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Volumn 21, Issue 2, 2011, Pages 175-186

Chromatin higher-order structures and gene regulation

Author keywords

[No Author keywords available]

Indexed keywords

GENOMIC DNA; HISTONE H2AZ; HISTONE H2B; HISTONE H3; HISTONE H4;

EID: 79953163378     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2011.01.022     Document Type: Review
Times cited : (337)

References (113)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997, 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
  • 2
    • 33646242052 scopus 로고    scopus 로고
    • EM measurements define the dimensions of the " 30-nm" chromatin fiber: evidence for a compact, interdigitated structure
    • Robinson P.J., Fairall L., Huynh V.A., Rhodes D. EM measurements define the dimensions of the " 30-nm" chromatin fiber: evidence for a compact, interdigitated structure. Proc Natl Acad Sci USA 2006, 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
  • 3
    • 77954490394 scopus 로고    scopus 로고
    • New chaps in the histone chaperone arena
    • Campos E.I., Reinberg D. New chaps in the histone chaperone arena. Genes Dev 2010, 24:1334-1338.
    • (2010) Genes Dev , vol.24 , pp. 1334-1338
    • Campos, E.I.1    Reinberg, D.2
  • 4
    • 77249178763 scopus 로고    scopus 로고
    • DNA methylation increases nucleosome compaction and rigidity
    • Choy J.S., Wei S., Lee J.Y., Tan S., Chu S., Lee T.H. DNA methylation increases nucleosome compaction and rigidity. J Am Chem Soc 2010, 132:1782-1783.
    • (2010) J Am Chem Soc , vol.132 , pp. 1782-1783
    • Choy, J.S.1    Wei, S.2    Lee, J.Y.3    Tan, S.4    Chu, S.5    Lee, T.H.6
  • 5
    • 2642515598 scopus 로고    scopus 로고
    • A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome
    • Park Y.J., Dyer P.N., Tremethick D.J., Luger K. A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome. J Biol Chem 2004, 279:24274-24282.
    • (2004) J Biol Chem , vol.279 , pp. 24274-24282
    • Park, Y.J.1    Dyer, P.N.2    Tremethick, D.J.3    Luger, K.4
  • 6
    • 34547128660 scopus 로고    scopus 로고
    • Protein-protein Forster resonance energy transfer analysis of nucleosome core particles containing H2A and H2A.Z
    • Hoch D.A., Stratton J.J., Gloss L.M. Protein-protein Forster resonance energy transfer analysis of nucleosome core particles containing H2A and H2A.Z. J Mol Biol 2007, 371:971-988.
    • (2007) J Mol Biol , vol.371 , pp. 971-988
    • Hoch, D.A.1    Stratton, J.J.2    Gloss, L.M.3
  • 7
    • 34250745886 scopus 로고    scopus 로고
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z
    • Jin C., Felsenfeld G. Nucleosome stability mediated by histone variants H3.3 and H2A.Z. Genes Dev 2007, 21:1519-1529.
    • (2007) Genes Dev , vol.21 , pp. 1519-1529
    • Jin, C.1    Felsenfeld, G.2
  • 9
    • 0037961635 scopus 로고    scopus 로고
    • The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling
    • Angelov D., Molla A., Perche P.Y., Hans F., Cote J., Khochbin S., Bouvet P., Dimitrov S. The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling. Mol Cell 2003, 11:1033-1041.
    • (2003) Mol Cell , vol.11 , pp. 1033-1041
    • Angelov, D.1    Molla, A.2    Perche, P.Y.3    Hans, F.4    Cote, J.5    Khochbin, S.6    Bouvet, P.7    Dimitrov, S.8
  • 14
    • 0022273023 scopus 로고
    • Structure of the 300A chromatin filament: X-ray diffraction from oriented samples
    • Widom J., Klug A. Structure of the 300A chromatin filament: X-ray diffraction from oriented samples. Cell 1985, 43:207-213.
