메뉴 건너뛰기




Volumn 18, Issue 10, 1998, Pages 5818-5827

Requirements for chromatin modulation and transcription activation by the Pho4 acidic activation domain

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE;

EID: 0031655430     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.10.5818     Document Type: Article
Times cited : (40)

References (45)
  • 1
    • 0022799341 scopus 로고
    • Nuclease hypersensitive regions with adjacent positioned nucleosomes mark the gene boundaries of the PHO5/PHO3 locus in yeast
    • Almer, A., and W. Hörz. 1986. Nuclease hypersensitive regions with adjacent positioned nucleosomes mark the gene boundaries of the PHO5/PHO3 locus in yeast. EMBO J. 5:2681-2687.
    • (1986) EMBO J. , vol.5 , pp. 2681-2687
    • Almer, A.1    Hörz, W.2
  • 2
    • 0022799080 scopus 로고
    • Removal of positioned nucleosomes from the yeast PHO5 promoter upon PHO5 induction releases additional upstream activating DNA elements
    • Almer, A., H. Rudolph, A. Hinnen, and W. Hörz. 1986. Removal of positioned nucleosomes from the yeast PHO5 promoter upon PHO5 induction releases additional upstream activating DNA elements. EMBO J. 5:2689-2696.
    • (1986) EMBO J. , vol.5 , pp. 2689-2696
    • Almer, A.1    Rudolph, H.2    Hinnen, A.3    Hörz, W.4
  • 3
    • 0025370208 scopus 로고
    • Isolation of the gene encoding the Saccharomyces cerevisiae centromere-binding protein CP1
    • Baker, R. E., and D. C. Masison. 1990. Isolation of the gene encoding the Saccharomyces cerevisiae centromere-binding protein CP1. Mol. Cell. Biol. 10:2458-2467.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2458-2467
    • Baker, R.E.1    Masison, D.C.2
  • 4
    • 0029957248 scopus 로고    scopus 로고
    • The homeodomain protein Pho2 and the basic-helix-loop-helix protein Pho4 bind DNA cooperatively at the yeast PHO5 promoter
    • Barbaric, S., M. Münsterkötter, J. Svaren, and W. Hörz. 1996. The homeodomain protein Pho2 and the basic-helix-loop-helix protein Pho4 bind DNA cooperatively at the yeast PHO5 promoter. Nucleic Acids Res. 24:4479-4486.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4479-4486
    • Barbaric, S.1    Münsterkötter, M.2    Svaren, J.3    Hörz, W.4
  • 5
    • 2642607009 scopus 로고    scopus 로고
    • Cooperative Pho2-Pho4 interactions at the PHO5 promoter facilitate Pho4 binding to UASp1 and enhance transactivation by Pho4 at UASp2
    • Barbaric, S., M. Münsterkötter, C. Goding, and W. Hörz. 1998. Cooperative Pho2-Pho4 interactions at the PHO5 promoter facilitate Pho4 binding to UASp1 and enhance transactivation by Pho4 at UASp2. Mol. Cell. Biol. 18:2629-2639.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2629-2639
    • Barbaric, S.1    Münsterkötter, M.2    Goding, C.3    Hörz, W.4
  • 6
    • 0025283868 scopus 로고
    • Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy
    • Cai, M., and R. W. Davis. 1990. Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy. Cell 61:437-446.
    • (1990) Cell , vol.61 , pp. 437-446
    • Cai, M.1    Davis, R.W.2
  • 7
    • 0028812627 scopus 로고
    • Trans-activation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein
    • Chang, J., D. H. Kim, S. W. Lee, K. Y. Choi, and Y. C. Sung. 1995. Trans-activation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein. J. Biol. Chem. 270:25014-25019.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25014-25019
    • Chang, J.1    Kim, D.H.2    Lee, S.W.3    Choi, K.Y.4    Sung, Y.C.5
  • 8
    • 0023711642 scopus 로고
    • Alpha-helix in the carboxy-terminal domains of histones H1 and H5
    • Clark, D. J., C. S. Hill, S. R. Martin, and J. O. Thomas. 1988. Alpha-helix in the carboxy-terminal domains of histones H1 and H5. EMBO J. 7:69-75.
