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Volumn 35, Issue 10, 2016, Pages 1115-1132

Nucleosomal arrays self-assemble into supramolecular globular structures lacking 30-nm fibers

Author keywords

10 nm chromatin fiber; analytical ultracentrifugation; microscopy; nucleosomal array; X ray scattering

Indexed keywords

DNA; MICROCOCCAL NUCLEASE; MONOMER; OLIGOMER; MAGNESIUM CHLORIDE; NUCLEOSOME;

EID: 84963853509     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201592660     Document Type: Article
Times cited : (148)

References (87)
  • 4
    • 30044447160 scopus 로고    scopus 로고
    • Cryoelectron microscopy of vitrified sections: A new challenge for the analysis of functional nuclear architecture
    • Bouchet-Marquis C, Dubochet J, Fakan S, (2006) Cryoelectron microscopy of vitrified sections: a new challenge for the analysis of functional nuclear architecture. Histochem Cell Biol 125: 43-51
    • (2006) Histochem Cell Biol , vol.125 , pp. 43-51
    • Bouchet-Marquis, C.1    Dubochet, J.2    Fakan, S.3
  • 5
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding
    • Carruthers LM, Bednar J, Woodcock CL, Hansen JC, (1998) Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: mechanistic ramifications for higher-order chromatin folding. Biochemistry 37: 14776-14787
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.L.3    Hansen, J.C.4
  • 6
    • 0034711232 scopus 로고    scopus 로고
    • The core histone N termini function independently of linker histones during chromatin condensation
    • Carruthers LM, Hansen JC, (2000) The core histone N termini function independently of linker histones during chromatin condensation. J Biol Chem 275: 37285-37290
    • (2000) J Biol Chem , vol.275 , pp. 37285-37290
    • Carruthers, L.M.1    Hansen, J.C.2
  • 8
    • 84878011578 scopus 로고    scopus 로고
    • Exploring the three-dimensional organization of genomes: Interpreting chromatin interaction data
    • Dekker J, Marti-Renom MA, Mirny LA, (2013) Exploring the three-dimensional organization of genomes: interpreting chromatin interaction data. Nat Rev Genet 14: 390-403
    • (2013) Nat Rev Genet , vol.14 , pp. 390-403
    • Dekker, J.1    Marti-Renom, M.A.2    Mirny, L.A.3
  • 9
    • 8844265931 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of highly heterogeneous systems
    • Demeler B, van Holde KE, (2004) Sedimentation velocity analysis of highly heterogeneous systems. Anal Biochem 335: 279-288
    • (2004) Anal Biochem , vol.335 , pp. 279-288
    • Demeler, B.1    Van Holde, K.E.2
  • 10
    • 33744816438 scopus 로고    scopus 로고
    • UltraScan - A comprehensive data analysis software package for analytical ultracentrifugation experiments
    • In, Scott D.J. Harding S.E. Rowe A.J. (eds), pp. London: Royal Society of Chemistry
    • Demeler B, (2005) UltraScan-a comprehensive data analysis software package for analytical ultracentrifugation experiments. In Modern Analytical Ultracentrifugation: Techniques and Methods, Scott DJ, Harding SE, Rowe AJ, (eds), pp 210-230. London: Royal Society of Chemistry
    • (2005) Modern Analytical Ultracentrifugation: Techniques and Methods , pp. 210-230
    • Demeler, B.1
  • 11
    • 84968920855 scopus 로고    scopus 로고
    • Analytical ultracentrifugation data analysis with ultrascan-III
    • (in press). In, Uchiyama S. Stafford W.F. Laue T. (eds), Chapter 8. Japan: Springer
    • Demeler B, Gorbet GE, (in press) Analytical ultracentrifugation data analysis with ultrascan-III. In Analytical Ultracentrifugation: Instrumentation, Software, and Applications, Uchiyama S, Stafford WF, Laue T, (eds), Chapter 8. Japan: Springer