    • (1985) Cell , vol.43 , pp. 207-213
    • Widom, J.1    Klug, A.2
  • 16
    • 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. Chromatin fibers are left-handed double helices with diameter and mass per unit length that depend on linker length. Biophys J 1986, 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
  • 17
    • 35648930403 scopus 로고    scopus 로고
    • Chromatin fiber structure: where is the problem now?
    • van Holde K., Zlatanova J. Chromatin fiber structure: where is the problem now?. Semin Cell Dev Biol 2007, 18:651-658.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 651-658
    • van Holde, K.1    Zlatanova, J.2
  • 19
    • 33744831161 scopus 로고    scopus 로고
    • Structure of the '30 nm' chromatin fibre: a key role for the linker histone
    • Robinson P.J., Rhodes D. Structure of the '30 nm' chromatin fibre: a key role for the linker histone. Curr Opin Struct Biol 2006, 16:336-343.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 336-343
    • Robinson, P.J.1    Rhodes, D.2
  • 20
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • Schalch T., Duda S., Sargent D.F., Richmond T.J. X-ray structure of a tetranucleosome and its implications for the chromatin fibre. Nature 2005, 436:138-141.
    • (2005) Nature , vol.436 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 21
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak M., Ishii H., Sun J.M., Pazin M.J., Davie J.R., Peterson C.L. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 2006, 311:844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 22
    • 48249103503 scopus 로고    scopus 로고
    • Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure
    • Routh A., Sandin S., Rhodes D. Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure. Proc Natl Acad Sci USA 2008, 105:8872-8877.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8872-8877
    • Routh, A.1    Sandin, S.2    Rhodes, D.3
  • 23
    • 0028858566 scopus 로고
    • Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms
    • Fletcher T.M., Hansen J.C. Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms. J Biol Chem 1995, 270:25359-25362.
    • (1995) J Biol Chem , vol.270 , pp. 25359-25362
    • Fletcher, T.M.1    Hansen, J.C.2
  • 24
    • 0029882454 scopus 로고    scopus 로고
    • Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains
    • Schwarz P.M., Felthauser A., Fletcher T.M., Hansen J.C. Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry 1996, 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
  • 25
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: requirement for the histone H4 N-terminal tail
    • Dorigo B., Schalch T., Bystricky K., Richmond T.J. Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J Mol Biol 2003, 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
  • 26
    • 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 J.C., Hayes J.J. Salt-dependent intra- and internucleosomal interactions of the H3 tail domain in a model oligonucleosomal array. J Biol Chem 2005, 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
  • 27
    • 33947201778 scopus 로고    scopus 로고
    • The H3 tail domain participates in multiple interactions during folding and self-association of nucleosome arrays
    • Kan P.Y., Lu X., Hansen J.C., Hayes J.J. The H3 tail domain participates in multiple interactions during folding and self-association of nucleosome arrays. Mol Cell Biol 2007, 27:2084-2091.
    • (2007) Mol Cell Biol , vol.27 , pp. 2084-2091
    • Kan, P.Y.1    Lu, X.2    Hansen, J.C.3    Hayes, J.J.4
  • 28
    • 8844281536 scopus 로고    scopus 로고
    • H2A.Z. alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding
    • Fan J.Y., Rangasamy D., Luger K., Tremethick D.J. H2A.Z. alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding. Mol Cell 2004, 16:655-661.
    • (2004) Mol Cell , vol.16 , pp. 655-661
    • Fan, J.Y.1    Rangasamy, D.2    Luger, K.3    Tremethick, D.J.4
  • 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 J.C. The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays. J Biol Chem 2005, 280:33701-33706.
    • (2005) J Biol Chem , vol.280 , pp. 33701-33706
    • Gordon, F.1    Luger, K.2    Hansen, J.C.3
  • 30
    • 67650531093 scopus 로고    scopus 로고
    • Determinants of histone H4 N-terminal domain function during nucleosomal array oligomerization: roles of amino acid sequence, domain length, and charge density
    • McBryant S.J., Klonoski J., Sorensen T.C., Norskog S.S., Williams S., Resch M.G., Toombs J.A., Hobdey S.E., Hansen J.C. Determinants of histone H4 N-terminal domain function during nucleosomal array oligomerization: roles of amino acid sequence, domain length, and charge density. J Biol Chem 2009, 284:16716-16722.
