메뉴 건너뛰기




Volumn 324, Issue 3, 2002, Pages 501-517

Asymmetric binding of histone H1 stabilizes MMTV nucleosomes and the interaction of progesterone receptor with the exposed HRE

Author keywords

Chromatin structure; Chromatosomes; Linker histones; Nuclear receptors

Indexed keywords

DNA; FORMALDEHYDE; HISTONE H1; NUCLEASE; PROGESTERONE RECEPTOR; RECOMBINANT PROTEIN; VIRUS NUCLEOPROTEIN;

EID: 18744399544     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01101-4     Document Type: Article
Times cited : (16)

References (68)
  • 2
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. (1997). Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature, 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R. K., Clarkson, M. J., Tremethick, D. J. & Luger, K. (2000). Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nature Struct. Biol. 7, 1121-1124.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 4
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J. T., Graziano, V., Lee, P. L. & Sweet, R. M. (1993). Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature, 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 5
    • 0028314834 scopus 로고
    • Histone H1 is located in the interior of the chromatin 30-nm filament
    • Graziano, V., Gerchman, S. E., Schneider, D. K. & Ramakrishnan, V. (1994). Histone H1 is located in the interior of the chromatin 30-nm filament. Nature, 368, 351-354.
    • (1994) Nature , vol.368 , pp. 351-354
    • Graziano, V.1    Gerchman, S.E.2    Schneider, D.K.3    Ramakrishnan, V.4
  • 6
    • 0032972980 scopus 로고    scopus 로고
    • The location of the linker histone on the nucleosome
    • Travers, A. (1999). The location of the linker histone on the nucleosome. Trends Biochem. Sci. 24, 4-7.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 4-7
    • Travers, A.1
  • 7
    • 0029151148 scopus 로고
    • DNA at the entry-exit of the nucleosome observed by cryoelectron microscopy
    • Furrer, P., Bednar, J., Dubochet, J., Hamiche, A. & Prunell, A. (1995). DNA at the entry-exit of the nucleosome observed by cryoelectron microscopy. J. Struct. Biol. 114, 177-183.
    • (1995) J. Struct. Biol. , vol.114 , pp. 177-183
    • Furrer, P.1    Bednar, J.2    Dubochet, J.3    Hamiche, A.4    Prunell, A.5
  • 9
    • 0028031310 scopus 로고
    • Contacts of the globular domain of histone H5 and core histones with DNA in a "chromatosome"
    • Hayes, J. J., Pruss, D. & Wolffe, A. P. (1994). Contacts of the globular domain of histone H5 and core histones with DNA in a "chromatosome". Proc. Natl Acad. Sci. USA, 91, 7817-7821.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7817-7821
    • Hayes, J.J.1    Pruss, D.2    Wolffe, A.P.3
  • 10
    • 0027999696 scopus 로고
    • Evidence indicating proximity in the nucleosome between the histone H4 N-termini and the globular domain of histone H1
    • Banerés, J. L., Essalouh, L., Jariel-Encontre, I., Mesnier, D., Garrod, S. & Parello, J. (1994). Evidence indicating proximity in the nucleosome between the histone H4 N-termini and the globular domain of histone H1. J. Mol. Biol. 243, 48-59.
    • (1994) J. Mol. Biol. , vol.243 , pp. 48-59
    • Banerés, J.L.1    Essalouh, L.2    Jariel-Encontre, I.3    Mesnier, D.4    Garrod, S.5    Parello, J.6
  • 11
    • 0018866555 scopus 로고
    • Points of contact between histone H1 and the histone octamer
    • Boulikas, T., Wiseman, J. M. & Garrard, W. T. (1980). Points of contact between histone H1 and the histone octamer. Proc. Natl Acad. Sci. USA, 77, 127-131.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 127-131
    • Boulikas, T.1    Wiseman, J.M.2    Garrard, W.T.3
  • 12
    • 0028053165 scopus 로고
    • DNA sequence organization in chromatosomes
    • Muyldermans, S. & Travers, A. A. (1994). DNA sequence organization in chromatosomes. J. Mol. Biol. 235, 855-870.
