메뉴 건너뛰기




Volumn 257, Issue 1, 1996, Pages 30-42

Linker histone-dependent DNA structure in linear mononucleosomes

Author keywords

Chromatin superstructure; DNA wrapping; Electron microscopy; Nucleosome fractionation; Nucleosome position

Indexed keywords

DNA FRAGMENT; HISTONE H5;

EID: 0029994947     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0144     Document Type: Article
Times cited : (158)

References (43)
  • 1
    • 0019157001 scopus 로고
    • The structure of histone Hl and its location in chromatin
    • Allan, J., Hartman, P. G., Crane-Robinson, C. & Aviles, F. X. (1980). The structure of histone Hl 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
  • 2
    • 0022446807 scopus 로고
    • Roles of H1 domains in determining higher order chromatin structure and Hl location
    • Allan, J., Mitchell, T., Harborne, N., Bohm, L. & Crane-Robinson, C. (1986). Roles of H1 domains in determining higher order chromatin structure and Hl location. J. Mol. Biol. 187, 591-601.
    • (1986) J. Mol. Biol. , vol.187 , pp. 591-601
    • Allan, J.1    Mitchell, T.2    Harborne, N.3    Bohm, L.4    Crane-Robinson, C.5
  • 3
    • 0022565962 scopus 로고
    • The superstructure of chromatin and its condensation mechanism. II theoretical analysis of the X-ray scattering patterns and model calculations
    • Bordas, J., Perez-Grau, L., Koch, M. H. J., Vega, M. C. & Nave, C. (1986). The superstructure of chromatin and its condensation mechanism. II Theoretical analysis of the X-ray scattering patterns and model calculations. Eur. Biophys. J. 13, 175-185.
    • (1986) Eur. Biophys. J. , vol.13 , pp. 175-185
    • Bordas, J.1    Perez-Grau, L.2    Koch, M.H.J.3    Vega, M.C.4    Nave, C.5
  • 4
    • 0026560170 scopus 로고
    • Site-directed mutagenesis studies on the binding of the globular domain of linker histone H5 to the nucleosome
    • Buckle, R. S., Maman, J. D. & Allan, J. (1992). Site-directed mutagenesis studies on the binding of the globular domain of linker histone H5 to the nucleosome. J. Mol. Biol. 223, 651-659.
    • (1992) J. Mol. Biol. , vol.223 , pp. 651-659
    • Buckle, R.S.1    Maman, J.D.2    Allan, J.3
  • 5
    • 0021524715 scopus 로고
    • A defined structure of the 30 nm chromatin fibre which accomodates different nucleosomal repeat lengths
    • Butler, P. J. G. (1984). A defined structure of the 30 nm chromatin fibre which accomodates different nucleosomal repeat lengths. EMBO J. 3, 2599-2604.
    • (1984) EMBO J. , vol.3 , pp. 2599-2604
    • Butler, P.J.G.1
  • 6
    • 0023711642 scopus 로고
    • α-Helix in the carboxy-terminal domains of histones H1 and H5
    • Clark, D. J., Hill, C. S., Martin, R. S. & Thomas, J. O. (1988). α-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, R.S.3    Thomas, J.O.4
  • 8
    • 0026546508 scopus 로고
    • Chromatin reconstitution on small DNA rings IV. DNA supercoiling and nucleosome sequence preference
    • Duband-Goulet, I., Carot, V., Ulyanov, A. V., Douc-Rasy S. & Prunell, A. (1992). Chromatin reconstitution on small DNA rings IV. DNA supercoiling and nucleosome sequence preference. J. Mol. Biol. 224, 981-1001.
    • (1992) J. Mol. Biol. , vol.224 , pp. 981-1001
    • Duband-Goulet, I.1    Carot, V.2    Ulyanov, A.V.3    Douc-Rasy, S.4    Prunell, A.5
  • 9
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch, J. T. & Klug, A. (1976). Solenoidal model for superstructure in chromatin. Proc. Natl Acad. Sci. USA, 73, 1897-1901.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 1897-1901
    • Finch, J.T.1    Klug, A.2
  • 10
    • 0029151148 scopus 로고
    • DNA at the entry-exit of the nucleosome observed by cryo-electron microscopy
    • Furrer, P, Bednar, J., Dubochet, J., Hamiche, A. & Prunell, A. (1995). DNA at the entry-exit of the nucleosome observed by cryo-electron 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