    • Analytical Ultracentrifugation: Instrumentation, Software, and Applications
    • Demeler, B.1    Gorbet, G.E.2
  • 12
    • 84917690836 scopus 로고    scopus 로고
    • Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions
    • Dhall A, Wei S, Fierz B, Woodcock CL, Lee TH, Chatterjee C, (2014) Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions. J Biol Chem 289: 33827-33837
    • (2014) J Biol Chem , vol.289 , pp. 33827-33837
    • Dhall, A.1    Wei, S.2    Fierz, B.3    Woodcock, C.L.4    Lee, T.H.5    Chatterjee, C.6
  • 13
    • 84861095603 scopus 로고    scopus 로고
    • Topological domains in mammalian genomes identified by analysis of chromatin interactions
    • Dixon JR, Selvaraj S, Yue F, Kim A, Li Y, Shen Y, Hu M, Liu JS, Ren B, (2012) Topological domains in mammalian genomes identified by analysis of chromatin interactions. Nature 485: 376-380
    • (2012) Nature , vol.485 , pp. 376-380
    • Dixon, J.R.1    Selvaraj, S.2    Yue, F.3    Kim, A.4    Li, Y.5    Shen, Y.6    Hu, M.7    Liu, J.S.8    Ren, B.9
  • 14
    • 0035354585 scopus 로고    scopus 로고
    • Changes in biomolecular conformation seen by small angle X-ray scattering
    • Doniach S, (2001) Changes in biomolecular conformation seen by small angle X-ray scattering. Chem Rev 101: 1763-1778
    • (2001) Chem Rev , vol.101 , pp. 1763-1778
    • Doniach, S.1
  • 15
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: Requirement for the histone H4 N-terminal tail
    • Dorigo B, Schalch T, Bystricky K, Richmond TJ, (2003) Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J Mol Biol 327: 85-96
    • (2003) J Mol Biol , vol.327 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.J.4
  • 17
    • 0014966666 scopus 로고
    • Molecular weights of coliphages and coliphage DNA. II. Measurement of diffusion coefficients using optical mixing spectroscopy, and measurement of sedimentation coefficients
    • Dubin SB, Benedek GB, Bancroft FC, Freifelder D, (1970) Molecular weights of coliphages and coliphage DNA. II. Measurement of diffusion coefficients using optical mixing spectroscopy, and measurement of sedimentation coefficients. J Mol Biol 54: 547-556
    • (1970) J Mol Biol , vol.54 , pp. 547-556
    • Dubin, S.B.1    Benedek, G.B.2    Bancroft, F.C.3    Freifelder, D.4
  • 18
    • 84946208311 scopus 로고    scopus 로고
    • Stable chromosome condensation revealed by chromosome conformation capture
    • Eagen KP, Hartl TA, Kornberg RD, (2015) Stable chromosome condensation revealed by chromosome conformation capture. Cell 163: 934-946
    • (2015) Cell , vol.163 , pp. 934-946
    • Eagen, K.P.1    Hartl, T.A.2    Kornberg, R.D.3
  • 19
    • 0020681351 scopus 로고
    • Architecture of metaphase chromosomes and chromosome scaffolds
    • Earnshaw WC, Laemmli UK, (1983) Architecture of metaphase chromosomes and chromosome scaffolds. J Cell Biol 96: 84-93
    • (1983) J Cell Biol , vol.96 , pp. 84-93
    • Earnshaw, W.C.1    Laemmli, U.K.2
  • 20
    • 58149401194 scopus 로고    scopus 로고
    • Analysis of cryo-electron microscopy images does not support the existence of 30-nm chromatin fibers in mitotic chromosomes in situ
    • Eltsov M, Maclellan KM, Maeshima K, Frangakis AS, Dubochet J, (2008) Analysis of cryo-electron microscopy images does not support the existence of 30-nm chromatin fibers in mitotic chromosomes in situ. Proc Natl Acad Sci USA 105: 19732-19737
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19732-19737
    • Eltsov, M.1    MacLellan, K.M.2    Maeshima, K.3    Frangakis, A.S.4    Dubochet, J.5
  • 21
    • 0036183219 scopus 로고    scopus 로고
    • The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states