    • (1994) J. Mol. Biol. , vol.235 , pp. 855-870
    • Muyldermans, S.1    Travers, A.A.2
  • 13
    • 0029680555 scopus 로고    scopus 로고
    • The linker histones and chromatin structure: New twists
    • Zlatanova, J. & van Holde, K. (1996). The linker histones and chromatin structure: New twists. Prog. Nucl. Acid Res. Mol. Biol. 52, 217-259.
    • (1996) Prog. Nucl. Acid Res. Mol. Biol. , vol.52 , pp. 217-259
    • Zlatanova, J.1    Van Holde, K.2
  • 14
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin core particle containing 160 base pairs of DNA and all the histones
    • Simpson, R. T. (1978). Structure of the chromatosome, a chromatin core particle containing 160 base pairs of DNA and all the histones. Biochemistry, 17, 5524-5531.
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 15
    • 0019157001 scopus 로고
    • The structure of histone H1 and its location in chromatin
    • Allan, J., Hartman, P. G., Crane-Robinson, C. & Aviles, F. X. (1980). The structure of histone H1 and its location in chromatin. Nature, 288, 675-679.
    • (1980) Nature , vol.288 , pp. 675-679
    • Allan, J.1    Hartman, P.G.2    Crane-Robinson, C.3    Aviles, F.X.4
  • 16
    • 0024195819 scopus 로고
    • Footprinting of linker histones H5 and H1 on the nucleosome
    • Staynov, D. Z. & Crane-Robinson, C. (1988). Footprinting of linker histones H5 and H1 on the nucleosome. EMBO J. 7, 3685-3691.
    • (1988) EMBO J. , vol.7 , pp. 3685-3691
    • Staynov, D.Z.1    Crane-Robinson, C.2
  • 17
    • 0024375866 scopus 로고
    • Binding of the globular domain of linker histones H5/H1 to the nucleosome: A hypothesis
    • Crane-Robinson, C. & Ptitsyn, O. B. (1989). Binding of the globular domain of linker histones H5/H1 to the nucleosome: A hypothesis. Protein Eng. 2, 577-582.
    • (1989) Protein Eng. , vol.2 , pp. 577-582
    • Crane-Robinson, C.1    Ptitsyn, O.B.2
  • 18
    • 0031106457 scopus 로고    scopus 로고
    • Where is the globular domain of linker histone located on the nucleosome?
    • Crane-Robinson, C. (1997). Where is the globular domain of linker histone located on the nucleosome? Trends. Biochem. Sci. 22, 75-77.
    • (1997) Trends. Biochem. Sci. , vol.22 , pp. 75-77
    • Crane-Robinson, C.1
  • 19
    • 0032584136 scopus 로고    scopus 로고
    • Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner
    • An, W. J., Leuba, S. H., van Holde, K. & Zlatanova, J. (1998). Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner. Proc. Natl Acad. Sci. USA, 95, 3396-3401.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3396-3401
    • An, W.J.1    Leuba, S.H.2    Van Holde, K.3    Zlatanova, J.4
  • 20
    • 0032563864 scopus 로고    scopus 로고
    • Position and orientation of the globular domain of linker histone H5 on the nucleosome
    • Zhou, Y. B., Gerchman, S. E., Ramakrishnan, V., Travers, A. & Muyldermans, S. (1998). Position and orientation of the globular domain of linker histone H5 on the nucleosome. Nature, 395, 402-405.
    • (1998) Nature , vol.395 , pp. 402-405
    • Zhou, Y.B.1    Gerchman, S.E.2    Ramakrishnan, V.3    Travers, A.4    Muyldermans, S.5
  • 21
    • 0030009322 scopus 로고    scopus 로고
    • A DNA sequence for positioning chromatosomes
    • Travers, A. A. & Muyldermans, S. V. (1996). A DNA sequence for positioning chromatosomes. J. Mol. Biol. 257, 486-491.