  • 11
    • 0028446542 scopus 로고
    • Expression of chicken linker histones in E. coli: Sources of problems and methods for overcoming some of the difficulties
    • Gerchman, S. E., Graziano, V. & Ramakrishnan, V. (1994). Expression of chicken linker histones in E. coli: sources of problems and methods for overcoming some of the difficulties. Protein Express. Purif. 5, 242-251.
    • (1994) Protein Express. Purif. , vol.5 , pp. 242-251
    • Gerchman, S.E.1    Graziano, V.2    Ramakrishnan, V.3
  • 12
  • 14
    • 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, 351-353.
    • (1994) Nature , vol.368 , pp. 351-353
    • Graziano, V.1    Gerchman, S.E.2    Schneider, D.K.3    Ramakrishnan, V.4
  • 15
    • 0028221098 scopus 로고
    • The three-dimensional architecture of chromatin in situ: Electron tomography reveals fibers composed of a continuously variable zig-zag nucleosomal ribbon
    • Horowitz, R. A., Agard, D. A., Sedat, J. W. & Woodcock, C. L. (1994). The three-dimensional architecture of chromatin in situ: electron tomography reveals fibers composed of a continuously variable zig-zag nucleosomal ribbon. J. Cell Biol. 125, 1-10.
    • (1994) J. Cell Biol. , vol.125 , pp. 1-10
    • Horowitz, R.A.1    Agard, D.A.2    Sedat, J.W.3    Woodcock, C.L.4
  • 16
    • 0022427783 scopus 로고
    • The arrangement of H5 molecules in extended and condensed chicken erythrocyte chromatin
    • Lennard, A. C. & Thomas, J. O. (1985). The arrangement of H5 molecules in extended and condensed chicken erythrocyte chromatin. EMBO J. 4, 3455-3462.
    • (1985) EMBO J. , vol.4 , pp. 3455-3462
    • Lennard, A.C.1    Thomas, J.O.2
  • 17
    • 0024413864 scopus 로고
    • Understanding the anomalous electrophoresis of bent DNA molecules: A reptation model
    • Levene, S. D. & Zimm, B. H. (1989). Understanding the anomalous electrophoresis of bent DNA molecules: a reptation model. Science, 245, 396-399.
    • (1989) Science , vol.245 , pp. 396-399
    • Levene, S.D.1    Zimm, B.H.2
  • 18
    • 0020447056 scopus 로고
    • Mobility of DNA in gel electrophoresis
    • Lumpkin, O. J. & Zimm, B. H. (1982). Mobility of DNA in gel electrophoresis. Biopolymers, 21, 2315-2316.
    • (1982) Biopolymers , vol.21 , pp. 2315-2316
    • Lumpkin, O.J.1    Zimm, B.H.2
  • 19
    • 0020645755 scopus 로고
    • Higher order structure of chromatin: Orientation of nucleosomes within the 30 nm chromatin solenoid is independent of species and spacer length
    • McGhee, J. D., Nickol, J. M., Felsenfeld, G. & Rau, D. C. (1983). Higher order structure of chromatin: orientation of nucleosomes within the 30 nm chromatin solenoid is independent of species and spacer length. Cell, 33, 831-841.
    • (1983) Cell , vol.33 , pp. 831-841
    • McGhee, J.D.1    Nickol, J.M.2    Felsenfeld, G.3    Rau, D.C.4
  • 20
    • 0026642219 scopus 로고
    • Mobile nucleosomes - A general behavior
    • Meersseman, G., Pennings, S. & Bradbury E. M. (1992). Mobile nucleosomes - a general behavior. EMBO J. 11, 2951-2959.
    • (1992) EMBO J. , vol.11 , pp. 2951-2959
    • Meersseman, G.1    Pennings, S.2    Bradbury, E.M.3
  • 21
    • 0028279576 scopus 로고
    • Octamer displacement and redistribution in transcription of single nucleosomes
    • O'Donohue, M.-F., Duband-Goulet, I., Hamiche, A. & Prunell, A. (1994). Octamer displacement and redistribution in transcription of single nucleosomes. Nucl. Acids Res. 22, 937-945.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 937-945
    • O'Donohue, M.-F.1    Duband-Goulet, I.2    Hamiche, A.3    Prunell, A.4
  • 22
    • 0029115144 scopus 로고
    • Probing the conformation of nucleosome linker DNA in situ with pyrimidine dimer formation
    • Pehrson, J. R. (1995). Probing the conformation of nucleosome linker DNA in situ with pyrimidine dimer formation. J. Biol. Chem. 270, 22440-22444.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22440-22444
