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Volumn 12, Issue 10, 2011, Pages 6544-6565

ATP-dependent chromatin remodeling factors and their roles in affecting nucleosome fiber composition

Author keywords

Centromere; Chromatin; Chromatin assembly; Chromatin remodeling factor; Histone variant; Linker histone

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ATP DEPENDENT CHROMATIN REMODELING FACTOR; CHROMOSOME PROTEIN; CYCLINE; DAXX PROTEIN; HIGH MOBILITY GROUP PROTEIN; HISTONE H1; HISTONE H2A; HISTONE H2AZ; HISTONE H3; HISTONE H3.1; HISTONE H3.2; HISTONE H3.3; SUCROSE NON FERMENTING 2 PROTEIN; UNCLASSIFIED DRUG; CHROMATIN; HISTONE; NUCLEOSOME;

EID: 80055063786     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12106544     Document Type: Review
Times cited : (17)

References (160)
  • 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
    • 0015964401 scopus 로고
    • Spheroid chromatin units (v bodies)
    • Olins, A.L.; Olins, D.E. Spheroid chromatin units (v bodies). Science 1974, 183, 330-332.
    • (1974) Science , vol.183 , pp. 330-332
    • Olins, A.L.1    Olins, D.E.2
  • 3
    • 0017251130 scopus 로고
    • Structural repeating units in chromatin. I. Evidence for their general occurrence
    • Woodcock, C.L.; Safer, J.P.; Stanchfield, J.E. Structural repeating units in chromatin. I. Evidence for their general occurrence. Exp. Cell Res. 1976, 97, 101-110.
    • (1976) Exp. Cell Res , vol.97 , pp. 101-110
    • Woodcock, C.L.1    Safer, J.P.2    Stanchfield, J.E.3
  • 4
    • 60349089645 scopus 로고    scopus 로고
    • Nucleosome positioning and gene regulation: Advances through genomics
    • Jiang, C.; Pugh, B.F. Nucleosome positioning and gene regulation: advances through genomics. Nat. Rev. Genet. 2009, 10, 161-172.
    • (2009) Nat. Rev. Genet , vol.10 , pp. 161-172
    • Jiang, C.1    Pugh, B.F.2
  • 5
    • 76949093375 scopus 로고    scopus 로고
    • Nucleosome positioning: How is it established, and why does it matter?
    • Radman-Livaja, M.; Rando, O.J. Nucleosome positioning: how is it established, and why does it matter? Dev. Biol. 2010, 339, 258-266.
    • (2010) Dev. Biol , vol.339 , pp. 258-266
    • Radman-Livaja, M.1    Rando, O.J.2
  • 6
    • 34247344995 scopus 로고    scopus 로고
    • Transcription elongation through a chromatin template
    • Lavelle, C. Transcription elongation through a chromatin template. Biochimie 2007, 89, 516-527.
    • (2007) Biochimie , vol.89 , pp. 516-527
    • Lavelle, C.1
  • 7
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function. Cell 2007, 128, 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 9
    • 33846804545 scopus 로고    scopus 로고
    • HMG chromosomal proteins in development and disease
    • Hock, R.; Furusawa, T.; Ueda, T.; Bustin, M. HMG chromosomal proteins in development and disease. Trends Cell Biol. 2007, 17, 72-79.
    • (2007) Trends Cell Biol , vol.17 , pp. 72-79
    • Hock, R.1    Furusawa, T.2    Ueda, T.3    Bustin, M.4
  • 10
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • Clapier, C.R.; Cairns, B.R. The biology of chromatin remodeling complexes. Annu. Rev. Biochem. 2009, 78, 273-304.
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 11
    • 33745122231 scopus 로고    scopus 로고
    • Identification of multiple distinct Snf2 subfamilies with conserved structural motifs
    • Flaus, A.; Martin, D.M.; Barton, G.J.; Owen-Hughes, T. Identification of multiple distinct Snf2 subfamilies with conserved structural motifs. Nucleic Acids Res. 2006, 34, 2887-2905.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2887-2905
    • Flaus, A.1    Martin, D.M.2    Barton, G.J.3    Owen-Hughes, T.4
  • 12
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A.E. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 1993, 3, 419-429.