    • (1996) J. Mol. Biol. , vol.257 , pp. 486-491
    • Travers, A.A.1    Muyldermans, S.V.2
  • 22
    • 0027248504 scopus 로고
    • Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome
    • Hayes, J. J. & Wolffe, A. P. (1993). Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome. Proc. Natl Acad. Sci. USA, 90, 6415-6419.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6415-6419
    • Hayes, J.J.1    Wolffe, A.P.2
  • 23
    • 0029805762 scopus 로고    scopus 로고
    • An asymmetric model for the nucleosome: A binding site for linker histones inside the DNA gyres
    • Pruss, D., Bartholomew, B., Persinger, J., Hayes, J., Arents, G., Moudrianakis, E. N. & Wolffe, A. P. (1996). An asymmetric model for the nucleosome: A binding site for linker histones inside the DNA gyres. Science, 274, 614-617.
    • (1996) Science , vol.274 , pp. 614-617
    • Pruss, D.1    Bartholomew, B.2    Persinger, J.3    Hayes, J.4    Arents, G.5    Moudrianakis, E.N.6    Wolffe, A.P.7
  • 24
    • 0032537558 scopus 로고    scopus 로고
    • Asymmetric linker histone association directs the asymmetric rearrangement of core histone interactions in a positioned nucleosome containing a thyroid hormone response element
    • Guschin, D., Chandler, S. & Wolffe, A. P. (1998). Asymmetric linker histone association directs the asymmetric rearrangement of core histone interactions in a positioned nucleosome containing a thyroid hormone response element. Biochemistry, 37, 8629-8636.
    • (1998) Biochemistry , vol.37 , pp. 8629-8636
    • Guschin, D.1    Chandler, S.2    Wolffe, A.P.3
  • 25
    • 0011863936 scopus 로고    scopus 로고
    • How do nuclear processes occur in chromatin
    • Academic Press, London
    • Wolffe, A. (1998). How do nuclear processes occur in chromatin. Chromatin: Structure and Function, Academic Press, London pp. 240-341.
    • (1998) Chromatin: Structure and Function , pp. 240-341
    • Wolffe, A.1
  • 26
    • 0025081555 scopus 로고
    • Chromatin structure of transcriptionally competent and repressed genes
    • Kamakaka, R. T. & Thomas, J. O. (1990). Chromatin structure of transcriptionally competent and repressed genes. EMBO J. 9, 3997-4006.
    • (1990) EMBO J. , vol.9 , pp. 3997-4006
    • Kamakaka, R.T.1    Thomas, J.O.2
  • 27
    • 0025978212 scopus 로고
    • Formaldehyde cross-linking and immunoprecipitation demonstrate developmental changes in H1 association with transcriptionally active genes
    • Dedon, P. C., Soults, J. A., Allis, C. D. & Gorovsky, M. A. (1991). Formaldehyde cross-linking and immunoprecipitation demonstrate developmental changes in H1 association with transcriptionally active genes. Mol. Cell. Biol. 11, 1729-1733.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1729-1733
    • Dedon, P.C.1    Soults, J.A.2    Allis, C.D.3    Gorovsky, M.A.4
  • 28
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen, X. T., Yu, L. L., Weir, J. W. & Gorovsky, M. A. (1995). Linker histones are not essential and affect chromatin condensation in vivo. Cell, 82, 47-56.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.T.1    Yu, L.L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 29
    • 0030576509 scopus 로고    scopus 로고
    • Linker histone H1 regulates specific gene expression but not global transcription in vivo
    • Shen, X. T. & Gorovsky, M. A. (1996). Linker histone H1 regulates specific gene expression but not global transcription in vivo. Cell, 86, 475-483.
