메뉴 건너뛰기




Volumn 281, Issue 3, 1998, Pages 401-407

Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA

Author keywords

Chromatin; Dinucleosomes; DNA bending; Linker DNA; Sedimentation

Indexed keywords

CURVED DNA; DIMER;

EID: 0032555763     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1954     Document Type: Article
Times cited : (37)

References (37)
  • 1
    • 0020131558 scopus 로고
    • Participation of core histone "tails" in the stabilization of the chromatin solenoid
    • Allan J., Harborne N., Rao D.C., Gould H. Participation of core histone "tails" in the stabilization of the chromatin solenoid. J. Cell Biol. 93:1982;285-297
    • (1982) J. Cell Biol. , vol.93 , pp. 285-297
    • Allan, J.1    Harborne, N.2    Rao, D.C.3    Gould, H.4
  • 2
    • 0019888694 scopus 로고
    • Histones H1 and H5: One or two molecules per nucleosome?
    • Bates D.L., Thomas J.O. Histones H1 and H5 one or two molecules per nucleosome? Nucl. Acids Res. 9:1981;5883-5894
    • (1981) Nucl. Acids Res. , vol.9 , pp. 5883-5894
    • Bates, D.L.1    Thomas, J.O.2
  • 3
    • 0019628147 scopus 로고
    • Stability of the higher-order structure of chicken-erythrocyte chromatin in solution
    • Bates D.L., Butler P.J.G., Pearson E.C., Thomas J.O. Stability of the higher-order structure of chicken-erythrocyte chromatin in solution. Eur. J. Biochem. 119:1981;464-476
    • (1981) Eur. J. Biochem. , vol.119 , pp. 464-476
    • Bates, D.L.1    Butler, P.J.G.2    Pearson, E.C.3    Thomas, J.O.4
  • 4
    • 0029583420 scopus 로고
    • Chromatin conformation and salt-induced compaction: Three-dimensional structural information from cryoelectron microscopy
    • Bednar J., Horowitz R.A., Dubochet J., Woodock C.L. Chromatin conformation and salt-induced compaction three-dimensional structural information from cryoelectron microscopy. J. Cell. Biol. 131:1995;1365-1376
    • (1995) J. Cell. Biol. , vol.131 , pp. 1365-1376
    • Bednar, J.1    Horowitz, R.A.2    Dubochet, J.3    Woodock, C.L.4
  • 5
    • 0019130753 scopus 로고
    • Changes in chromatin folding in solution
    • Butler P.J.G., Thomas J.O. Changes in chromatin folding in solution. J. Mol. Biol. 140:1980;505-529
    • (1980) J. Mol. Biol. , vol.140 , pp. 505-529
    • Butler, P.J.G.1    Thomas, J.O.2
  • 6
    • 0019880525 scopus 로고
    • Exchange of histone H1 between segments of chromatin
    • Caron F., Thomas J.O. Exchange of histone H1 between segments of chromatin. J. Mol. Biol. 146:1981;513-537
    • (1981) J. Mol. Biol. , vol.146 , pp. 513-537
    • Caron, F.1    Thomas, J.O.2
  • 7
    • 0025327471 scopus 로고
    • Electrostatic mechanism of chromatin folding
    • Clark D.J., Kimura T. Electrostatic mechanism of chromatin folding. J. Mol. Biol. 211:1990;883-896
    • (1990) J. Mol. Biol. , vol.211 , pp. 883-896
    • Clark, D.J.1    Kimura, T.2
  • 8
    • 0026782131 scopus 로고
    • Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1
    • Garcia-Ramirez M., Dong F., Ausio J. Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1. J. Biol. Chem. 267:1992;19587-19595
    • (1992) J. Biol. Chem. , vol.267 , pp. 19587-19595
    • Garcia-Ramirez, M.1    Dong, F.2    Ausio, J.3
  • 11
    • 0024468871 scopus 로고
    • Homogeneous reconstituted oligonucleosomes. Evidence for salt-dependent folding in the absence of histone H1
    • Hansen J.C., Ausio J., Stanik V.H., van Holde K.E. Homogeneous reconstituted oligonucleosomes. Evidence for salt-dependent folding in the absence of histone H1. Biochemistry. 28:1989;9129-9136
    • (1989) Biochemistry , vol.28 , pp. 9129-9136
    • Hansen, J.C.1    Ausio, J.2    Stanik, V.H.3    Van Holde, K.E.4
  • 12
    • 0025056959 scopus 로고
    • Core histone - DNA interactions in sea urchin sperm chromatin. the N-terminal tail of H2B interacts with linker DNA
    • Hill C.S., Thomas J.O. Core histone - DNA interactions in sea urchin sperm chromatin. The N-terminal tail of H2B interacts with linker DNA. Eur. J. Biochem. 187:1990;145-153