    • (2009) J Biol Chem , vol.284 , pp. 16716-16722
    • McBryant, S.J.1    Klonoski, J.2    Sorensen, T.C.3    Norskog, S.S.4    Williams, S.5    Resch, M.G.6    Toombs, J.A.7    Hobdey, S.E.8    Hansen, J.C.9
  • 31
    • 37549023859 scopus 로고    scopus 로고
    • Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure
    • Wang X., Hayes J.J. Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure. Mol Cell Biol 2008, 28:227-236.
    • (2008) Mol Cell Biol , vol.28 , pp. 227-236
    • Wang, X.1    Hayes, J.J.2
  • 32
    • 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 P.Y., Caterino T.L., Hayes J.J. The H4 tail domain participates in intra- and internucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays. Mol Cell Biol 2009, 29:538-546.
    • (2009) Mol Cell Biol , vol.29 , pp. 538-546
    • Kan, P.Y.1    Caterino, T.L.2    Hayes, J.J.3
  • 33
    • 0036183219 scopus 로고    scopus 로고
    • The essential histone variant H2A.Z. regulates the equilibrium between different chromatin conformational states
    • Fan J.Y., Gordon F., Luger K., Hansen J.C., Tremethick D.J. The essential histone variant H2A.Z. regulates the equilibrium between different chromatin conformational states. Nat Struct Biol 2002, 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
  • 34
    • 35848931678 scopus 로고    scopus 로고
    • The nucleosome surface regulates chromatin compaction and couples it with transcriptional repression
    • Zhou J., Fan J.Y., Rangasamy D., Tremethick D.J. The nucleosome surface regulates chromatin compaction and couples it with transcriptional repression. Nat Struct Mol Biol 2007, 14:1070-1076.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1070-1076
    • Zhou, J.1    Fan, J.Y.2    Rangasamy, D.3    Tremethick, D.J.4
  • 35
    • 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 K.M., Maeshima K., Frangakis A.S., Dubochet J. 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 2008, 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
  • 36
    • 59349086115 scopus 로고    scopus 로고
    • Chromatin loops in gene regulation
    • Kadauke S., Blobel G.A. Chromatin loops in gene regulation. Biochim Biophys Acta 2009, 1789:17-25.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 17-25
    • Kadauke, S.1    Blobel, G.A.2
  • 37
    • 60549103722 scopus 로고    scopus 로고
    • BRG1 requirement for long-range interaction of a locus control region with a downstream promoter
    • Kim S.I., Bultman S.J., Kiefer C.M., Dean A., Bresnick E.H. BRG1 requirement for long-range interaction of a locus control region with a downstream promoter. Proc Natl Acad Sci USA 2009, 106:2259-2264.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2259-2264
    • Kim, S.I.1    Bultman, S.J.2    Kiefer, C.M.3    Dean, A.4    Bresnick, E.H.5
  • 38
    • 65549121213 scopus 로고    scopus 로고
    • Cyclical chromatin looping and transcription factor association on the regulatory regions of the p21 (CDKN1A) gene in response to 1alpha, 25-dihydroxyvitamin D3
    • Saramaki A., Diermeier S., Kellner R., Laitinen H., Vaisanen S., Carlberg C. Cyclical chromatin looping and transcription factor association on the regulatory regions of the p21 (CDKN1A) gene in response to 1alpha, 25-dihydroxyvitamin D3. J Biol Chem 2009, 284:8073-8082.
    • (2009) J Biol Chem , vol.284 , pp. 8073-8082
    • Saramaki, A.1    Diermeier, S.2    Kellner, R.3    Laitinen, H.4    Vaisanen, S.5    Carlberg, C.6
  • 41
    • 29144472375 scopus 로고    scopus 로고
    • A role for the CPF 3'-end processing machinery in RNAP II-dependent gene looping
    • Ansari A., Hampsey M. A role for the CPF 3'-end processing machinery in RNAP II-dependent gene looping. Genes Dev 2005, 19:2969-2978.