    • (1996) Cell , vol.86 , pp. 475-483
    • Shen, X.T.1    Gorovsky, M.A.2
  • 31
    • 0031835433 scopus 로고    scopus 로고
    • Role of histone H1 as an architectural determinant of chromatin structure and as a specific repressor of transcription on Xenopus oocyte 5S rRNA genes
    • Sera, T. & Wolffe, A. P. (1998). Role of histone H1 as an architectural determinant of chromatin structure and as a specific repressor of transcription on Xenopus oocyte 5S rRNA genes. Mol. Cell. Biol. 18, 3668-3680.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3668-3680
    • Sera, T.1    Wolffe, A.P.2
  • 32
    • 0028230983 scopus 로고
    • RNA polymerase II cofactor PC2 facilitates activation of transcription by GAL4-AH in vitro
    • Kretzschmar, M., Stelzer, G., Roeder, R. G. & Meisterernst, M. (1994). RNA polymerase II cofactor PC2 facilitates activation of transcription by GAL4-AH in vitro. Mol. Cell. Biol. 14, 3927-3937.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3927-3937
    • Kretzschmar, M.1    Stelzer, G.2    Roeder, R.G.3    Meisterernst, M.4
  • 33
    • 0033566728 scopus 로고    scopus 로고
    • Overproduction of histone H1 variants in vivo increases basal and induced activity of the mouse mammary tumor virus promoter
    • Gunjan, A. & Brown, D. T. (1999). Overproduction of histone H1 variants in vivo increases basal and induced activity of the mouse mammary tumor virus promoter. Nucl. Acids Res. 27, 3355-3363.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 3355-3363
    • Gunjan, A.1    Brown, D.T.2
  • 35
    • 0032525164 scopus 로고    scopus 로고
    • The MMTV promoter positioned on a tetramer of histones H3 and H4 binds nuclear factor 1 and OTF1
    • Spangenberg, C., Eisfeld, K., Stünkel, W., Luger, K., Flaus, A., Richmond, T. J. et al. (1998). The MMTV promoter positioned on a tetramer of histones H3 and H4 binds nuclear factor 1 and OTF1. J. Mol. Biol. 278, 725-739.
    • (1998) J. Mol. Biol. , vol.278 , pp. 725-739
    • Spangenberg, C.1    Eisfeld, K.2    Stünkel, W.3    Luger, K.4    Flaus, A.5    Richmond, T.J.6
  • 36
    • 0034680588 scopus 로고    scopus 로고
    • Two DNA-binding sites on the globular domain of histone H5 are required for binding to both bulk and 5 S reconstituted nucleosomes
    • Duggan, M. M. & Thomas, J. O. (2000). Two DNA-binding sites on the globular domain of histone H5 are required for binding to both bulk and 5 S reconstituted nucleosomes. J. Mol. Biol. 304, 21-33.
    • (2000) J. Mol. Biol. , vol.304 , pp. 21-33
    • Duggan, M.M.1    Thomas, J.O.2
  • 37
    • 0021768552 scopus 로고
    • Reconstitution of mononucleosomes: Characterization of distinct particles that differ in the position of the histone core
    • Linxweiler, W. & Hörz, W. (1984). Reconstitution of mononucleosomes: Characterization of distinct particles that differ in the position of the histone core. Nucl. Acids Res. 12, 9395-9413.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 9395-9413
    • Linxweiler, W.1    Hörz, W.2
  • 38
    • 0031079897 scopus 로고    scopus 로고
    • Analysis of in vivo nucleosome positions by determination of nucleosome-linker boundaries in crosslinked chromatin
    • Fragoso, G. & Hager, G. L. (1997). Analysis of in vivo nucleosome positions by determination of nucleosome-linker boundaries in crosslinked chromatin. Methods, 11, 246-252.
    • (1997) Methods , vol.11 , pp. 246-252
    • Fragoso, G.1    Hager, G.L.2
  • 39
    • 0033000670 scopus 로고    scopus 로고
    • Restriction enzymes as probes of nucleosome stability and dynamics
    • Polach, K. J. & Widom, J. (1999). Restriction enzymes as probes of nucleosome stability and dynamics. Methods Enzymol. 304, 278-298.
    • (1999) Methods Enzymol. , vol.304 , pp. 278-298
    • Polach, K.J.1    Widom, J.2
  • 40
    • 0028791330 scopus 로고
    • Mechanism of protein access to specific DNA sequences in chromatin: A dynamic equilibrium model for gene regulation
    • Polach, K. J. & Widom, J. (1995). Mechanism of protein access to specific DNA sequences in chromatin: A dynamic equilibrium model for gene regulation. J. Mol. Biol. 254, 130-149.
    • (1995) J. Mol. Biol. , vol.254 , pp. 130-149
    • Polach, K.J.1    Widom, J.2
  • 41
    • 0029875865 scopus 로고    scopus 로고
    • A model for the cooperative binding of eukaryotic regulatory proteins to nucleosomal target sites
    • Polach, K. J. & Widom, J. (1996). A model for the cooperative binding of eukaryotic regulatory proteins to nucleosomal target sites. J. Mol. Biol. 258, 800-812.
