) Oncogene , vol.9 , pp. 675-684
    • Kerppola, T.K.1    Curran, T.2
  • 38
    • 0026592736 scopus 로고
    • The general transcription factor RAP30 binds to RNA polymerase II and prevents it from binding nonspecifically to DNA
    • Killeen, M. T., and J. F. Greenblatt. 1992. The general transcription factor RAP30 binds to RNA polymerase II and prevents it from binding nonspecifically to DNA. Mol. Cell. Biol. 12:30-37.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 30-37
    • Killeen, M.T.1    Greenblatt, J.F.2
  • 39
    • 0028282551 scopus 로고
    • A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II
    • Kim, Y. J., S. Bjorklund, Y. Li, M. Sayre, and R. Kornberg. 1994. A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II Cell 77:599-608.
    • (1994) Cell , vol.77 , pp. 599-608
    • Kim, Y.J.1    Bjorklund, S.2    Li, Y.3    Sayre, M.4    Kornberg, R.5
  • 40
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • Lai, J.-S., and W. Herr. 1992. Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc. Natl. Acad Sci. USA 89:6958-6962.
    • (1992) Proc. Natl. Acad Sci. USA , vol.89 , pp. 6958-6962
    • Lai, J.-S.1    Herr, W.2
  • 41
    • 0024295767 scopus 로고
    • The leucine binding zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz, W. H., P. F. Johnson, and S. L. McKnight. 1988. The leucine binding zipper: a hypothetical structure common to a new class of DNA binding proteins. Science 240:1759-1764.
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 42
    • 0025311439 scopus 로고
    • In vitro transcriptional activation, dimerization, and DNA-binding specificity of the Epstein-Barr virus Zta protein
    • Lieberman, P. M., and A. J. Berk. 1990. In vitro transcriptional activation, dimerization, and DNA-binding specificity of the Epstein-Barr virus Zta protein. J. Virol. 64:2560-2568.
    • (1990) J. Virol. , vol.64 , pp. 2560-2568
    • Lieberman, P.M.1    Berk, A.J.2
  • 43
    • 0026263755 scopus 로고
    • The Zta trans-activator protein stabilizes TFIID association with promoter DNA by direct protein-protein interaction
    • Lieberman, P. M., and A. J. Berk. 1991. The Zta trans-activator protein stabilizes TFIID association with promoter DNA by direct protein-protein interaction. Genes Dev. 5:2441-2454.
    • (1991) Genes Dev. , vol.5 , pp. 2441-2454
    • Lieberman, P.M.1    Berk, A.J.2
  • 44
    • 0028269517 scopus 로고
    • A mechanism for TAFs in transcriptional activation: Activation domain enhancement of TFIID-TFIIA-promoter DNA complex formation
    • Lieberman, P. M., and A. J. Berk. 1994 A mechanism for TAFs in transcriptional activation: activation domain enhancement of TFIID-TFIIA-promoter DNA complex formation. Genes Dev. 8:995-1006
    • (1994) Genes Dev. , vol.8 , pp. 995-1006
    • Lieberman, P.M.1    Berk, A.J.2
  • 45
    • 0026093414 scopus 로고
    • Mechanism of action of an acidic transcriptional activator in vitro
    • Lin, Y. S., and M. R. Green. 1991. Mechanism of action of an acidic transcriptional activator in vitro. Cell 64:971-981.
    • (1991) Cell , vol.64 , pp. 971-981
    • Lin, Y.S.1    Green, M.R.2
  • 46
    • 0025790439 scopus 로고
    • The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex
    • Lu, H., O. Flores, R. Weinmann, and D. Reinberg. 1991. The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex. Proc. Natl. Acad. Sci. USA 88:10004-10008.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10004-10008
    • Lu, H.1    Flores, O.2    Weinmann, R.3    Reinberg, D.4
  • 47
    • 0026731557 scopus 로고
    • Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II
    • Lu, H., L. Zawel, L. Fisher, J. M. Egly, and D. Reinberg. 1992. Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II. Nature (London) 358:641-645.
    • (1992) Nature (London) , vol.358 , pp. 641-645
    • Lu, H.1    Zawel, L.2    Fisher, L.3    Egly, J.M.4    Reinberg, D.5
  • 48
    • 0025217198 scopus 로고
    • Direct cloning of Ieucine zipper pioteins: Jun binds cooperatively to the CRE with CRE-BP1
    • Macgregor, P. F., C. Abate, and T. Curran. 1990 Direct cloning of Ieucine zipper pioteins: Jun binds cooperatively to the CRE with CRE-BP1. Oncogene 5:451-458.