    • Pehrson, J.R.1
  • 23
    • 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
  • 24
    • 0021760689 scopus 로고
    • Structure of the nucleosome core particle at 7 Å resolution
    • Richmond, T. J., Finch, J. T., Rushton, B. M., Rhodes, D. & Klug, A. (1984). Structure of the nucleosome core particle at 7 Å resolution. Nature, 311, 532-537.
    • (1984) Nature , vol.311 , pp. 532-537
    • Richmond, T.J.1    Finch, J.T.2    Rushton, B.M.3    Rhodes, D.4    Klug, A.5
  • 25
    • 0021112873 scopus 로고
    • Close contacts between H1 histone molecules in nuclei
    • Ring, D. & Cole, R. D. (1983). Close contacts between H1 histone molecules in nuclei. J. Biol. Chem. 258, 15361-15364.
    • (1983) J. Biol. Chem. , vol.258 , pp. 15361-15364
    • Ring, D.1    Cole, R.D.2
  • 26
    • 0027279063 scopus 로고
    • Probability of DNA knotting and the effective diameter of the DNA double helix
    • Rybenkov, V. V., Cozzarelli, N. R. & Vologodskii, A. V. (1993). Probability of DNA knotting and the effective diameter of the DNA double helix. Proc. Natl Acad. Sci. USA, 90, 5307-5311.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5307-5311
    • Rybenkov, V.V.1    Cozzarelli, N.R.2    Vologodskii, A.V.3
  • 27
    • 0027200062 scopus 로고
    • Knotting of a DNA chain during ring closure
    • Shaw, S. Y. & Wang, J. C. (1993). Knotting of a DNA chain during ring closure. Science, 260, 533-536.
    • (1993) Science , vol.260 , pp. 533-536
    • Shaw, S.Y.1    Wang, J.C.2
  • 28
    • 0020695571 scopus 로고
    • Structural features of a phased nucleosome core particle
    • Simpson R. T. & Stafford, D. W. (1983). Structural features of a phased nucleosome core particle. Proc. Natl Acad. Sci. USA, 80, 51-55.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 51-55
    • Simpson, R.T.1    Stafford, D.W.2
  • 29
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones. A model system for study of higher order structure
    • Simpson, R. T., Thoma, F. & Brubaker, J. M. (1985). Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones. A model system for study of higher order structure. Cell, 42, 799-808.
    • (1985) Cell , vol.42 , pp. 799-808
    • Simpson, R.T.1    Thoma, F.2    Brubaker, J.M.3
  • 30
    • 0002093485 scopus 로고
    • Possible nucleosome arrangements in the higher-order structure of chromatin
    • Staynov, D. Z. (1983). Possible nucleosome arrangements in the higher-order structure of chromatin. Int. J. Biol. Macromol. 5, 3-10.
    • (1983) Int. J. Biol. Macromol. , vol.5 , pp. 3-10
    • Staynov, D.Z.1
  • 31
    • 0023745077 scopus 로고
    • Generation of different nucleosome spacing periodicities in vitro. Possible origin of cell type specificity
    • Stein, A. & Mitchell, M. (1988). Generation of different nucleosome spacing periodicities in vitro. Possible origin of cell type specificity J. Mol. Biol. 203, 1029-1043.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1029-1043
    • Stein, A.1    Mitchell, M.2
  • 32
    • 0020530868 scopus 로고
    • Involvement of the domains of histones H1 and H5 in the structural organization of soluble chromatin
    • Thoma, F., Losa, R. & Koller, T. (1983). Involvement of the domains of histones H1 and H5 in the structural organization of soluble chromatin. J. Mol. Biol. 167, 619-640.
    • (1983) J. Mol. Biol. , vol.167 , pp. 619-640
    • Thoma, F.1    Losa, R.2    Koller, T.3
  • 33
    • 0017903377 scopus 로고
    • The study of histone-histone association by chemical cross-linking
    • Thomas, J. O. & Kornberg, R. D. (1978). The study of histone-histone association by chemical cross-linking. Methods Cell Biol. 18, 429-440.
    • (1978) Methods Cell Biol. , vol.18 , pp. 429-440
    • Thomas, J.O.1    Kornberg, R.D.2
  • 34