    • Fan JY, Gordon F, Luger K, Hansen JC, Tremethick DJ, (2002) The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states. Nat Struct Biol 9: 172-176
    • (2002) Nat Struct Biol , vol.9 , pp. 172-176
    • Fan, J.Y.1    Gordon, F.2    Luger, K.3    Hansen, J.C.4    Tremethick, D.J.5
  • 24
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch JT, 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
  • 27
    • 84885863242 scopus 로고    scopus 로고
    • Chromatin in a marine picoeukaryote is a disordered assemblage of nucleosomes
    • Gan L, Ladinsky MS, Jensen GJ, (2013) Chromatin in a marine picoeukaryote is a disordered assemblage of nucleosomes. Chromosoma 122: 377-386
    • (2013) Chromosoma , vol.122 , pp. 377-386
    • Gan, L.1    Ladinsky, M.S.2    Jensen, G.J.3
  • 28
    • 4444258534 scopus 로고    scopus 로고
    • Chromatin architecture of the human genome: Gene-rich domains are enriched in open chromatin fibers
    • Gilbert N, Boyle S, Fiegler H, Woodfine K, Carter NP, Bickmore WA, (2004) Chromatin architecture of the human genome: gene-rich domains are enriched in open chromatin fibers. Cell 118: 555-566
    • (2004) Cell , vol.118 , pp. 555-566
    • Gilbert, N.1    Boyle, S.2    Fiegler, H.3    Woodfine, K.4    Carter, N.P.5    Bickmore, W.A.6
  • 29
    • 26644471508 scopus 로고    scopus 로고
    • The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays
    • Gordon F, Luger K, Hansen JC, (2005) The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays. J Biol Chem 280: 33701-33706
    • (2005) J Biol Chem , vol.280 , pp. 33701-33706
    • Gordon, F.1    Luger, K.2    Hansen, J.C.3
  • 30
    • 69449098842 scopus 로고    scopus 로고
    • Evidence for heteromorphic chromatin fibers from analysis of nucleosome interactions
    • Grigoryev SA, Arya G, Correll S, Woodcock CL, Schlick T, (2009) Evidence for heteromorphic chromatin fibers from analysis of nucleosome interactions. Proc Natl Acad Sci USA 106: 13317-13322
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13317-13322
    • Grigoryev, S.A.1    Arya, G.2    Correll, S.3    Woodcock, C.L.4    Schlick, T.5
  • 31
    • 84861956987 scopus 로고    scopus 로고
    • Chromatin organization - The 30 nm fiber
    • Grigoryev SA, Woodcock CL, (2012) Chromatin organization-the 30 nm fiber. Exp Cell Res 318: 1448-1455
    • (2012) Exp Cell Res , vol.318 , pp. 1448-1455
    • Grigoryev, S.A.1    Woodcock, C.L.2
  • 32
    • 0027412701 scopus 로고
    • Assembly and structural properties of subsaturated chromatin arrays
    • Hansen JC, Lohr D, (1993) Assembly and structural properties of subsaturated chromatin arrays. J Biol Chem 268: 5840-5848
    • (1993) J Biol Chem , vol.268 , pp. 5840-5848
    • Hansen, J.C.1    Lohr, D.2
  • 33
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions
    • Hansen JC, (2002) Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions. Annu Rev Biophys Biomol Struct 31: 361-392
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 36
    • 84924795571 scopus 로고    scopus 로고
    • Chromosome dynamics during mitosis
    • Hirano T, (2015) Chromosome dynamics during mitosis. Cold Spring Harb Perspect Biol 7: a015792
    • (2015) Cold Spring Harb Perspect Biol , vol.7 , pp. a015792
    • Hirano, T.1
  • 37
    • 0041440100 scopus 로고    scopus 로고
    • Condensin is required for nonhistone protein assembly and structural integrity of vertebrate mitotic chromosomes
    • Hudson DF, Vagnarelli P, Gassmann R, Earnshaw WC, (2003) Condensin is required for nonhistone protein assembly and structural integrity of vertebrate mitotic chromosomes. Dev Cell 5: 323-336
    • (2003) Dev Cell , vol.5 , pp. 323-336
    • Hudson, D.F.1    Vagnarelli, P.2    Gassmann, R.3    Earnshaw, W.C.4
