메뉴 건너뛰기




Volumn 79, Issue 1, 2000, Pages 584-594

Salt-dependent compaction of di- and trinucleosomes studied by small- angle neutron scattering

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ARTICLE; CHICKEN; CHROMATIN STRUCTURE; ELECTRON MICROSCOPY; ERYTHROCYTE; NEUTRON SCATTERING; NONHUMAN; NUCLEOSOME; SCANNING FORCE MICROSCOPY; SIMULATION; ULTRACENTRIFUGATION;

EID: 0342323657     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76318-1     Document Type: Article
Times cited : (22)

References (41)
  • 1
    • 0029583420 scopus 로고
    • Chromatin conformation and salt-induced compaction: Three-dimensional structural information from cryoelectron microscopy
    • Bednar, J., R. A. Horowitz, J. Dubochet, and C. L. Woodcock. 1995. Chromatin conformation and salt-induced compaction: three-dimensional structural information from cryoelectron microscopy. J. Cell Biol. 131:1365-1376.
    • (1995) J. Cell Biol. , vol.131 , pp. 1365-1376
    • Bednar, J.1    Horowitz, R.A.2    Dubochet, J.3    Woodcock, C.L.4
  • 2
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin
    • Bednar, J., R. A. Horowitz, S. A. Grigoryev, L. M. Carruthers, J. C. Hansen, A. J. Koster, and C. L. Woodcock. 1998. Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Proc. Natl. Acad. Sci. USA. 95:14173-14178.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14173-14178
    • Bednar, J.1    Horowitz, R.A.2    Grigoryev, S.A.3    Carruthers, L.M.4    Hansen, J.C.5    Koster, A.J.6    Woodcock, C.L.7
  • 4
    • 0019130753 scopus 로고
    • Changes in chromatin folding in solution
    • Butler, P. J., and J. O. Thomas. 1980. Changes in chromatin folding in solution. J Mol. Biol. 140:505-529.
    • (1980) J Mol. Biol. , vol.140 , pp. 505-529
    • Butler, P.J.1    Thomas, J.O.2
  • 5
    • 0032555763 scopus 로고    scopus 로고
    • Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA
    • Butler, P. J., and J. O. Thomas. 1998. Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA. J. Mol. Biol. 281:401-407.
    • (1998) J. Mol. Biol. , vol.281 , pp. 401-407
    • Butler, P.J.1    Thomas, J.O.2
  • 6
    • 0019316524 scopus 로고
    • Acetylation of histone H4 and its role in chromatin structure and function
    • Chahal, S. S., H. R. Matthews, and E. M. Bradbury. 1980. Acetylation of histone H4 and its role in chromatin structure and function. Nature. 287: 76-79.
    • (1980) Nature , vol.287 , pp. 76-79
    • Chahal, S.S.1    Matthews, H.R.2    Bradbury, E.M.3
  • 8
    • 0025836653 scopus 로고
    • Nucleosome positioning is determined by the (H3-H4)2 tetramer
    • Dong, F., and K. E. van Holde. 1991. Nucleosome positioning is determined by the (H3-H4)2 tetramer. Proc. Natl. Acad. Sci. USA. 88: 10596-10600.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10596-10600
    • Dong, F.1    Van Holde, K.E.2
  • 9
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • H.-J. Hinz, editor. Springer-Verlag, Berlin
    • Durchschlag, H. 1986. Specific volumes of biological macromolecules and some other molecules of biological interest. In Thermodynamic Data for Biochemistry and Biotechnology. H.-J. Hinz, editor. Springer-Verlag, Berlin.45-128.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-128
    • Durchschlag, H.1
  • 10
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch, J. T., and A. Klug. 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
  • 11
    • 0029815618 scopus 로고    scopus 로고
    • The nucleosomal array: Structure/ function relationships
    • Fletcher, T. M., and J. C. Hansen. 1996. The nucleosomal array: structure/ function relationships. Crit. Rev. Eukaryot. Gene Exp. 6:149-188.
    • (1996) Crit. Rev. Eukaryot. Gene Exp. , vol.6 , pp. 149-188
    • Fletcher, T.M.1    Hansen, J.C.2
  • 13
    • 0023447159 scopus 로고
    • Chromatin higher-order structure studied by neutron scattering and scanning transmission electron microscopy
    • Gerchman, S. E., and V. Ramakrishnan. 1987. Chromatin higher-order structure studied by neutron scattering and scanning transmission electron microscopy. Proc. Natl. Acad. Sci. USA. 84:7802-7806.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7802-7806
    • Gerchman, S.E.1    Ramakrishnan, V.2
  • 14
    • 0002622807 scopus 로고
    • Data evaluation in small angle scattering: Calculation of the radial electron density distribution by means of indirect Fourier transformation