    • 0021104510 scopus 로고
    • Exchange of histones H1 and H5 between chromatin fragments. A preference of H5 for higher-order structures
    • Thomas, J. O. & Rees, C. (1983). Exchange of histones H1 and H5 between chromatin fragments. A preference of H5 for higher-order structures. Eur. J. Biochem. 134, 109-115.
    • (1983) Eur. J. Biochem. , vol.134 , pp. 109-115
    • Thomas, J.O.1    Rees, C.2
  • 35
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to λ sire-specific recombination complexes
    • Thompson, J. F. & Landy A. (1988). Empirical estimation of protein-induced DNA bending angles: applications to λ sire-specific recombination complexes. Nucl. Acids Res. 16, 9687-9705.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 36
    • 0003903126 scopus 로고
    • Springer-Verlag, Berlin
    • van Holde, K. E. (1988). Chromatin, Springer-Verlag, Berlin.
    • (1988) Chromatin
    • Van Holde, K.E.1
  • 37
    • 0022650876 scopus 로고
    • Chromatin fibers are left-handed double helices with diameter and mass per unit length that depend on linker length
    • Williams, S. P., Athey B. D., Muglia, L. J., Schappe, R. S., Gough, A. H. & Langmore, J. P. (1986). Chromatin fibers are left-handed double helices with diameter and mass per unit length that depend on linker length. Biophys. J. 49, 233-248.
    • (1986) Biophys. J. , vol.49 , pp. 233-248
    • Williams, S.P.1    Athey, B.D.2    Muglia, L.J.3    Schappe, R.S.4    Gough, A.H.5    Langmore, J.P.6
  • 38
    • 0027517831 scopus 로고
    • A chromatin folding model that incorporates linker variability generates fibers resembling the native structures
    • Woodcock, C. L., Grigoryev, S. A., Horowitz, R. A. & Whitaker, N. (1993). A chromatin folding model that incorporates linker variability generates fibers resembling the native structures. Proc. Natl Acad. Sci. USA, 90, 9021-9025.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9021-9025
    • Woodcock, C.L.1    Grigoryev, S.A.2    Horowitz, R.A.3    Whitaker, N.4
  • 39
    • 0021268779 scopus 로고
    • The locus of sequence-directed and protein-induced DNA bending
    • Wu, H.-M. & Crothers, D. M. (1984). The locus of sequence-directed and protein-induced DNA bending. Nature, 308, 509-513.
    • (1984) Nature , vol.308 , pp. 509-513
    • Wu, H.-M.1    Crothers, D.M.2
  • 41
    • 0024292379 scopus 로고
    • Chromatin reconstitution on small DNA rings II. DNA supercoiling on the nucleosome
    • Zivanovic, Y., Goulet, I., Révet, B., Le Bret, M. & Prunell, A. (1988). Chromatin reconstitution on small DNA rings II. DNA supercoiling on the nucleosome. J. Mol. Biol. 200, 267-290.
    • (1988) J. Mol. Biol. , vol.200 , pp. 267-290
    • Zivanovic, Y.1    Goulet, I.2    Révet, B.3    Le Bret, M.4    Prunell, A.5
  • 42
    • 0025063459 scopus 로고
    • Chromatin reconstitution on small DNA rings. III. Histone H5 dependence of DNA supercoiling on the nucleosome
    • Zivanovic, Y., Duband-Goulet, I., Schultz, P., Stofer, E., Oudet, P. & Prunell, A. (1990). Chromatin reconstitution on small DNA rings. III. Histone H5 dependence of DNA supercoiling on the nucleosome., J. Mol. Biol. 214, 479-495.
    • (1990) J. Mol. Biol. , vol.214 , pp. 479-495
    • Zivanovic, Y.1    Duband-Goulet, I.2    Schultz, P.3    Stofer, E.4    Oudet, P.5    Prunell, A.6
  • 43
    • 0028286015 scopus 로고
    • Linker DNA accessibility in chromatin fibers of different conformations: A reevaluation
    • Zlatanova, J., Leuba, S. H., Yang, G., Bustamante, C. & van Holde, K. (1994). Linker DNA accessibility in chromatin fibers of different conformations: a reevaluation. Proc. Natl Acad. Sci. USA, 91, 5277-5280.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5277-5280
    • Zlatanova, J.1    Leuba, S.H.2    Yang, G.3    Bustamante, C.4    Van Holde, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.