  • 38
    • 0035805498 scopus 로고    scopus 로고
    • Magnesium-dependent association and folding of oligonucleosomes reconstituted with ubiquitinated H2A
    • Jason LJ, Moore SC, Ausio J, Lindsey G, (2001) Magnesium-dependent association and folding of oligonucleosomes reconstituted with ubiquitinated H2A. J Biol Chem 276: 14597-14601
    • (2001) J Biol Chem , vol.276 , pp. 14597-14601
    • Jason, L.J.1    Moore, S.C.2    Ausio, J.3    Lindsey, G.4
  • 41
    • 58249118858 scopus 로고    scopus 로고
    • The H4 tail domain participates in intra- and internucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays
    • Kan PY, Caterino TL, Hayes JJ, (2009) The H4 tail domain participates in intra- and internucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays. Mol Cell Biol 29: 538-546
    • (2009) Mol Cell Biol , vol.29 , pp. 538-546
    • Kan, P.Y.1    Caterino, T.L.2    Hayes, J.J.3
  • 42
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ, (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24: 946-950
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 43
    • 0020583592 scopus 로고
    • Low angle x-ray diffraction studies of chromatin structure in vivo and in isolated nuclei and metaphase chromosomes
    • Langmore JP, Paulson JR, (1983) Low angle x-ray diffraction studies of chromatin structure in vivo and in isolated nuclei and metaphase chromosomes. J Cell Biol 96: 1120-1131
    • (1983) J Cell Biol , vol.96 , pp. 1120-1131
    • Langmore, J.P.1    Paulson, J.R.2
  • 44
    • 84943197820 scopus 로고    scopus 로고
    • Structure and organization of chromatin fiber in the nucleus
    • Li G, Zhu P, (2015) Structure and organization of chromatin fiber in the nucleus. FEBS Lett 589: 2893-2904
    • (2015) FEBS Lett , vol.589 , pp. 2893-2904
    • Li, G.1    Zhu, P.2
  • 45
    • 82555176461 scopus 로고    scopus 로고
    • Influence of histone tails and H4 tail acetylations on nucleosome-nucleosome interactions
    • Liu Y, Lu C, Yang Y, Fan Y, Yang R, Liu CF, Korolev N, Nordenskiold L, (2011) Influence of histone tails and H4 tail acetylations on nucleosome-nucleosome interactions. J Mol Biol 414: 749-764
    • (2011) J Mol Biol , vol.414 , pp. 749-764
    • Liu, Y.1    Lu, C.2    Yang, Y.3    Fan, Y.4    Yang, R.5    Liu, C.F.6    Korolev, N.7    Nordenskiold, L.8
  • 46
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • Lowary PT, Widom J, (1998) New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J Mol Biol 276: 19-42
    • (1998) J Mol Biol , vol.276 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 47
    • 58549094957 scopus 로고    scopus 로고
    • Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder
    • Lu X, Hamkalo B, Parseghian MH, Hansen JC, (2009) Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry 48: 164-172
    • (2009) Biochemistry , vol.48 , pp. 164-172
    • Lu, X.1    Hamkalo, B.2    Parseghian, M.H.3    Hansen, J.C.4
  • 48
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ, (1997) Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389: 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 49
    • 0037380769 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of flexible macromolecules: Self-association and tangling of amyloid fibrils
    • MacRaild CA, Hatters DM, Lawrence LJ, Howlett GJ, (2003) Sedimentation velocity analysis of flexible macromolecules: self-association and tangling of amyloid fibrils. Biophys J 84: 2562-2569
    • (2003) Biophys J , vol.84 , pp. 2562-2569
    • MacRaild, C.A.1    Hatters, D.M.2    Lawrence, L.J.3    Howlett, G.J.4
  • 50
    • 77954819238 scopus 로고    scopus 로고
    • Chromatin structure: Does the 30-nm fibre exist in vivo?