    • (2005) Genes Dev , vol.19 , pp. 2969-2978
    • Ansari, A.1    Hampsey, M.2
  • 42
    • 42449140588 scopus 로고    scopus 로고
    • Dynamic interactions between the promoter and terminator regions of the mammalian BRCA1 gene
    • Tan-Wong S.M., French J.D., Proudfoot N.J., Brown M.A. Dynamic interactions between the promoter and terminator regions of the mammalian BRCA1 gene. Proc Natl Acad Sci USA 2008, 105:5160-5165.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5160-5165
    • Tan-Wong, S.M.1    French, J.D.2    Proudfoot, N.J.3    Brown, M.A.4
  • 49
    • 34250777112 scopus 로고    scopus 로고
    • The nuclear envelope and transcriptional control
    • Akhtar A., Gasser S.M. The nuclear envelope and transcriptional control. Nat Rev Genet 2007, 8:507-517.
    • (2007) Nat Rev Genet , vol.8 , pp. 507-517
    • Akhtar, A.1    Gasser, S.M.2
  • 50
    • 77649210955 scopus 로고    scopus 로고
    • Nuclear pore proteins nup153 and megator define transcriptionally active regions in the Drosophila genome
    • Vaquerizas J.M., Suyama R., Kind J., Miura K., Luscombe N.M., Akhtar A. Nuclear pore proteins nup153 and megator define transcriptionally active regions in the Drosophila genome. PLoS Genet 2010, 6:e1000846.
    • (2010) PLoS Genet , vol.6
    • Vaquerizas, J.M.1    Suyama, R.2    Kind, J.3    Miura, K.4    Luscombe, N.M.5    Akhtar, A.6
  • 51
    • 75749103380 scopus 로고    scopus 로고
    • Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes
    • Capelson M., Liang Y., Schulte R., Mair W., Wagner U., Hetzer M.W. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell 2010, 140:372-383.
    • (2010) Cell , vol.140 , pp. 372-383
    • Capelson, M.1    Liang, Y.2    Schulte, R.3    Mair, W.4    Wagner, U.5    Hetzer, M.W.6
  • 52
    • 75749117571 scopus 로고    scopus 로고
    • Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm
    • Kalverda B., Pickersgill H., Shloma V.V., Fornerod M. Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm. Cell 2010, 140:360-371.
    • (2010) Cell , vol.140 , pp. 360-371
    • Kalverda, B.1    Pickersgill, H.2    Shloma, V.V.3    Fornerod, M.4
  • 53
    • 0032490917 scopus 로고    scopus 로고
    • Perinuclear localization of chromatin facilitates transcriptional silencing
    • Andrulis E.D., Neiman A.M., Zappulla D.C., Sternglanz R. Perinuclear localization of chromatin facilitates transcriptional silencing. Nature 1998, 394:592-595.
    • (1998) Nature , vol.394 , pp. 592-595
    • Andrulis, E.D.1    Neiman, A.M.2    Zappulla, D.C.3    Sternglanz, R.4
  • 54
    • 40749122641 scopus 로고    scopus 로고
    • Transcriptional repression mediated by repositioning of genes to the nuclear lamina
    • Reddy K.L., Zullo J.M., Bertolino E., Singh H. Transcriptional repression mediated by repositioning of genes to the nuclear lamina. Nature 2008, 452:243-247.
    • (2008) Nature , vol.452 , pp. 243-247
    • Reddy, K.L.1    Zullo, J.M.2    Bertolino, E.3    Singh, H.4
  • 55
    • 34247341747 scopus 로고    scopus 로고
    • H2A.Z-mediated localization of genes at the nuclear periphery confers epigenetic memory of previous transcriptional state
    • Brickner D.G., Cajigas I., Fondufe-Mittendorf Y., Ahmed S., Lee P.C., Widom J., Brickner J.H. H2A.Z-mediated localization of genes at the nuclear periphery confers epigenetic memory of previous transcriptional state. PLoS Biol 2007, 5:e81.