    • (1988) EMBO J. , vol.7 , pp. 69-75
    • Clark, D.J.1    Hill, C.S.2    Martin, S.R.3    Thomas, J.O.4
  • 9
    • 0026086914 scopus 로고
    • Critical structural elements of the VP16 transcriptional activation domain
    • Cress, W. D., and S. J. Triezenberg. 1991. Critical structural elements of the VP16 transcriptional activation domain. Science 251:87-90.
    • (1991) Science , vol.251 , pp. 87-90
    • Cress, W.D.1    Triezenberg, S.J.2
  • 10
    • 0019497821 scopus 로고
    • Design, synthesis and characterization of a cytotoxic peptide with melittin-like activity
    • Degrado, W. F., F. J. Kedzy, and E. T. Kaiser. 1981. Design, synthesis and characterization of a cytotoxic peptide with melittin-like activity. J. Am. Chem. Soc. 103:679-681.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 679-681
    • Degrado, W.F.1    Kedzy, F.J.2    Kaiser, E.T.3
  • 11
    • 0026540830 scopus 로고
    • Purification and characterization of the carboxy terminal transactivation domain of Vmw65 from herpes simplex virus
    • Donaldson, L., and J. P. Capone. 1992. Purification and characterization of the carboxy terminal transactivation domain of Vmw65 from herpes simplex virus. J. Biol. Chem. 267:1411-1414.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1411-1414
    • Donaldson, L.1    Capone, J.P.2
  • 12
    • 0028840090 scopus 로고
    • The transcriptional activator GCN4 contains multiple activation domains that are critically dependent on hydrophobic amino acids
    • Drysdale, C. M., E. Duenas, B. M. Jackson, U. Ruesser, G. H. Braus, and A. G. Hinnebusch. 1995. The transcriptional activator GCN4 contains multiple activation domains that are critically dependent on hydrophobic amino acids. Mol. Cell. Biol. 15:1220-1233.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1220-1233
    • Drysdale, C.M.1    Duenas, E.2    Jackson, B.M.3    Ruesser, U.4    Braus, G.H.5    Hinnebusch, A.G.6
  • 13
    • 0025291085 scopus 로고
    • Role of trans-activating proteins in the generation of active chromatin at the PHO5 promoter in 5. cerevisiae
    • Fascher, K. D., J. Schmitz, and W. Hörz. 1990. Role of trans-activating proteins in the generation of active chromatin at the PHO5 promoter in 5. cerevisiae. EMBO J. 9:2523-2528.
    • (1990) EMBO J. , vol.9 , pp. 2523-2528
    • Fascher, K.D.1    Schmitz, J.2    Hörz, W.3
  • 14
    • 0027295561 scopus 로고
    • Structural and functional requirements for the chromatin transition at the PHO5 promoter in Saccharomyces cerevisiae upon PHO5 activation
    • Fascher, K. D., J. Schmitz, and W. Hörz. 1993. Structural and functional requirements for the chromatin transition at the PHO5 promoter in Saccharomyces cerevisiae upon PHO5 activation. J. Mol. Biol. 231:658-667.
    • (1993) J. Mol. Biol. , vol.231 , pp. 658-667
    • Fascher, K.D.1    Schmitz, J.2    Hörz, W.3
  • 15
    • 0025830886 scopus 로고
    • C-myc and the yeast transcription factor PHO4 share a common CACGTG-binding motif
    • Fisher, F., P. S. Jayaraman, and C. R. Goding. 1991. C-myc and the yeast transcription factor PHO4 share a common CACGTG-binding motif. Oncogene 6:1099-1104.