    • Maeshima K, Hihara S, Eltsov M, (2010) Chromatin structure: does the 30-nm fibre exist in vivo? Curr Opin Cell Biol 22: 291-297
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 291-297
    • Maeshima, K.1    Hihara, S.2    Eltsov, M.3
  • 51
    • 85027920795 scopus 로고    scopus 로고
    • Chromatin structure revealed by X-ray scattering analysis and computational modeling
    • Maeshima K, Imai R, Hikima T, Joti Y, (2014a) Chromatin structure revealed by X-ray scattering analysis and computational modeling. Methods 70: 154-161
    • (2014) Methods , vol.70 , pp. 154-161
    • Maeshima, K.1    Imai, R.2    Hikima, T.3    Joti, Y.4
  • 53
    • 44349116198 scopus 로고    scopus 로고
    • The silent information regulator 3 protein, SIR3p, binds to chromatin fibers and assembles a hypercondensed chromatin architecture in the presence of salt
    • McBryant SJ, Krause C, Woodcock CL, Hansen JC, (2008) The silent information regulator 3 protein, SIR3p, binds to chromatin fibers and assembles a hypercondensed chromatin architecture in the presence of salt. Mol Cell Biol 28: 3563-3572
    • (2008) Mol Cell Biol , vol.28 , pp. 3563-3572
    • McBryant, S.J.1    Krause, C.2    Woodcock, C.L.3    Hansen, J.C.4
  • 54
    • 79959870239 scopus 로고    scopus 로고
    • The linker region of macroH2A promotes self-association of nucleosomal arrays
    • Muthurajan UM, McBryant SJ, Lu X, Hansen JC, Luger K, (2011) The linker region of macroH2A promotes self-association of nucleosomal arrays. J Biol Chem 286: 23852-23864
    • (2011) J Biol Chem , vol.286 , pp. 23852-23864
    • Muthurajan, U.M.1    McBryant, S.J.2    Lu, X.3    Hansen, J.C.4    Luger, K.5
  • 59
    • 84897475985 scopus 로고    scopus 로고
    • Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure
    • Pepenella S, Murphy KJ, Hayes JJ, (2014) Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure. Chromosoma 123: 3-13
    • (2014) Chromosoma , vol.123 , pp. 3-13
    • Pepenella, S.1    Murphy, K.J.2    Hayes, J.J.3
  • 61
    • 84924559967 scopus 로고    scopus 로고
    • Chromatin fibers are formed by heterogeneous groups of nucleosomes in vivo
    • Ricci MA, Manzo C, Garcia-Parajo MF, Lakadamyali M, Cosma MP, (2015) Chromatin fibers are formed by heterogeneous groups of nucleosomes in vivo. Cell 160: 1145-1158
    • (2015) Cell , vol.160 , pp. 1145-1158
    • Ricci, M.A.1    Manzo, C.2    Garcia-Parajo, M.F.3    Lakadamyali, M.4    Cosma, M.P.5
  • 62
    • 33646242052 scopus 로고    scopus 로고
    • EM measurements define the dimensions of the "30-nm" chromatin fiber: Evidence for a compact, interdigitated structure
    • Robinson PJ, Fairall L, Huynh VA, Rhodes D, (2006) EM measurements define the dimensions of the "30-nm" chromatin fiber: evidence for a compact, interdigitated structure. Proc Natl Acad Sci USA 103: 6506-6511
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6506-6511
    • Robinson, P.J.1    Fairall, L.2    Huynh, V.A.3    Rhodes, D.4
  • 63
    • 33744831161 scopus 로고    scopus 로고
    • Structure of the "30 nm" chromatin fibre: A key role for the linker histone
    • Robinson PJ, Rhodes D, (2006) Structure of the "30 nm" chromatin fibre: a key role for the linker histone. Curr Opin Struct Biol 16: 336-343