    • (2007) PLoS Biol , vol.5
    • Brickner, D.G.1    Cajigas, I.2    Fondufe-Mittendorf, Y.3    Ahmed, S.4    Lee, P.C.5    Widom, J.6    Brickner, J.H.7
  • 61
    • 77956282773 scopus 로고    scopus 로고
    • Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
    • Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D. Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc Natl Acad Sci USA 2010, 107:14075-14080.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14075-14080
    • Lewis, P.W.1    Elsaesser, S.J.2    Noh, K.M.3    Stadler, S.C.4    Allis, C.D.5
  • 63
    • 55549141877 scopus 로고    scopus 로고
    • Histone H2A.Z. and DNA methylation are mutually antagonistic chromatin marks
    • Zilberman D., Coleman-Derr D., Ballinger T., Henikoff S. Histone H2A.Z. and DNA methylation are mutually antagonistic chromatin marks. Nature 2008, 456:125-129.
    • (2008) Nature , vol.456 , pp. 125-129
    • Zilberman, D.1    Coleman-Derr, D.2    Ballinger, T.3    Henikoff, S.4
  • 64
    • 77952355762 scopus 로고    scopus 로고
    • Genome-wide evolutionary analysis of eukaryotic DNA methylation
    • Zemach A., McDaniel I.E., Silva P., Zilberman D. Genome-wide evolutionary analysis of eukaryotic DNA methylation. Science 2010, 328:916-919.
    • (2010) Science , vol.328 , pp. 916-919
    • Zemach, A.1    McDaniel, I.E.2    Silva, P.3    Zilberman, D.4
  • 66
    • 33846569960 scopus 로고    scopus 로고
    • A stem cell-like chromatin pattern may predispose tumor suppressor genes to DNA hypermethylation and heritable silencing
    • Ohm J.E., McGarvey K.M., Yu X., Cheng L., Schuebel K.E., Cope L., Mohammad H.P., Chen W., Daniel V.C., Yu W., et al. A stem cell-like chromatin pattern may predispose tumor suppressor genes to DNA hypermethylation and heritable silencing. Nat Genet 2007, 39:237-242.
    • (2007) Nat Genet , vol.39 , pp. 237-242
    • Ohm, J.E.1    McGarvey, K.M.2    Yu, X.3    Cheng, L.4    Schuebel, K.E.5    Cope, L.6    Mohammad, H.P.7    Chen, W.8    Daniel, V.C.9    Yu, W.10
  • 67
    • 0033813699 scopus 로고    scopus 로고
    • Linker histone binding and displacement: versatile mechanism for transcriptional regulation
    • Zlatanova J., Caiafa P., Van Holde K. Linker histone binding and displacement: versatile mechanism for transcriptional regulation. FASEB J 2000, 14:1697-1704.
    • (2000) FASEB J , vol.14 , pp. 1697-1704
    • Zlatanova, J.1    Caiafa, P.2    Van Holde, K.3
  • 68
    • 33745020770 scopus 로고    scopus 로고
    • Determinants of histone H1 mobility and chromatin binding in living cells
    • Catez F., Ueda T., Bustin M. Determinants of histone H1 mobility and chromatin binding in living cells. Nat Struct Mol Biol 2006, 13:305-310.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 305-310
    • Catez, F.1    Ueda, T.2    Bustin, M.3
  • 69
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • Hendzel M.J., Lever M.A., Crawford E., Th'ng J.P. The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. J Biol Chem 2004, 279:20028-20034.
    • (2004) J Biol Chem , vol.279 , pp. 20028-20034
    • Hendzel, M.J.1    Lever, M.A.2    Crawford, E.3    Th'ng, J.P.4
  • 70
    • 70349655631 scopus 로고    scopus 로고
    • Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF
    • Clausell J., Happel N., Hale T.K., Doenecke D., Beato M. Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF. PLoS ONE 2009, 4:e0007243.