    • (1996) J. Mol. Biol. , vol.258 , pp. 800-812
    • Polach, K.J.1    Widom, J.2
  • 42
    • 0030793885 scopus 로고    scopus 로고
    • Binding of NF1 to the MMTV promoter in nucleosomes: Influence of rotational phasing, translational positioning and histone H1
    • Eisfeld, K., Candau, R., Truss, M. & Beato, M. (1997). Binding of NF1 to the MMTV promoter in nucleosomes: Influence of rotational phasing, translational positioning and histone H1. Nucl. Acids Res. 25, 3733-3742.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3733-3742
    • Eisfeld, K.1    Candau, R.2    Truss, M.3    Beato, M.4
  • 43
    • 0025239781 scopus 로고
    • Nucleosome positioning modulates accessibility of regulatory proteins to the mouse mammary tumor virus promoter
    • Piña, B., Brüggemeier, U. & Beato, M. (1990). Nucleosome positioning modulates accessibility of regulatory proteins to the mouse mammary tumor virus promoter. Cell, 60, 719-731.
    • (1990) Cell , vol.60 , pp. 719-731
    • Piña, B.1    Brüggemeier, U.2    Beato, M.3
  • 44
    • 0023938276 scopus 로고
    • Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus
    • Chalepakis, G., Arnemann, J., Slater, E., Bruller, H. J., Gross, B. & Beato, M. (1988). Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus. Cell, 53, 371-382.
    • (1988) Cell , vol.53 , pp. 371-382
    • Chalepakis, G.1    Arnemann, J.2    Slater, E.3    Bruller, H.J.4    Gross, B.5    Beato, M.6
  • 45
    • 0344009861 scopus 로고
    • Contacts between receptor and DNA double helix within a glucocorticoid regulatory element of mouse mammary tumor
    • Scheidereit, C. & Beato, M. (1984). Contacts between receptor and DNA double helix within a glucocorticoid regulatory element of mouse mammary tumor. Proc. Natl Acad. Sci. USA, 81, 3029-3033.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3029-3033
    • Scheidereit, C.1    Beato, M.2
  • 46
    • 0026505146 scopus 로고
    • Glucocorticoid receptor DNA-binding specificity is increased by the organization of DNA in nucleosomes
    • Perlmann, T. (1992). Glucocorticoid receptor DNA-binding specificity is increased by the organization of DNA in nucleosomes. Proc. Natl Acad. Sci. USA, 89, 3884-3888.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3884-3888
    • Perlmann, T.1
  • 47
    • 1842314454 scopus 로고
    • Sequence-specific positioning of nucleosomes over the steroid-inducible MMTV promoter
    • Richard-Foy, H. & Hager, G. L. (1987). Sequence-specific positioning of nucleosomes over the steroid-inducible MMTV promoter. EMBO J. 6, 2321-2328.
    • (1987) EMBO J. , vol.6 , pp. 2321-2328
    • Richard-Foy, H.1    Hager, G.L.2
  • 48
    • 0028793532 scopus 로고
    • Constitutive repression and nuclear factor I-dependent hormone activation of the mouse mammary tumor virus promoter in Saccharomyces cerevisiae
    • Chavez, S., Candau, R., Truss, M. & Beato, M. (1995). Constitutive repression and nuclear factor I-dependent hormone activation of the mouse mammary tumor virus promoter in Saccharomyces cerevisiae. Mol. Cell. Biol. 15, 6987-6998.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6987-6998
    • Chavez, S.1    Candau, R.2    Truss, M.3    Beato, M.4
  • 49
    • 0029034248 scopus 로고
    • Hormone induces binding of receptors and transcription factors to a rearranged nucleosome on the MMTV promoter in vivo
    • Truss, M., Bartsch, J., Schelbert, A., Haché, R. J. G. & Beato, M. (1995). Hormone induces binding of receptors and transcription factors to a rearranged nucleosome on the MMTV promoter in vivo. EMBO J. 14, 1737-1751.