    • (1991) Oncogene , vol.6 , pp. 1099-1104
    • Fisher, F.1    Jayaraman, P.S.2    Goding, C.R.3
  • 16
    • 0030935280 scopus 로고    scopus 로고
    • RNA polymerase holoenzyme recruitment is sufficient to remodel chromatin at the yeast PHO5 promoter
    • Gaudreau, L., A. Schmid, D. Blaschke, M. Ptashne, and W. Hörz. 1997. RNA polymerase holoenzyme recruitment is sufficient to remodel chromatin at the yeast PHO5 promoter. Cell 89:55-62.
    • (1997) Cell , vol.89 , pp. 55-62
    • Gaudreau, L.1    Schmid, A.2    Blaschke, D.3    Ptashne, M.4    Hörz, W.5
  • 17
    • 0023500809 scopus 로고
    • Transcription in yeast activated by a putative amphipathic alpha helix linked to a DNA binding unit
    • Giniger, E., and M. Ptashne. 1987. Transcription in yeast activated by a putative amphipathic alpha helix linked to a DNA binding unit. Nature 330:670-672.
    • (1987) Nature , vol.330 , pp. 670-672
    • Giniger, E.1    Ptashne, M.2
  • 18
    • 0028027464 scopus 로고
    • The transcription factor, the Cdk, its cyclin and their regulator:directing the transcriptional response to a nutritional signal
    • Hirst, K., F. Fisher, P. C. McAndrew, and C. R. Goding. 1994. The transcription factor, the Cdk, its cyclin and their regulator:directing the transcriptional response to a nutritional signal. EMBO J. 13:5410-5420.
    • (1994) EMBO J. , vol.13 , pp. 5410-5420
    • Hirst, K.1    Fisher, F.2    McAndrew, P.C.3    Goding, C.R.4
  • 19
    • 0032574795 scopus 로고    scopus 로고
    • Transcriptional activator-cofactor recognition:nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding
    • Hua, X.-Q., W.-H. Jia, B. P. Bullock, J. F. Habener, and M. A. Weiss. 1998. Transcriptional activator-cofactor recognition:nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding. Biochemistry 37:5858-5866.
    • (1998) Biochemistry , vol.37 , pp. 5858-5866
    • Hua, X.-Q.1    Jia, W.-H.2    Bullock, B.P.3    Habener, J.F.4    Weiss, M.A.5
  • 20
    • 0029791550 scopus 로고    scopus 로고
    • Identification of seven hydrophobic clusters in GCN4 making redundant contributions to transcriptional activation
    • Jackson, B. M., C. M. Drysdale, K. Natarajan, and A. G. Hinnebusch. 1996. Identification of seven hydrophobic clusters in GCN4 making redundant contributions to transcriptional activation. Mol. Cell. Biol. 16:5557-5571.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5557-5571
    • Jackson, B.M.1    Drysdale, C.M.2    Natarajan, K.3    Hinnebusch, A.G.4
  • 21
    • 0028174643 scopus 로고
    • Quantitation of helical propensities from trifluoroethanol titration curves
    • Jasanoff, A., and A. R. Fersht. 1994. Quantitation of helical propensities from trifluoroethanol titration curves. Biochemistry 33:2129-2135.
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 22
    • 0028351946 scopus 로고
    • The activation domain of a basic helix-loop-helix protein is masked by repressor interaction with domains distinct from that required for transcription regulation
    • Javaraman, P. S., K. Hirst, and C. R. Goding. 1994. The activation domain of a basic helix-loop-helix protein is masked by repressor interaction with domains distinct from that required for transcription regulation. EMBO J. 13:2192-2199.
    • (1994) EMBO J. , vol.13 , pp. 2192-2199
    • Javaraman, P.S.1    Hirst, K.2    Goding, C.R.3
  • 23
    • 0028207513 scopus 로고
    • Phosphorylation tion of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85
    • Kaffman, A., I. Herskowitz, R. Tjian, and E. K. O'Shea. 1994. Phosphorylation tion of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85. Science 263:1153-1156.