    • (1990) Oncogene , vol.5 , pp. 451-458
    • Macgregor, P.F.1    Abate, C.2    Curran, T.3
  • 50
    • 0029038933 scopus 로고
    • News on initiation and elongation of transcription by RNA polymerase II
    • Maldonado, E., and D. Reinberg. 1995 News on initiation and elongation of transcription by RNA polymerase II. Curr. Opin. Cell Biol. 7:352-361.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 352-361
    • Maldonado, E.1    Reinberg, D.2
  • 51
    • 0028296106 scopus 로고
    • Transcription factor IIE binds preferentially to RNA polymerase IIa and recruits TFIIH: A model for promoter clearance
    • Maxon, M. E., J. A. Goodrich, and R. Tjian. 1994. Transcription factor IIE binds preferentially to RNA polymerase IIa and recruits TFIIH: a model for promoter clearance Genes Dev. 8:515-524.
    • (1994) Genes Dev. , vol.8 , pp. 515-524
    • Maxon, M.E.1    Goodrich, J.A.2    Tjian, R.3
  • 52
    • 0025834732 scopus 로고
    • Related RNA polymerase-binding regions in human RAP30/74 and Escherichia coli sigma 70
    • McCracken, S., and J. Greenblatt. 1991. Related RNA polymerase-binding regions in human RAP30/74 and Escherichia coli sigma 70. Science 253:900-902
    • (1991) Science , vol.253 , pp. 900-902
    • McCracken, S.1    Greenblatt, J.2
  • 54
    • 0027730042 scopus 로고
    • The bZIP motif of the Epstein-Barr virus (EBV) transcription factor EB1 mediates a direct interaction with TBP
    • Mikaelian, I., E. Manet, and A. Sergeant. 1993. The bZIP motif of the Epstein-Barr virus (EBV) transcription factor EB1 mediates a direct interaction with TBP. C. R. Acad. Sci. Ser. III 316:1424-1432.
    • (1993) C. R. Acad. Sci. Ser. III , vol.316 , pp. 1424-1432
    • Mikaelian, I.1    Manet, E.2    Sergeant, A.3
  • 55
    • 0023198109 scopus 로고
    • Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene
    • Montminy, M. R., and L. M. Bilezikjian. 1987. Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene Genes Dev. 328:175-178.
    • (1987) Genes Dev. , vol.328 , pp. 175-178
    • Montminy, M.R.1    Bilezikjian, L.M.2
  • 56
    • 0024206625 scopus 로고
    • Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element
    • Norman, C., M. Runswick, R. Pollock, and R. Treisman. 1988. Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element. Cell 55:989-1003.
    • (1988) Cell , vol.55 , pp. 989-1003
    • Norman, C.1    Runswick, M.2    Pollock, R.3    Treisman, R.4
  • 57
    • 0029163246 scopus 로고
    • Analysis of the role of TFIIE in basal transcription and TFIIH-mediated carboxy-terminal domain phosphorylation through structure-function studies of TFIIE-α
    • Ohkuma, Y., S. Hashimoto, C. K. Wang, M. Horikoshi, and R. G. Roeder. 1995. Analysis of the role of TFIIE in basal transcription and TFIIH-mediated carboxy-terminal domain phosphorylation through structure-function studies of TFIIE-α Mol. Cell. Biol 15:4856-4866
    • (1995) Mol. Cell. Biol , vol.15 , pp. 4856-4866
    • Ohkuma, Y.1    Hashimoto, S.2    Wang, C.K.3    Horikoshi, M.4    Roeder, R.G.5
  • 58
    • 0028293210 scopus 로고
    • Regulation of TFIIH ATPase and kinase activities by TFIIE during active initiation complex formation
    • Ohkuma, Y., and R. G. Roeder. 1994. Regulation of TFIIH ATPase and kinase activities by TFIIE during active initiation complex formation. Nature (London) 368:160-163.
    • (1994) Nature (London) , vol.368 , pp. 160-163
    • Ohkuma, Y.1    Roeder, R.G.2
  • 59
    • 0025633257 scopus 로고
    • Factors involved in specific transcription by mammalian RNA polymerase II: Purification and characterization of general transcription factor TFIIE
    • Ohkuma, Y., H. Sumimoto, M. Horikoshi, and R. G. Roeder. 1990 Factors involved in specific transcription by mammalian RNA polymerase II: purification and characterization of general transcription factor TFIIE Proc. Natl. Acad Sci. USA 87:9163-9167.