    • (1995) EMBO J. , vol.14 , pp. 1737-1751
    • Truss, M.1    Bartsch, J.2    Schelbert, A.3    Haché, R.J.G.4    Beato, M.5
  • 50
    • 0028130301 scopus 로고
    • Linker histones H1 and H5 prevent the mobility of positioned nucleosomes
    • Pennings, S., Meersseman, G. & Bradbury, E. M. (1994). Linker histones H1 and H5 prevent the mobility of positioned nucleosomes. Proc. Natl Acad. Sci. USA, 91, 10275-10279.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10275-10279
    • Pennings, S.1    Meersseman, G.2    Bradbury, E.M.3
  • 51
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever, M. A., Th'ng, J. P., Sun, X. & Hendzel, M. J. (2000). Rapid exchange of histone H1.1 on chromatin in living human cells. Nature, 408, 873-876.
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 52
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli, T., Gunjan, A., Hock, R., Bustin, M. & Brown, D. T. (2000). Dynamic binding of histone H1 to chromatin in living cells. Nature, 408, 877-881.
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 53
    • 0020568696 scopus 로고
    • The glucocorticoid receptor binds to defined nucleotide sequences near the promoter of mouse mammary tumour virus
    • Scheidereit, C., Geisse, S., Westphal, H. M. & Beato, M. (1983). The glucocorticoid receptor binds to defined nucleotide sequences near the promoter of mouse mammary tumour virus. Nature, 304, 749-752.
    • (1983) Nature , vol.304 , pp. 749-752
    • Scheidereit, C.1    Geisse, S.2    Westphal, H.M.3    Beato, M.4
  • 54
    • 0033166365 scopus 로고    scopus 로고
    • Two-steps synegism between progesterone receptor and the DNA binding domain of NF1 on MMTV mini-chromosomes
    • Di Croce, L., Koop, R., Venditti, P., Westphal, H. M., Nightingale, K., Becker, P. & Beato, M. (1999). Two-steps synegism between progesterone receptor and the DNA binding domain of NF1 on MMTV mini-chromosomes. Mol. Cell, 4, 45-54.
    • (1999) Mol. Cell. , vol.4 , pp. 45-54
    • Di Croce, L.1    Koop, R.2    Venditti, P.3    Westphal, H.M.4    Nightingale, K.5    Becker, P.6    Beato, M.7
  • 55
    • 0026738762 scopus 로고
    • Purified cofactors and histone H1 mediate transcriptional regulation by CTF/NF-I
    • Dusserre, Y. & Mermod, N. (1992). Purified cofactors and histone H1 mediate transcriptional regulation by CTF/NF-I. Mol. Cell. Biol. 12, 5228-5237.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5228-5237
    • Dusserre, Y.1    Mermod, N.2
  • 56
    • 0033621414 scopus 로고    scopus 로고
    • Effects of H1 histone variant overexpression on chromatin structure
    • Gunjan, A., Alexander, B. T., Sittman, D. B. & Brown, D. T. (1999). Effects of H1 histone variant overexpression on chromatin structure. J. Biol. Chem. 274, 37950-37956.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37950-37956
    • Gunjan, A.1    Alexander, B.T.2    Sittman, D.B.3    Brown, D.T.4
  • 57
    • 0032488030 scopus 로고    scopus 로고
    • Chromatin structure: Linking structure to function with histone H1
    • Widom, J. (1998). Chromatin structure: Linking structure to function with histone H1. Curr. Biol. 8, 788-791.
    • (1998) Curr. Biol. , vol.8 , pp. 788-791
    • Widom, J.1
  • 58
    • 0025941083 scopus 로고
    • Histone-H1 and the regulation of transcription by nuclear receptors
    • Oikarinen, J. (1991). Histone-H1 and the regulation of transcription by nuclear receptors. FEBS Letters, 294, 6-10.