    • (1990) Eur. J. Biochem. , vol.187 , pp. 145-153
    • Hill, C.S.1    Thomas, J.O.2
  • 13
    • 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. The three-dimensional architecture of chromatin in situ electron tomography reveals fibers composed of a continuously variable zig-zag nucleosomal ribbon. J. Cell Biol. 125:1994;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
  • 15
    • 0025884566 scopus 로고
    • Extended C-terminal tail of wheat H2A interacts with DNA of the "linker" region
    • Lindsey G.G., Orgeig S., Thompson P., Davies N., Maeder D.L. Extended C-terminal tail of wheat H2A interacts with DNA of the "linker" region. J. Mol. Biol. 218:1991;805-813
    • (1991) J. Mol. Biol. , vol.218 , pp. 805-813
    • Lindsey, G.G.1    Orgeig, S.2    Thompson, P.3    Davies, N.4    Maeder, D.L.5
  • 16
    • 0020645755 scopus 로고
    • Higher order structure of chromatin: Orientation of nucleosomes within the 30 nm chromatin solenoid is independent of species and linker length
    • McGhee J.D., Nickol J.D., Felsenfeld G., Rau D.C. Higher order structure of chromatin orientation of nucleosomes within the 30 nm chromatin solenoid is independent of species and linker length. Cell. 33:1983;831-841
    • (1983) Cell , vol.33 , pp. 831-841
    • McGhee, J.D.1    Nickol, J.D.2    Felsenfeld, G.3    Rau, D.C.4
  • 17
    • 0001743558 scopus 로고
    • Asymmetric lateral distribution of unshielded phosphate groups in nucleosomal DNA and its role in DNA bending
    • Mirzabekov A.D., Rich A. Asymmetric lateral distribution of unshielded phosphate groups in nucleosomal DNA and its role in DNA bending. Proc. Natl Acad. Sci. USA. 76:1979;1118-1121
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1118-1121
    • Mirzabekov, A.D.1    Rich, A.2
  • 18
    • 0017358203 scopus 로고
    • Action of micrococcal nuclease on chromatin and the location of histone H1
    • Noll M., Kornberg R.D. Action of micrococcal nuclease on chromatin and the location of histone H1. J. Mol. Biol. 109:1977;393-404
    • (1977) J. Mol. Biol. , vol.109 , pp. 393-404
    • Noll, M.1    Kornberg, R.D.2
  • 19
    • 0024380891 scopus 로고
    • Thymine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin
    • Pehrson J.R. Thymine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin. Proc. Natl. Acad. Sci. USA. 86:1989;9149-9153
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9149-9153
    • Pehrson, J.R.1
  • 20
    • 0029115144 scopus 로고
    • Probing the conformation of nucleosome linker DNA in situ with pyrimidine dimer formation
    • Pehrson J.R. Probing the conformation of nucleosome linker DNA in situ with pyrimidine dimer formation. J. Biol. Chem. 270:1995;22440-22444
    • (1995) J. Biol. Chem. , vol.270 , pp. 22440-22444
    • Pehrson, J.R.1
  • 21
  • 22
    • 0017123378 scopus 로고
    • The mass per unit length of chromatin by low-angle X-ray scattering
    • Sperling L., Tardieu A. The mass per unit length of chromatin by low-angle X-ray scattering. FEBS Letters. 64:1976;89-91
    • (1976) FEBS Letters , vol.64 , pp. 89-91
    • Sperling, L.1    Tardieu, A.2
  • 23
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford W.F. III. Boundary analysis in sedimentation transport experiments a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203:1992;295-301
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford III, W.F.1
  • 24
    • 0002114003 scopus 로고
    • Methods for obtaining sedimentation coefficient distributions
    • S.E. Harding, A.J. Rowe, & J.C. Horton. Cambridge, UK: The Royal Society of Chemistry
    • Stafford W.F. III. Methods for obtaining sedimentation coefficient distributions. Harding S.E., Rowe A.J., Horton J.C. Analytical Ultracentrifugation in Biochemistry and Polymer Science. 1994;359-393 The Royal Society of Chemistry, Cambridge, UK
    • (1994) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 359-393
    • Stafford III, W.F.1
  • 25
    • 0028672523 scopus 로고