    • (2009) PLoS ONE , vol.4
    • Clausell, J.1    Happel, N.2    Hale, T.K.3    Doenecke, D.4    Beato, M.5
  • 71
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • Wisniewski J.R., Zougman A., Kruger S., Mann M. Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol Cell Proteomics 2007, 6:72-87.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Kruger, S.3    Mann, M.4
  • 72
    • 49849084013 scopus 로고    scopus 로고
    • Global changes in and characterization of specific sites of phosphorylation in mouse and human histone H1 Isoforms upon CDK inhibitor treatment using mass spectrometry
    • Deterding L.J., Bunger M.K., Banks G.C., Tomer K.B., Archer T.K. Global changes in and characterization of specific sites of phosphorylation in mouse and human histone H1 Isoforms upon CDK inhibitor treatment using mass spectrometry. J Proteome Res 2008, 7:2368-2379.
    • (2008) J Proteome Res , vol.7 , pp. 2368-2379
    • Deterding, L.J.1    Bunger, M.K.2    Banks, G.C.3    Tomer, K.B.4    Archer, T.K.5
  • 73
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P., Reinberg D. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 2004, 16:93-105.
    • (2004) Mol Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 75
    • 27844519267 scopus 로고    scopus 로고
    • HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding
    • Daujat S., Zeissler U., Waldmann T., Happel N., Schneider R. HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding. J Biol Chem 2005, 280:38090-38095.
    • (2005) J Biol Chem , vol.280 , pp. 38090-38095
    • Daujat, S.1    Zeissler, U.2    Waldmann, T.3    Happel, N.4    Schneider, R.5
  • 76
    • 67649800263 scopus 로고    scopus 로고
    • Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the Jumonji domain-containing JMJD2/KDM4 proteins
    • Trojer P., Zhang J., Yonezawa M., Schmidt A., Zheng H., Jenuwein T., Reinberg D. Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the Jumonji domain-containing JMJD2/KDM4 proteins. J Biol Chem 2009, 284:8395-8405.
    • (2009) J Biol Chem , vol.284 , pp. 8395-8405
    • Trojer, P.1    Zhang, J.2    Yonezawa, M.3    Schmidt, A.4    Zheng, H.5    Jenuwein, T.6    Reinberg, D.7
  • 78
    • 74449093801 scopus 로고    scopus 로고
    • HMGN5/NSBP1: a new member of the HMGN protein family that affects chromatin structure and function
    • Rochman M., Malicet C., Bustin M. HMGN5/NSBP1: a new member of the HMGN protein family that affects chromatin structure and function. Biochim Biophys Acta 2010, 1799:86-92.
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 86-92
    • Rochman, M.1    Malicet, C.2    Bustin, M.3
  • 79
    • 69949100154 scopus 로고    scopus 로고
    • The interaction of NSBP1/HMGN5 with nucleosomes in euchromatin counteracts linker histone-mediated chromatin compaction and modulates transcription
    • Rochman M., Postnikov Y., Correll S., Malicet C., Wincovitch S., Karpova T.S., McNally J.G., Wu X., Bubunenko N.A., Grigoryev S., et al. The interaction of NSBP1/HMGN5 with nucleosomes in euchromatin counteracts linker histone-mediated chromatin compaction and modulates transcription. Mol Cell 2009, 35:642-656.
    • (2009) Mol Cell , vol.35 , pp. 642-656
    • Rochman, M.1    Postnikov, Y.2    Correll, S.3    Malicet, C.4    Wincovitch, S.5    Karpova, T.S.6    McNally, J.G.7    Wu, X.8    Bubunenko, N.A.9    Grigoryev, S.10
  • 80
    • 56949091228 scopus 로고    scopus 로고
    • The interaction of HMGB1 and linker histones occurs through their acidic and basic tails
    • Cato L., Stott K., Watson M., Thomas J.O. The interaction of HMGB1 and linker histones occurs through their acidic and basic tails. J Mol Biol 2008, 384:1262-1272.