    • (1990) Proc. Natl. Acad Sci. USA , vol.87 , pp. 9163-9167
    • Ohkuma, Y.1    Sumimoto, H.2    Horikoshi, M.3    Roeder, R.G.4
  • 60
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zipper from Fos and Jun
    • O'Shea, E. K., R. Rutkowski, W. F. Stafford, and P. S. Kim. 1989 Preferential heterodimer formation by isolated leucine zipper from Fos and Jun Science 245:646-648
    • (1989) Science , vol.245 , pp. 646-648
    • O'Shea, E.K.1    Rutkowski, R.2    Stafford, W.F.3    Kim, P.S.4
  • 61
    • 0027984529 scopus 로고
    • Molecular cloning of the small (γ) sub-unit of human TFIIA reveals functions critical for activated transcription
    • Ozer, J., P. A. Moore, A. H. Bolden, A. Lee, C. A. Rosen, and P. Lieberman. 1994. Molecular cloning of the small (γ) sub-unit of human TFIIA reveals functions critical for activated transcription. Genes Dev. 8:2324-2335.
    • (1994) Genes Dev. , vol.8 , pp. 2324-2335
    • Ozer, J.1    Moore, P.A.2    Bolden, A.H.3    Lee, A.4    Rosen, C.A.5    Lieberman, P.6
  • 62
    • 0025017975 scopus 로고
    • Altered protein conformation on DNA binding by Fos and Jun
    • Patel, L., C. Abate, and T. Curran. 1990. Altered protein conformation on DNA binding by Fos and Jun. Nature (London) 347:572-575.
    • (1990) Nature (London) , vol.347 , pp. 572-575
    • Patel, L.1    Abate, C.2    Curran, T.3
  • 63
    • 0028364259 scopus 로고
    • Energy transfer analysis of Fos-Jun dimerization and DNA binding
    • Patel, L. R., T. Curran, and T. K. Kerppola. 1994. Energy transfer analysis of Fos-Jun dimerization and DNA binding. Proc. Natl. Acad. Sci USA 91:7360-7364.
    • (1994) Proc. Natl. Acad. Sci USA , vol.91 , pp. 7360-7364
    • Patel, L.R.1    Curran, T.2    Kerppola, T.K.3
  • 65
    • 0027351256 scopus 로고
    • The bZIP domains of Fos and Jun mediate a physical association with the TATA box-binding protein
    • Ransone, L. J., L. D. Kerr, M. J. Schmitt, P. Wamsley, and I. M. Verma. 1993. The bZIP domains of Fos and Jun mediate a physical association with the TATA box-binding protein. Gene Expr. 3:37-48.
    • (1993) Gene Expr. , vol.3 , pp. 37-48
    • Ransone, L.J.1    Kerr, L.D.2    Schmitt, M.J.3    Wamsley, P.4    Verma, I.M.5
  • 66
    • 0023739967 scopus 로고
    • A family of human CCAAT-box-binding proteins activate in transcription and DNA replication: Cloning and expression of multiple cDNAs
    • Santoro, C., N. Mermod, P. C. Andrews, and R. Tjian. 1988 A family of human CCAAT-box-binding proteins activate in transcription and DNA replication: cloning and expression of multiple cDNAs. Nature (London) 334:218-224.
    • (1988) Nature (London) , vol.334 , pp. 218-224
    • Santoro, C.1    Mermod, N.2    Andrews, P.C.3    Tjian, R.4
  • 67
    • 0028989623 scopus 로고
    • Control of transcription by Kruppel through interactions with TFIIB and TFIIEβ
    • Sauer, F., J. D. Fondell, Y. Ohkuma, R. G. Roeder, and H. Jackle. 1995. Control of transcription by Kruppel through interactions with TFIIB and TFIIEβ. Nature (London) 375:162-164.
    • (1995) Nature (London) , vol.375 , pp. 162-164
    • Sauer, F.1    Fondell, J.D.2    Ohkuma, Y.3    Roeder, R.G.4    Jackle, H.5
  • 68
    • 0024744568 scopus 로고
    • Mutations in the glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities
    • Schena, M., L. P. Freedman, and K. R. Yamamoto. 1989. Mutations in the glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities. Genes Dev. 3:1590-1601.
    • (1989) Genes Dev. , vol.3 , pp. 1590-1601
    • Schena, M.1    Freedman, L.P.2    Yamamoto, K.R.3
  • 69
    • 0024390631 scopus 로고
    • Sp1 activates transaction without enhancing DNA-binding activity of the TATA box factor
    • Schmidt, M. C., Q. Zhou, and A. J. Berk. 1989. Sp1 activates transaction without enhancing DNA-binding activity of the TATA box factor Mol Cell. Biol. 9:3299-3307.