    • Numerical computer methods, part B: Boundary analysis in sedimentation velocity experiments
    • Stafford W.F. III. Numerical computer methods, part B boundary analysis in sedimentation velocity experiments. Methods Enzymol. 240:1994;478-501
    • (1994) Methods Enzymol. , vol.240 , pp. 478-501
    • Stafford III, W.F.1
  • 26
    • 0002093485 scopus 로고
    • Possible nucleosome arrangements in the higher order structure of chromatin
    • Staynov D. Possible nucleosome arrangements in the higher order structure of chromatin. Int. J. Biol. Macromol. 5:1983;3-9
    • (1983) Int. J. Biol. Macromol. , vol.5 , pp. 3-9
    • Staynov, D.1
  • 27
    • 0028597967 scopus 로고
    • DNA bending by asymmetric phosphate neutralization
    • Strauss J.K., Maher L.J. DNA bending by asymmetric phosphate neutralization. Science. 266:1994;1829-1834
    • (1994) Science , vol.266 , pp. 1829-1834
    • Strauss, J.K.1    Maher, L.J.2
  • 28
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma F., Koller Th., Klug A. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J. Cell Biol. 83:1979;403-427
    • (1979) J. Cell Biol. , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, Th.2    Klug, A.3
  • 29
    • 0000179826 scopus 로고    scopus 로고
    • Isolation and fractionation of chromatin and linker histones
    • H. Gould. Oxford: Oxford University Press
    • Thomas J.O. Isolation and fractionation of chromatin and linker histones. Gould H. Chromatin. 1998;1-34 Oxford University Press, Oxford
    • (1998) Chromatin , pp. 1-34
    • Thomas, J.O.1
  • 30
    • 0019197607 scopus 로고
    • Size-dependence of a stable higher-order structure of chromatin
    • Thomas J.O., Butler P.J.G. Size-dependence of a stable higher-order structure of chromatin. J. Mol. Biol. 144:1980;89-93
    • (1980) J. Mol. Biol. , vol.144 , pp. 89-93
    • Thomas, J.O.1    Butler, P.J.G.2
  • 31
    • 0017903377 scopus 로고
    • The study of histone-histone associations by chemical cross-linking
    • Thomas J.O., Kornberg R.D. The study of histone-histone associations by chemical cross-linking. Methods Cell Biol. 18:1978;429-440
    • (1978) Methods Cell Biol. , vol.18 , pp. 429-440
    • Thomas, J.O.1    Kornberg, R.D.2
  • 32
    • 0029780079 scopus 로고    scopus 로고
    • What determines the folding of the chromatin fiber?
    • van Holde K., Zlatanova J. What determines the folding of the chromatin fiber? Proc. Natl Acad Sci. USA. 93:1996;10548-10555
    • (1996) Proc. Natl Acad Sci. USA , vol.93 , pp. 10548-10555
    • Van Holde, K.1    Zlatanova, J.2
  • 33
    • 0022650876 scopus 로고
    • Chromatin fibers are left-handed 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. Chromatin fibers are left-handed helices with diameter and mass per unit length that depend on linker length. Biophys. J. 49:1986;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
  • 34
    • 0021250785 scopus 로고
    • The higher-order structure of chromatin: Evidence for a helical ribbon arrangement
    • Woodcock C.L.F., Frado L.-L., Rattner J.B. The higher-order structure of chromatin evidence for a helical ribbon arrangement. J. Cell. Biol. 99:1984;42-52
    • (1984) J. Cell. Biol. , vol.99 , pp. 42-52
    • Woodcock, C.L.F.1    Frado, L.-L.2    Rattner, J.B.3
  • 35
    • 0025009844 scopus 로고
    • Direct detection of linker DNA bending in defined-length oligomers of chromatin
    • Yao J., Lowary P.T., Widom J. Direct detection of linker DNA bending in defined-length oligomers of chromatin. Proc. Natl Acad. Sci. USA. 87:1990;7603-7607
    • (1990) Proc. Natl Acad. Sci. USA. , vol.87 , pp. 7603-7607
    • Yao, J.1    Lowary, P.T.2    Widom, J.3
  • 36
    • 0026015325 scopus 로고
    • Linker DNA bending induced by the core histones of chromatin
    • Yao J., Lowary P.T., Widom J. Linker DNA bending induced by the core histones of chromatin. Biochemistry. 30:1991;8408-8414
    • (1991) Biochemistry , vol.30 , pp. 8408-8414
    • Yao, J.1    Lowary, P.T.2    Widom, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.