    • Glatter, O. 1977. Data evaluation in small angle scattering: calculation of the radial electron density distribution by means of indirect Fourier transformation. Acta Physica Austriaca. 47:83-102.
    • (1977) Acta Physica Austriaca , vol.47 , pp. 83-102
    • Glatter, O.1
  • 15
    • 0026455115 scopus 로고
    • Chromatin structure of Schizosaccharomyces pombe. A nucleosome repeat length that is shorter than the chromatosomal DNA length
    • Godde, J. S., and J. Widom. 1992. Chromatin structure of Schizosaccharomyces pombe. A nucleosome repeat length that is shorter than the chromatosomal DNA length. J. Mol. Biol. 226:1009-1025.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1009-1025
    • Godde, J.S.1    Widom, J.2
  • 16
    • 0028314834 scopus 로고
    • Histone H1 is located in the interior of the chromatin 30-nm filament
    • Graziano, V., S. E. Gerchman, D. K. Schneider, and V. Ramakrishnan. 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
  • 18
    • 84985720098 scopus 로고
    • Monte Carlo approach to the analysis of the rotational diffusion of wormlike chains
    • Hagerman, P. J., and B. H. Zimm. 1981. Monte Carlo approach to the analysis of the rotational diffusion of wormlike chains. Biopolymers. 20:1481-1502.
    • (1981) Biopolymers , vol.20 , pp. 1481-1502
    • Hagerman, P.J.1    Zimm, B.H.2
  • 20
    • 0023720138 scopus 로고
    • Interparticle interactions and structural changes of nucleosome core particles in low-salt solution
    • Hirai, M., N. Niimura, M. Zama, K. Mita, S. Ichimura, F. Tokunaga, and Y. Ishikawa. 1988. Interparticle interactions and structural changes of nucleosome core particles in low-salt solution. Biochemistry. 27:7924-7931.
    • (1988) Biochemistry , vol.27 , pp. 7924-7931
    • Hirai, M.1    Niimura, N.2    Zama, M.3    Mita, K.4    Ichimura, S.5    Tokunaga, F.6    Ishikawa, Y.7
  • 21
    • 0031835671 scopus 로고    scopus 로고
    • Linker histone tails and N-tails of histone H3 are redundant: Scanning force microscopy studies of reconstituted fibers
    • Leuba, S. H., C. Bustamante, K. van Holde, and J. Zlatanova. 1998a. Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers. Biophys. J. 74: 2830-2839.
    • (1998) Biophys. J. , vol.74 , pp. 2830-2839
    • Leuba, S.H.1    Bustamante, C.2    Van Holde, K.3    Zlatanova, J.4
  • 22
    • 0031806540 scopus 로고    scopus 로고
    • Contributions of linker histones and histone H3 to chromatin structure: Scanning force microscopy studies on trypsinized fibers
    • Leuba, S. H., C. Bustamante, J. Zlatanova, and K. van Holde. 1998b. Contributions of linker histones and histone H3 to chromatin structure: scanning force microscopy studies on trypsinized fibers. Biophys. J. 74:2823-2829.
    • (1998) Biophys. J. , vol.74 , pp. 2823-2829
    • Leuba, S.H.1    Bustamante, C.2    Zlatanova, J.3    Van Holde, K.4
  • 23
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., A. W. Mäder, R. K. Richmond, D. F. Sargent, and T. J. Richmond. 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
  • 24
  • 25
    • 0032553448 scopus 로고    scopus 로고
    • Chromatin conformation in living cells: Support for a zigzag model of the 30 nm chromatin fiber
    • Rydberg, B., W. R. Holley, I. S. Mian, and A. Chatterjee. 1998. Chromatin conformation in living cells: support for a zigzag model of the 30 nm chromatin fiber. J. Mol. Biol. 284:71-84.
    • (1998) J. Mol. Biol. , vol.284 , pp. 71-84
    • Rydberg, B.1    Holley, W.R.2    Mian, I.S.3    Chatterjee, A.4
  • 26
    • 0018435056 scopus 로고
    • A new procedure for purifying histone pairs H2a + H2B and H3 + H4 from chromatin using hydroxylapatite
    • Simon, R. H., and G. Felsenfeld. 1979. A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite. Nucleic Acids Res. 6:689-696.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 689-696
    • Simon, R.H.1    Felsenfeld, G.2
  • 27
    • 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., F. Thoma, and J. M. Brubaker. 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
  • 28
    • 0017123378 scopus 로고
    • The mass per unit length of chromatin by low-angle x-ray scattering
    • Sperling, L. 1976. The mass per unit length of chromatin by low-angle x-ray scattering. FEBS Lett. 64:89-91.
    • (1976) FEBS Lett. , vol.64 , pp. 89-91