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 336-343
    • Robinson, P.J.1    Rhodes, D.2
  • 66
    • 84948567515 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of large oligomeric chromatin complexes using interference detection
    • Rogge RA, Hansen JC, (2015) Sedimentation velocity analysis of large oligomeric chromatin complexes using interference detection. Methods Enzymol 562: 349-362
    • (2015) Methods Enzymol , vol.562 , pp. 349-362
    • Rogge, R.A.1    Hansen, J.C.2
  • 67
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • Schalch T, Duda S, Sargent DF, Richmond TJ, (2005) X-ray structure of a tetranucleosome and its implications for the chromatin fibre. Nature 436: 138-141
    • (2005) Nature , vol.436 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 68
    • 84877044364 scopus 로고    scopus 로고
    • Analytical ultracentrifugation as a tool for studying protein interactions
    • Schuck P, (2013) Analytical ultracentrifugation as a tool for studying protein interactions. Biophys Rev 5: 159-171
    • (2013) Biophys Rev , vol.5 , pp. 159-171
    • Schuck, P.1
  • 69
    • 0028363760 scopus 로고
    • Formation and stability of higher order chromatin structures. Contributions of the histone octamer
    • Schwarz PM, Hansen JC, (1994) Formation and stability of higher order chromatin structures. Contributions of the histone octamer. J Biol Chem 269: 16284-16289
    • (1994) J Biol Chem , vol.269 , pp. 16284-16289
    • Schwarz, P.M.1    Hansen, J.C.2
  • 70
    • 0029882454 scopus 로고    scopus 로고
    • Reversible oligonucleosome self-association: Dependence on divalent cations and core histone tail domains
    • Schwarz PM, Felthauser A, Fletcher TM, Hansen JC, (1996) Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry 35: 4009-4015
    • (1996) Biochemistry , vol.35 , pp. 4009-4015
    • Schwarz, P.M.1    Felthauser, A.2    Fletcher, T.M.3    Hansen, J.C.4
  • 73
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: A model system for study of higher order structure
    • Simpson RT, Thoma F, Brubaker JM, (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
  • 74
    • 84899570718 scopus 로고    scopus 로고
    • Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units
    • Song F, Chen P, Sun D, Wang M, Dong L, Liang D, Xu RM, Zhu P, Li G, (2014) Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units. Science 344: 376-380
    • (2014) Science , vol.344 , pp. 376-380
    • Song, F.1    Chen, P.2    Sun, D.3    Wang, M.4    Dong, L.5    Liang, D.6    Xu, R.M.7    Zhu, P.8    Li, G.9
  • 75
    • 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 WF III, (1992) Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem 203: 295-301
    • (1992) Anal Biochem , vol.203 , pp. 295-301
    • Stafford, W.F.1
  • 76
    • 77957759247 scopus 로고    scopus 로고
    • Activator-dependent p300 acetylation of chromatin in vitro: Enhancement of transcription by disruption of repressive nucleosome-nucleosome interactions
    • Szerlong HJ, Prenni JE, Nyborg JK, Hansen JC, (2010) Activator-dependent p300 acetylation of chromatin in vitro: enhancement of transcription by disruption of repressive nucleosome-nucleosome interactions. J Biol Chem 285: 31954-31964