    • (2008) J Mol Biol , vol.384 , pp. 1262-1272
    • Cato, L.1    Stott, K.2    Watson, M.3    Thomas, J.O.4
  • 83
    • 77952692464 scopus 로고    scopus 로고
    • PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression
    • Congdon L.M., Houston S.I., Veerappan C.S., Spektor T.M., Rice J.C. PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression. J Cell Biochem 2010, 110:609-619.
    • (2010) J Cell Biochem , vol.110 , pp. 609-619
    • Congdon, L.M.1    Houston, S.I.2    Veerappan, C.S.3    Spektor, T.M.4    Rice, J.C.5
  • 86
    • 9444244427 scopus 로고    scopus 로고
    • Chromatin compaction by a polycomb group protein complex
    • Francis N.J., Kingston R.E., Woodcock C.L. Chromatin compaction by a polycomb group protein complex. Science 2004, 306:1574-1577.
    • (2004) Science , vol.306 , pp. 1574-1577
    • Francis, N.J.1    Kingston, R.E.2    Woodcock, C.L.3
  • 88
    • 0242353300 scopus 로고    scopus 로고
    • Role of the M-loop and reactive center loop domains in the folding and bridging of nucleosome arrays by MENT
    • Springhetti E.M., Istomina N.E., Whisstock J.C., Nikitina T., Woodcock C.L., Grigoryev S.A. Role of the M-loop and reactive center loop domains in the folding and bridging of nucleosome arrays by MENT. J Biol Chem 2003, 278:43384-43393.
    • (2003) J Biol Chem , vol.278 , pp. 43384-43393
    • Springhetti, E.M.1    Istomina, N.E.2    Whisstock, J.C.3    Nikitina, T.4    Woodcock, C.L.5    Grigoryev, S.A.6
  • 89
    • 0042357071 scopus 로고    scopus 로고
    • Chromatin compaction by human MeCP2. Assembly of novel secondary chromatin structures in the absence of DNA methylation
    • Georgel P.T., Horowitz-Scherer R.A., Adkins N., Woodcock C.L., Wade P.A., Hansen J.C. Chromatin compaction by human MeCP2. Assembly of novel secondary chromatin structures in the absence of DNA methylation. J Biol Chem 2003, 278:32181-32188.
    • (2003) J Biol Chem , vol.278 , pp. 32181-32188
    • Georgel, P.T.1    Horowitz-Scherer, R.A.2    Adkins, N.3    Woodcock, C.L.4    Wade, P.A.5    Hansen, J.C.6
  • 92
    • 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 S.J., Krause C., Woodcock C.L., Hansen J.C. 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 2008, 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
  • 96
    • 34249080596 scopus 로고    scopus 로고
    • Theoretical analysis of epigenetic cell memory by nucleosome modification
    • Dodd I.B., Micheelsen M.A., Sneppen K., Thon G. Theoretical analysis of epigenetic cell memory by nucleosome modification. Cell 2007, 129:813-822.
    • (2007) Cell , vol.129 , pp. 813-822
    • Dodd, I.B.1    Micheelsen, M.A.2    Sneppen, K.3    Thon, G.4
  • 97
    • 77950462427 scopus 로고    scopus 로고
    • Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly
    • Xu M., Long C., Chen X., Huang C., Chen S., Zhu B. Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly. Science 2010, 328:94-98.
    • (2010) Science , vol.328 , pp. 94-98
    • Xu, M.1    Long, C.2    Chen, X.3    Huang, C.4    Chen, S.5    Zhu, B.6
  • 102
    • 77949678340 scopus 로고    scopus 로고
    • Chromatin structure and the inheritance of epigenetic information
    • Margueron R., Reinberg D. Chromatin structure and the inheritance of epigenetic information. Nat Rev Genet 2010, 11:285-296.
    • (2010) Nat Rev Genet , vol.11 , pp. 285-296
    • Margueron, R.1    Reinberg, D.2
  • 103
    • 33947137710 scopus 로고    scopus 로고
    • Dynamics of replication-independent histone turnover in budding yeast
    • Dion M.F., Kaplan T., Kim M., Buratowski S., Friedman N., Rando O.J. Dynamics of replication-independent histone turnover in budding yeast. Science 2007, 315:1405-1408.