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1
  • 13
    • 4444289406 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodelling: Factors and functions
    • Eberharter, A.; Becker, P.B. ATP-dependent nucleosome remodelling: factors and functions. J. Cell Sci. 2004, 117, 3707-3711.
    • (2004) J. Cell Sci , vol.117 , pp. 3707-3711
    • Eberharter, A.1    Becker, P.B.2
  • 14
    • 0344198456 scopus 로고    scopus 로고
    • Chromatin remodeling by ATP-dependent molecular machines
    • Lusser, A.; Kadonaga, J.T. Chromatin remodeling by ATP-dependent molecular machines. Bioessays 2003, 25, 1192-1200.
    • (2003) Bioessays , vol.25 , pp. 1192-1200
    • Lusser, A.1    Kadonaga, J.T.2
  • 15
    • 34147101544 scopus 로고    scopus 로고
    • INO80 subfamily of chromatin remodeling complexes
    • Bao, Y.; Shen, X. INO80 subfamily of chromatin remodeling complexes. Mutat. Res. 2007, 618, 18-29.
    • (2007) Mutat. Res , vol.618 , pp. 18-29
    • Bao, Y.1    Shen, X.2
  • 16
    • 34147158728 scopus 로고    scopus 로고
    • The Chd family of chromatin remodelers
    • Marfella, C.G.; Imbalzano, A.N. The Chd family of chromatin remodelers. Mutat. Res. 2007, 618, 30-40.
    • (2007) Mutat. Res , vol.618 , pp. 30-40
    • Marfella, C.G.1    Imbalzano, A.N.2
  • 17
    • 79952539053 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling: Genetics, genomics and mechanisms
    • Hargreaves, D.C.; Crabtree, G.R. ATP-dependent chromatin remodeling: genetics, genomics and mechanisms. Cell Res. 2011, 21, 396-420.
    • (2011) Cell Res , vol.21 , pp. 396-420
    • Hargreaves, D.C.1    Crabtree, G.R.2
  • 23
    • 76349103252 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe genome-wide nucleosome mapping reveals positioning mechanisms distinct from those of Saccharomyces cerevisiae
    • Lantermann, A.B.; Straub, T.; Stralfors, A.; Yuan, G.C.; Ekwall, K.; Korber, P. Schizosaccharomyces pombe genome-wide nucleosome mapping reveals positioning mechanisms distinct from those of Saccharomyces cerevisiae. Nat. Struct. Mol. Biol. 2010, 17, 251-257.
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 251-257
    • Lantermann, A.B.1    Straub, T.2    Stralfors, A.3    Yuan, G.C.4    Ekwall, K.5    Korber, P.6
  • 24
    • 79956316470 scopus 로고    scopus 로고
    • A packing mechanism for nucleosome organization reconstituted across a eukaryotic genome
    • Zhang, Z.; Wippo, C.J.; Wal, M.; Ward, E.; Korber, P.; Pugh, B.F. A packing mechanism for nucleosome organization reconstituted across a eukaryotic genome. Science 2011, 332, 977-980.
    • (2011) Science , vol.332 , pp. 977-980
    • Zhang, Z.1    Wippo, C.J.2    Wal, M.3    Ward, E.4    Korber, P.5    Pugh, B.F.6
  • 25
    • 80052970429 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling: The means to the end
    • Flaus, A.; Owen-Hughes, T. Mechanisms for ATP-dependent chromatin remodelling: the means to the end. FEBS J. 2011, 278, 3579-3595.
    • (2011) FEBS J , vol.278 , pp. 3579-3595
    • Flaus, A.1    Owen-Hughes, T.2
  • 26
    • 1542328273 scopus 로고    scopus 로고
    • Nucleosome remodeling: One mechanism, many phenomena?
    • Langst, G.; Becker, P.B. Nucleosome remodeling: one mechanism, many phenomena? Biochim. Biophys. Acta 2004, 1677, 58-63.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 58-63
    • Langst, G.1    Becker, P.B.2
  • 27
    • 52049091808 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling enzymes and their various roles in cell cycle control
    • Morettini, S.; Podhraski, V.; Lusser, A. ATP-dependent chromatin remodeling enzymes and their various roles in cell cycle control. Front. Biosci. 2008, 13, 5522-5532.