    • (1991) FEBS Letters , vol.294 , pp. 6-10
    • Oikarinen, J.1
  • 59
    • 0027235972 scopus 로고
    • The glucocorticoid receptor acts as an antirepressor in receptor-dependent in vitro transcription
    • Eriksson, P. & Wrange, O. (1993). The glucocorticoid receptor acts as an antirepressor in receptor-dependent in vitro transcription. Eur. J. Biochem. 215, 505-511.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 505-511
    • Eriksson, P.1    Wrange, O.2
  • 60
    • 0032472365 scopus 로고    scopus 로고
    • Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome
    • Cirillo, L. A., McPherson, C. E., Bossard, P., Stevens, K., Cherian, S., Shim, E. Y. et al. (1998). Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome. EMBO J. 17, 244-254.
    • (1998) EMBO J. , vol.17 , pp. 244-254
    • Cirillo, L.A.1    McPherson, C.E.2    Bossard, P.3    Stevens, K.4    Cherian, S.5    Shim, E.Y.6
  • 61
    • 0033388099 scopus 로고    scopus 로고
    • An early developmental transcription factor complex that is more stable on nucleosome core particles than on free DNA
    • Cirillo, L. A. & Zaret, K. S. (1999). An early developmental transcription factor complex that is more stable on nucleosome core particles than on free DNA. Mol. Cell. 4, 961-969.
    • (1999) Mol. Cell. , vol.4 , pp. 961-969
    • Cirillo, L.A.1    Zaret, K.S.2
  • 62
    • 0027507894 scopus 로고
    • An active tissue-specific enhancer and bound transcription factors existing in a precisely positioned nucleosomal array
    • McPherson, C. E., Shim, E. Y., Friedman, D. S. & Zaret, K. S. (1993). An active tissue-specific enhancer and bound transcription factors existing in a precisely positioned nucleosomal array. Cell, 75, 387-398.
    • (1993) Cell , vol.75 , pp. 387-398
    • McPherson, C.E.1    Shim, E.Y.2    Friedman, D.S.3    Zaret, K.S.4
  • 63
    • 0032473501 scopus 로고    scopus 로고
    • Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter
    • Lee, H. L. & Archer, T. K. (1998). Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter. EMBO J. 17, 1454-1466.
    • (1998) EMBO J. , vol.17 , pp. 1454-1466
    • Lee, H.L.1    Archer, T.K.2
  • 64
    • 0034935019 scopus 로고    scopus 로고
    • Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling
    • Bhattacharjee, R. N., Banks, G. C., Trotter, K. W., Lee, H. L. & Archer, T. K. (2001). Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling. Mol. Cell. Biol. 21, 5417-5425.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5417-5425
    • Bhattacharjee, R.N.1    Banks, G.C.2    Trotter, K.W.3    Lee, H.L.4    Archer, T.K.5
  • 65
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • Luger, K., Rechsteiner, T. J. & Richmond, T. J. (1999). Preparation of nucleosome core particle from recombinant histones. Methods Enzymol. 304, 3-19.
    • (1999) Methods Enzymol. , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 66
    • 0027096119 scopus 로고
    • Nucleosome core displacement in vitro via a metastable transcription factor-nucleosome complex
    • Workman, J. L. & Kingston, R. E. (1992). Nucleosome core displacement in vitro via a metastable transcription factor-nucleosome complex. Science, 258, 1780-1784.
    • (1992) Science , vol.258 , pp. 1780-1784
    • Workman, J.L.1    Kingston, R.E.2
  • 67
    • 0024512994 scopus 로고
    • Binding of hormone accelerates the kinetics of glucocorticoid and progesterone receptor binding to DNA
    • Schauer, M., Chalepakis, G., Willmann, T. & Beato, M. (1989). Binding of hormone accelerates the kinetics of glucocorticoid and progesterone receptor binding to DNA. Proc. Natl Acad. Sci. USA, 86, 1123-1127.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 1123-1127
    • Schauer, M.1    Chalepakis, G.2    Willmann, T.3    Beato, M.4
  • 68
    • 0025311114 scopus 로고
    • DNA and protein determinants of nucleosome positioning on sea urchin 5S rRNA gene sequences in vitro
    • Dong, F., Hansen, J. C. & van Holde, K. E. (1990). DNA and protein determinants of nucleosome positioning on sea urchin 5S rRNA gene sequences in vitro. Proc. Natl Acad. Sci. USA, 87, 5724-5728.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5724-5728
    • Dong, F.1    Hansen, J.C.2    Van Holde, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.