    • Sperling, L.1
  • 29
    • 0002114003 scopus 로고
    • Methods for obtaining sedimentation coefficient distributions
    • S. E. Harding, A. J. Rowe, and J. Horton, editors. Royal Society of Chemistry, Cambridge
    • Stafford, W. F. 1992. Methods for obtaining sedimentation coefficient distributions. In Analytical Ultracentrifugation in Biochemistry and Polymer Science. S. E. Harding, A. J. Rowe, and J. Horton, editors. Royal Society of Chemistry, Cambridge. 359-393.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 359-393
    • Stafford, W.F.1
  • 30
    • 0028672523 scopus 로고
    • Boundary analysis in sedimentation velocity experiments
    • Stafford, W. F. 1994. Boundary analysis in sedimentation velocity experiments. Methods Enzymol. 240:478-501.
    • (1994) Methods Enzymol. , vol.240 , pp. 478-501
    • Stafford, W.F.1
  • 31
    • 0031031734 scopus 로고    scopus 로고
    • Sedimentation velocity spins a new weave for an old fabric
    • Stafford, W. F. 1997. Sedimentation velocity spins a new weave for an old fabric. Curr. Opin. Biotechnol. 8:14-24.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 14-24
    • Stafford, W.F.1
  • 32
    • 0030063505 scopus 로고    scopus 로고
    • Alterations in nucleosome core structure in linker histone-depleted chromatin
    • Usachenko, S. I., I. M. Gavin, and S. G. Bavykin. 1996. Alterations in nucleosome core structure in linker histone-depleted chromatin. J. Biol. Chem. 271:3831-3836.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3831-3836
    • Usachenko, S.I.1    Gavin, I.M.2    Bavykin, S.G.3
  • 33
    • 0003903126 scopus 로고
    • Springer-Verlag. Heidelberg
    • van Holde, K. E. 1989. Chromatin. Springer-Verlag. Heidelberg.
    • (1989) Chromatin
    • Van Holde, K.E.1
  • 34
    • 0028935863 scopus 로고
    • Chromatin higher order structure: Chasing a mirage?
    • van Holde, K., and J. Zlatanova. 1995. Chromatin higher order structure: chasing a mirage? J. Biol. Chem. 270:8373-8376.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8373-8376
    • Van Holde, K.1    Zlatanova, J.2
  • 35
    • 0029780079 scopus 로고    scopus 로고
    • What determines the folding of the chromatin fiber
    • van Holde, K., and J. Zlatanova. 1996. What determines the folding of the chromatin fiber. Proc. Natl. Acad. Sci. USA. 93:10548-10555.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10548-10555
    • Van Holde, K.1    Zlatanova, J.2
  • 36
    • 0033057811 scopus 로고    scopus 로고
    • Analysis of modulators of chromatin structure in Drosophila
    • Varga-Weisz, P. D., E. J. Bonte, and P. B. Becker. 1999. Analysis of modulators of chromatin structure in Drosophila. Methods Enzymol. 304:742-757.
    • (1999) Methods Enzymol. , vol.304 , pp. 742-757
    • Varga-Weisz, P.D.1    Bonte, E.J.2    Becker, P.B.3
  • 37
    • 0031831516 scopus 로고    scopus 로고
    • Structure, dynamics, and function of chromatin in vitro
    • Widom, J. 1998. Structure, dynamics, and function of chromatin in vitro. Annu. Rev. Biophys. Biomol. Struct. 27:285-327.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 285-327
    • Widom, J.1
  • 39
    • 0025009844 scopus 로고
    • Direct detection of linker DNA bending in defined-length oligomers of chromatin
    • Yao, J., P. T. Lowary, and J. Widom. 1990. Direct detection of linker DNA bending in defined-length oligomers of chromatin. Proc. Natl. Acad. Sci. USA. 87:7603-7607.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7603-7607
    • Yao, J.1    Lowary, P.T.2    Widom, J.3
  • 40
    • 0026015325 scopus 로고
    • Linker DNA bending induced by the core histones of chromatin
    • Yao, J., P. T. Lowary, and J. Widom. 1991. Linker DNA bending induced by the core histones of chromatin. Biochemistry. 30:8408-8414.
    • (1991) Biochemistry , vol.30 , pp. 8408-8414
    • Yao, J.1    Lowary, P.T.2    Widom, J.3
  • 41
    • 0031968760 scopus 로고    scopus 로고
    • Chromatin fiber structure: Morphology, molecular determinants, structural transitions
    • Zlatanova, J., S. H. Leuba, and K. van Holde. 1998. Chromatin fiber structure: morphology, molecular determinants, structural transitions. Biophys. J. 74:2554-2566.
    • (1998) Biophys. J. , vol.74 , pp. 2554-2566
    • Zlatanova, J.1    Leuba, S.H.2    Van Holde, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.