    • (2008) Front. Biosci , vol.13 , pp. 5522-5532
    • Morettini, S.1    Podhraski, V.2    Lusser, A.3
  • 28
    • 33846170060 scopus 로고    scopus 로고
    • Functional differentiation of SWI/SNF remodelers in transcription and cell cycle control
    • Moshkin, Y.M.; Mohrmann, L.; van Ijcken, W.F.; Verrijzer, C.P. Functional differentiation of SWI/SNF remodelers in transcription and cell cycle control. Mol. Cell. Biol. 2007, 27, 651-661.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 651-661
    • Moshkin, Y.M.1    Mohrmann, L.2    van Ijcken, W.F.3    Verrijzer, C.P.4
  • 29
    • 0034624960 scopus 로고    scopus 로고
    • ATP-Dependent histone octamer mobilization and histone deacetylation mediated by the Mi-2 chromatin remodeling complex
    • Guschin, D.; Wade, P.A.; Kikyo, N.; Wolffe, A.P. ATP-Dependent histone octamer mobilization and histone deacetylation mediated by the Mi-2 chromatin remodeling complex. Biochemistry (Mosc.) 2000, 39, 5238-5245.
    • (2000) Biochemistry (Mosc.) , vol.39 , pp. 5238-5245
    • Guschin, D.1    Wade, P.A.2    Kikyo, N.3    Wolffe, A.P.4
  • 30
    • 18344410319 scopus 로고    scopus 로고
    • dMi-2 and ISWI chromatin remodelling factors have distinct nucleosome binding and mobilization properties
    • Brehm, A.; Langst, G.; Kehle, J.; Clapier, C.R.; Imhof, A.; Eberharter, A.; Muller, J.; Becker, P.B. dMi-2 and ISWI chromatin remodelling factors have distinct nucleosome binding and mobilization properties. EMBO J. 2000, 19, 4332-4341.
    • (2000) EMBO J , vol.19 , pp. 4332-4341
    • Brehm, A.1    Langst, G.2    Kehle, J.3    Clapier, C.R.4    Imhof, A.5    Eberharter, A.6    Muller, J.7    Becker, P.B.8
  • 31
    • 33745221438 scopus 로고    scopus 로고
    • Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin remodeling complexes
    • Stockdale, C.; Flaus, A.; Ferreira, H.; Owen-Hughes, T. Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin remodeling complexes. J. Biol. Chem. 2006, 281, 16279-16288.
    • (2006) J. Biol. Chem , vol.281 , pp. 16279-16288
    • Stockdale, C.1    Flaus, A.2    Ferreira, H.3    Owen-Hughes, T.4
  • 32
    • 0033603212 scopus 로고    scopus 로고
    • Nucleosome movement by CHRAC and ISWI without disruption or trans- displacement of the histone octamer
    • Langst, G.; Bonte, E.J.; Corona, D.F.; Becker, P.B. Nucleosome movement by CHRAC and ISWI without disruption or trans- displacement of the histone octamer. Cell 1999, 97, 843-852.
    • (1999) Cell , vol.97 , pp. 843-852
    • Langst, G.1    Bonte, E.J.2    Corona, D.F.3    Becker, P.B.4
  • 33
    • 0033603238 scopus 로고    scopus 로고
    • ATP-dependent histone octamer sliding mediated by the chromatin remodeling complex NURF
    • Hamiche, A.; Sandaltzopoulos, R.; Gdula, D.A.; Wu, C. ATP-dependent histone octamer sliding mediated by the chromatin remodeling complex NURF. Cell 1999, 97, 833-842.