    • (1994) Science , vol.263 , pp. 1153-1156
    • Kaffman, A.1    Herskowitz, I.2    Tjian, R.3    O'Shea, E.K.4
  • 24
  • 26
    • 0027394585 scopus 로고
    • Genetic evidence that an activation domain of GAL4 does not require acidity and may form a beta-sheet
    • Leuther, K. K., J. M. Salmeron, and S. A. Johnston. 1993. Genetic evidence that an activation domain of GAL4 does not require acidity and may form a beta-sheet. Cell 72:575-585.
    • (1993) Cell , vol.72 , pp. 575-585
    • Leuther, K.K.1    Salmeron, J.M.2    Johnston, S.A.3
  • 27
    • 0028303752 scopus 로고
    • Several Hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein
    • Lin, J., J. Chen, B. Elenbaas, and A. J. Levine. 1994. Several Hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein. Genes Dev. 8:1235-1246.
    • (1994) Genes Dev. , vol.8 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3    Levine, A.J.4
  • 28
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol:a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Luo, P., and R. L. Baldwin. 1997. Mechanism of helix induction by trifluoroethanol:a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36:8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 29
    • 0023649184 scopus 로고
    • A new class of yeast transcriptional activators
    • Ma, J., and M. Ptashne. 1987. A new class of yeast transcriptional activators. Cell 51:113-119.
    • (1987) Cell , vol.51 , pp. 113-119
    • Ma, J.1    Ptashne, M.2
  • 31
    • 0025354922 scopus 로고
    • Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae
    • Ogawa, N., and Y. Oshima. 1990. Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:2224-2236.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2224-2236
    • Ogawa, N.1    Oshima, Y.2
  • 33
    • 0030059223 scopus 로고    scopus 로고
    • Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex
    • O'Neill, E. M., A. Kaffman, E. R. Jolly, and E. K. O'Shea. 1996. Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex. Science 271:209-212.
    • (1996) Science , vol.271 , pp. 209-212
    • O'Neill, E.M.1    Kaffman, A.2    Jolly, E.R.3    O'Shea, E.K.4
  • 34
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB:a model for activator:coactivator interactions
    • Radhakrishnan, I., G. C. Perez-Alvarado, D. Parker, H. J. Dyson, M. R. Montminy, and P. E. Wright. 1997. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB:a model for activator:coactivator interactions. Cell 91:741-752.
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Perez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 35
    • 0027402497 scopus 로고
    • Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator
    • Regier, J. L., F. Shen, and S. J. Triezenberg. 1993. Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator. Proc. Natl. Acad. Sci. USA 90:883-887.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 883-887
    • Regier, J.L.1    Shen, F.2    Triezenberg, S.J.3
  • 36
    • 0026465372 scopus 로고
    • Nucleosome disruption at the yeast PHO5 promoter upon PHO5 induction occurs in the absence of DNA replication
    • Schmid, A., K. D. Fascher, and W. Hörz. 1992. Nucleosome disruption at the yeast PHO5 promoter upon PHO5 induction occurs in the absence of DNA replication. Cell 71:853-864.
    • (1992) Cell , vol.71 , pp. 853-864
    • Schmid, A.1    Fascher, K.D.2    Hörz, W.3
  • 37
    • 0029948550 scopus 로고    scopus 로고
    • Interaction of Saccharomyces cerevisiae Pho2 with Pho4 increases the accessibility of the activation domain
    • Shao, D., C. L. Creasy, and L. W. Bergman. 1996. Interaction of Saccharomyces cerevisiae Pho2 with Pho4 increases the accessibility of the activation domain. Mol. Gen. Genet. 251:358-364.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 358-364
    • Shao, D.1    Creasy, C.L.2    Bergman, L.W.3
  • 38
    • 0027948986 scopus 로고
    • The transactivation domain of Pho4 is required for nucleosome disruption at the PHO5 promoter
    • Svaren, J., J, Schmitz, and W. Hörz. 1994. The transactivation domain of Pho4 is required for nucleosome disruption at the PHO5 promoter. EMBO J. 13:4856-4862.