    • (2010) J Biol Chem , vol.285 , pp. 31954-31964
    • Szerlong, H.J.1    Prenni, J.E.2    Nyborg, J.K.3    Hansen, J.C.4
  • 79
    • 0030922941 scopus 로고    scopus 로고
    • Hybrid trypsinized nucleosomal arrays: Identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction
    • Tse C, Hansen JC, (1997) Hybrid trypsinized nucleosomal arrays: identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction. Biochemistry 36: 11381-11388
    • (1997) Biochemistry , vol.36 , pp. 11381-11388
    • Tse, C.1    Hansen, J.C.2
  • 80
    • 0345898980 scopus 로고    scopus 로고
    • Reconstitution of chromatin in vitro
    • Ura K, Kaneda Y, (2001) Reconstitution of chromatin in vitro. Methods Mol Biol 181: 309-325
    • (2001) Methods Mol Biol , vol.181 , pp. 309-325
    • Ura, K.1    Kaneda, Y.2
  • 82
    • 84879476144 scopus 로고    scopus 로고
    • Modulation of higher order chromatin conformation in mammalian cell nuclei can be mediated by polyamines and divalent cations
    • Visvanathan A, Ahmed K, Even-Faitelson L, Lleres D, Bazett-Jones DP, Lamond AI, (2013) Modulation of higher order chromatin conformation in mammalian cell nuclei can be mediated by polyamines and divalent cations. PLoS ONE 8: e67689
    • (2013) PLoS ONE , vol.8 , pp. e67689
    • Visvanathan, A.1    Ahmed, K.2    Even-Faitelson, L.3    Lleres, D.4    Bazett-Jones, D.P.5    Lamond, A.I.6
  • 83
    • 0022273023 scopus 로고
    • Structure of the 300A chromatin filament: X-ray diffraction from oriented samples
    • Widom J, Klug A, (1985) Structure of the 300A chromatin filament: X-ray diffraction from oriented samples. Cell 43: 207-213
    • (1985) Cell , vol.43 , pp. 207-213
    • Widom, J.1    Klug, A.2
  • 84
    • 0021250785 scopus 로고
    • The higher-order structure of chromatin: Evidence for a helical ribbon arrangement
    • Woodcock CL, Frado LL, Rattner JB, (1984) The higher-order structure of chromatin: evidence for a helical ribbon arrangement. J Cell Biol 99: 42-52
    • (1984) J Cell Biol , vol.99 , pp. 42-52
    • Woodcock, C.L.1    Frado, L.L.2    Rattner, J.B.3
  • 85
    • 0025869750 scopus 로고
    • Ultrastructure of chromatin. I. Negative staining of isolated fibers
    • Woodcock CL, Woodcock H, Horowitz RA, (1991) Ultrastructure of chromatin. I. Negative staining of isolated fibers. J Cell Sci 99 (Pt 1): 99-106
    • (1991) J Cell Sci , vol.99 , pp. 99-106
    • Woodcock, C.L.1    Woodcock, H.2    Horowitz, R.A.3
  • 86
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • Woodcock CL, Skoultchi AI, Fan Y, (2006) Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res 14: 17-25
    • (2006) Chromosome Res , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoultchi, A.I.2    Fan, Y.3
  • 87
    • 25844484588 scopus 로고    scopus 로고
    • Salt-dependent intra- and internucleosomal interactions of the H3 tail domain in a model oligonucleosomal array
    • Zheng C, Lu X, Hansen JC, Hayes JJ, (2005) Salt-dependent intra- and internucleosomal interactions of the H3 tail domain in a model oligonucleosomal array. J Biol Chem 280: 33552-33557
    • (2005) J Biol Chem , vol.280 , pp. 33552-33557
    • Zheng, C.1    Lu, X.2    Hansen, J.C.3    Hayes, J.J.4


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