    • (1989) Mol Cell. Biol. , vol.9 , pp. 3299-3307
    • Schmidt, M.C.1    Zhou, Q.2    Berk, A.J.3
  • 70
    • 0027992539 scopus 로고
    • An oligomeric form of the large subunit of transcription factor (TF) IIE activates phosphorylation of the RNA polymerase II carboxyl-terminal domain by TFIIH
    • Serizawa, H., J. W. Conaway, and R. C. Conaway. 1994 An oligomeric form of the large subunit of transcription factor (TF) IIE activates phosphorylation of the RNA polymerase II carboxyl-terminal domain by TFIIH J. Biol. Chem. 269:20750-20756
    • (1994) J. Biol. Chem. , vol.269 , pp. 20750-20756
    • Serizawa, H.1    Conaway, J.W.2    Conaway, R.C.3
  • 71
    • 0026571502 scopus 로고
    • A molecular mechanism for combinatorial control in yeast: MCM1 protein sets the spacing and orientation of the homeodomains of an alpha 2 dimer
    • Smith, D. L., and A. D. Johnson. 1992. A molecular mechanism for combinatorial control in yeast: MCM1 protein sets the spacing and orientation of the homeodomains of an alpha 2 dimer. Cell 68:133-142.
    • (1992) Cell , vol.68 , pp. 133-142
    • Smith, D.L.1    Johnson, A.D.2
  • 72
    • 0026737773 scopus 로고
    • Conserved motifs in Fos and Jun define a new class of activation domain
    • Sutherland, J. A., A. Cook, A. J. Bannister, and T. Kouzarides. 1992 Conserved motifs in Fos and Jun define a new class of activation domain. Genes Dev. 6:1810-1819.
    • (1992) Genes Dev. , vol.6 , pp. 1810-1819
    • Sutherland, J.A.1    Cook, A.2    Bannister, A.J.3    Kouzarides, T.4
  • 73
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few pieces
    • Tjian, R., and T. Maniatis. 1994. Transcriptional activation: a complex puzzle with few pieces. Cell 77:5-8.
    • (1994) Cell , vol.77 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 74
    • 0028897411 scopus 로고
    • The 62- and SlUkDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protean 2
    • Tong, X., R. Drapkin, D. Reinberg, and E. Kieff. 1995. The 62- and SlUkDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protean 2. Proc. Natl. Acad. Sci. USA 92:3259-3263.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3259-3263
    • Tong, X.1    Drapkin, R.2    Reinberg, D.3    Kieff, E.4
  • 75
    • 0026646156 scopus 로고
    • HAP1 positive control mutants specific for one of two binding sites
    • Turcotte, B., and L. Guarente. 1992. HAP1 positive control mutants specific for one of two binding sites. Genes Dev. 6:2001-2009.
    • (1992) Genes Dev. , vol.6 , pp. 2001-2009
    • Turcotte, B.1    Guarente, L.2
  • 76
    • 0027168947 scopus 로고
    • Identification of a minimal set of proteins that is sufficient for accurate initiation of transcription by RNA polymerase II
    • Tyree, C. M., C. P. George, L. M. Lira-DeVito, S. L. Wampler, M. E. Dahmus, L. Zawel, and J. T. Kadonaga. 1993. Identification of a minimal set of proteins that is sufficient for accurate initiation of transcription by RNA polymerase II. Genes Dev. 7:1254-1265.
    • (1993) Genes Dev. , vol.7 , pp. 1254-1265
    • Tyree, C.M.1    George, C.P.2    Lira-DeVito, L.M.3    Wampler, S.L.4    Dahmus, M.E.5    Zawel, L.6    Kadonaga, J.T.7
  • 77
    • 0026561087 scopus 로고
    • Inhibition of Fos- and Ras-induced transformation by mutant Fos proteins with structural alterations in functionally different domains
    • Wick, M., F. C. Lucibello, and R. Muller. 1992. Inhibition of Fos- and Ras-induced transformation by mutant Fos proteins with structural alterations in functionally different domains Oncogene 7:859-867.
    • (1992) Oncogene , vol.7 , pp. 859-867
    • Wick, M.1    Lucibello, F.C.2    Muller, R.3
  • 79
    • 0028236808 scopus 로고
    • Transcriptional elongation by RNA polymerase II is stimulated by transactivators
    • Yankulov, K., J. Blau, T. Purton, S. Roberts, and D. L. Bentley. 1994. Transcriptional elongation by RNA polymerase II is stimulated by transactivators Cell 77:749-759.
    • (1994) Cell , vol.77 , pp. 749-759
    • Yankulov, K.1    Blau, J.2    Purton, T.3    Roberts, S.4    Bentley, D.L.5
  • 80
    • 0029042392 scopus 로고
    • Common themes in assembly and function of eukaryotic transcription complexes
    • Zawel, L., and D. Reinberg. 1995 Common themes in assembly and function of eukaryotic transcription complexes Annu. Rev. Biochem. 64:533-561.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 533-561
    • Zawel, L.1    Reinberg, D.2


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