    • (1994) EMBO J. , vol.13 , pp. 4856-4862
    • Svaren, J.1    Schmitz, J.2    Hörz, W.3
  • 39
    • 0000270283 scopus 로고
    • In vivo analysis of nucleosome structure and transcription factor binding in S. cerevisiae
    • Svaren, J., U. Venter, and W. Hörz. 1995. In vivo analysis of nucleosome structure and transcription factor binding in S. cerevisiae. Methods Mol. Genet. 6:153-167.
    • (1995) Methods Mol. Genet. , vol.6 , pp. 153-167
    • Svaren, J.1    Venter, U.2    Hörz, W.3
  • 40
    • 0029976446 scopus 로고    scopus 로고
    • Modulation of promoter occupancy by cooperative DNA/ binding and activation-domain function is a major determinant of transcriptional regulation by activators in vivo
    • Tanaka, M. 1996. Modulation of promoter occupancy by cooperative DNA/ binding and activation-domain function is a major determinant of transcriptional regulation by activators in vivo. Proc. Natl. Acad. Sci. USA 93:4311-4315.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4311-4315
    • Tanaka, M.1
  • 41
    • 0030756675 scopus 로고    scopus 로고
    • Induced alpha helix in the VP16 activation domain upon binding to a human TAF
    • Uesugi, M., O. Nyanguile, H. Lu, A. J. Levine, and G. L. Verdine. 1997. Induced alpha helix in the VP16 activation domain upon binding to a human TAF. Science 277:1310-1313.
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 42
    • 0027522642 scopus 로고
    • The acidic activation domains of the GCN4 and GAL4 proteins are not alpha-helical but form beta sheets
    • Van Hoy, M., K. K. Leuther, T. Kodadek, and S. A. Johnston. 1993. The acidic activation domains of the GCN4 and GAL4 proteins are not alpha-helical but form beta sheets. Cell 72:587-594.
    • (1993) Cell , vol.72 , pp. 587-594
    • Van Hoy, M.1    Leuther, K.K.2    Kodadek, T.3    Johnston, S.A.4
  • 43
    • 0028856072 scopus 로고
    • The activation domain of GAL4 protein mediates cooperative promoter binding with general transcription factors in vivo
    • Vashee, S., and T. Kodadek. 1995. The activation domain of GAL4 protein mediates cooperative promoter binding with general transcription factors in vivo. Proc. Natl. Acad. Sci. USA 92:10683-10687.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10683-10687
    • Vashee, S.1    Kodadek, T.2
  • 44
    • 0027943272 scopus 로고
    • A nucleosome precludes binding of the transcription factor Pho4 in vivo to a critical target site in the PHO5 promoter
    • Venter, U., J. Svaren, J. Schmitz, A. Schmitz, and W. Hörz. 1994. A nucleosome precludes binding of the transcription factor Pho4 in vivo to a critical target site in the PHO5 promoter. EMBO J. 13:4848-4855.
    • (1994) EMBO J. , vol.13 , pp. 4848-4855
    • Venter, U.1    Svaren, J.2    Schmitz, J.3    Schmitz, A.4    Hörz, W.5
  • 45
    • 0029739903 scopus 로고    scopus 로고
    • Quantitation of putative activator-target affinities predicts transcriptional activating potentials
    • Wu, R., R. J. Reece, and M. Ptashne. 1996. Quantitation of putative activator-target affinities predicts transcriptional activating potentials. EMBO J. 15:3951-3963.
    • (1996) EMBO J. , vol.15 , pp. 3951-3963
    • Wu, R.1    Reece, R.J.2    Ptashne, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.