    • (2007) Science , vol.315 , pp. 1405-1408
    • Dion, M.F.1    Kaplan, T.2    Kim, M.3    Buratowski, S.4    Friedman, N.5    Rando, O.J.6
  • 105
    • 77950342430 scopus 로고    scopus 로고
    • Highly compacted chromatin formed in vitro reflects the dynamics of transcription activation in vivo
    • Li G., Margueron R., Hu G., Stokes D., Wang Y.H., Reinberg D. Highly compacted chromatin formed in vitro reflects the dynamics of transcription activation in vivo. Mol Cell 2010, 38:41-53.
    • (2010) Mol Cell , vol.38 , pp. 41-53
    • Li, G.1    Margueron, R.2    Hu, G.3    Stokes, D.4    Wang, Y.H.5    Reinberg, D.6
  • 106
    • 0033166365 scopus 로고    scopus 로고
    • Two-step synergism between the progesterone receptor and the DNA-binding domain of nuclear factor 1 on MMTV minichromosomes
    • Di Croce L., Koop R., Venditti P., Westphal H.M., Nightingale K.P., Corona D.F., Becker P.B., Beato M. Two-step synergism between the progesterone receptor and the DNA-binding domain of nuclear factor 1 on MMTV minichromosomes. Mol Cell 1999, 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.P.5    Corona, D.F.6    Becker, P.B.7    Beato, M.8
  • 107
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R., Penot G., Hubner M.R., Reid G., Brand H., Kos M., Gannon F. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 2003, 115:751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 109
    • 0036184236 scopus 로고    scopus 로고
    • Opening of compacted chromatin by early developmental transcription factors HNF3 (FoxA) and GATA-4
    • Cirillo L.A., Lin F.R., Cuesta I., Friedman D., Jarnik M., Zaret K.S. Opening of compacted chromatin by early developmental transcription factors HNF3 (FoxA) and GATA-4. Mol Cell 2002, 9:279-289.
    • (2002) Mol Cell , vol.9 , pp. 279-289
    • Cirillo, L.A.1    Lin, F.R.2    Cuesta, I.3    Friedman, D.4    Jarnik, M.5    Zaret, K.S.6
  • 110
    • 33646691283 scopus 로고    scopus 로고
    • Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II
    • Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D. Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Cell 2006, 125:703-717.
    • (2006) Cell , vol.125 , pp. 703-717
    • Pavri, R.1    Zhu, B.2    Li, G.3    Trojer, P.4    Mandal, S.5    Shilatifard, A.6    Reinberg, D.7
  • 111
    • 63049138876 scopus 로고    scopus 로고
    • Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro
    • Francis N.J., Follmer N.E., Simon M.D., Aghia G., Butler J.D. Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro. Cell 2009, 137:110-122.
    • (2009) Cell , vol.137 , pp. 110-122
    • Francis, N.J.1    Follmer, N.E.2    Simon, M.D.3    Aghia, G.4    Butler, J.D.5
  • 112
    • 77956924034 scopus 로고    scopus 로고
    • Inheriting nuclear organization: can nuclear lamins impart spatial memory during post-mitotic nuclear assembly?
    • Martin C., Chen S., Jackson D.A. Inheriting nuclear organization: can nuclear lamins impart spatial memory during post-mitotic nuclear assembly?. Chromosome Res 2010, 18:525-541.
    • (2010) Chromosome Res , vol.18 , pp. 525-541
    • Martin, C.1    Chen, S.2    Jackson, D.A.3
  • 113
    • 33847106524 scopus 로고    scopus 로고
    • Higher-order structures of chromatin: the elusive 30nm fiber
    • Tremethick D.J. Higher-order structures of chromatin: the elusive 30nm fiber. Cell 2008, 128:651-654.
    • (2008) Cell , vol.128 , pp. 651-654
    • Tremethick, D.J.1


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