    • (1999) Cell , vol.97 , pp. 833-842
    • Hamiche, A.1    Sandaltzopoulos, R.2    Gdula, D.A.3    Wu, C.4
  • 34
    • 35348984181 scopus 로고    scopus 로고
    • DNA sequence- and conformation-directed positioning of nucleosomes by chromatin-remodeling complexes
    • Rippe, K.; Schrader, A.; Riede, P.; Strohner, R.; Lehmann, E.; Langst, G. DNA sequence- and conformation-directed positioning of nucleosomes by chromatin-remodeling complexes. Proc. Natl. Acad. Sci. USA 2007, 104, 15635-15640.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 15635-15640
    • Rippe, K.1    Schrader, A.2    Riede, P.3    Strohner, R.4    Lehmann, E.5    Langst, G.6
  • 35
    • 0029901861 scopus 로고    scopus 로고
    • CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes
    • Stokes, D.G.; Tartof, K.D.; Perry, R.P. CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes. Proc. Natl. Acad. Sci. USA 1996, 93, 7137-7142.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7137-7142
    • Stokes, D.G.1    Tartof, K.D.2    Perry, R.P.3
  • 36
    • 17744371151 scopus 로고    scopus 로고
    • The Drosophila trithorax group protein Kismet facilitates an early step in transcriptional elongation by RNA Polymerase II
    • Srinivasan, S.; Armstrong, J.A.; Deuring, R.; Dahlsveen, I.K.; McNeill, H.; Tamkun, J.W. The Drosophila trithorax group protein Kismet facilitates an early step in transcriptional elongation by RNA Polymerase II. Development 2005, 132, 1623-1635.
    • (2005) Development , vol.132 , pp. 1623-1635
    • Srinivasan, S.1    Armstrong, J.A.2    Deuring, R.3    Dahlsveen, I.K.4    McNeill, H.5    Tamkun, J.W.6
  • 37
    • 33745847547 scopus 로고    scopus 로고
    • Antagonistic forces that position nucleosomes in vivo
    • Whitehouse, I.; Tsukiyama, T. Antagonistic forces that position nucleosomes in vivo. Nat. Struct. Mol. Biol. 2006, 13, 633-640.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 633-640
    • Whitehouse, I.1    Tsukiyama, T.2
  • 39
    • 46149108345 scopus 로고    scopus 로고
    • Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci
    • Petesch, S.J.; Lis, J.T. Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci. Cell 2008, 134, 74-84.
    • (2008) Cell , vol.134 , pp. 74-84
    • Petesch, S.J.1    Lis, J.T.2
  • 41
    • 0036928142 scopus 로고    scopus 로고
    • A role for chromatin remodeling in transcriptional termination by RNA polymerase II
    • Alen, C.; Kent, N.A.; Jones, H.S.; O'Sullivan, J.; Aranda, A.; Proudfoot, N.J. A role for chromatin remodeling in transcriptional termination by RNA polymerase II. Mol. Cell 2002, 10, 1441-1452.
    • (2002) Mol. Cell , vol.10 , pp. 1441-1452
    • Alen, C.1    Kent, N.A.2    Jones, H.S.3    O'Sullivan, J.4    Aranda, A.5    Proudfoot, N.J.6
  • 43
    • 0028093378 scopus 로고
    • Nucleosome disruption and enhancement of activator binding by a human SW1/SNF complex
    • Kwon, H.; Imbalzano, A.N.; Khavari, P.A.; Kingston, R.E.; Green, M.R. Nucleosome disruption and enhancement of activator binding by a human SW1/SNF complex. Nature 1994, 370, 477-481.
    • (1994) Nature , vol.370 , pp. 477-481
    • Kwon, H.1    Imbalzano, A.N.2    Khavari, P.A.3    Kingston, R.E.4    Green, M.R.5
  • 45
    • 0028467446 scopus 로고
    • Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex
    • Cote, J.; Quinn, J.; Workman, J.L.; Peterson, C.L. Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex. Science 1994, 265, 53-60.
    • (1994) Science , vol.265 , pp. 53-60
    • Cote, J.1    Quinn, J.2    Workman, J.L.3    Peterson, C.L.4
  • 46
    • 0029814422 scopus 로고    scopus 로고
    • Nucleosome disruption by human SWI/SNF is maintained in the absence of continued ATP hydrolysis
    • Imbalzano, A.N.; Schnitzler, G.R.; Kingston, R.E. Nucleosome disruption by human SWI/SNF is maintained in the absence of continued ATP hydrolysis. J. Biol. Chem. 1996, 271, 20726-20733.
    • (1996) J. Biol. Chem , vol.271 , pp. 20726-20733
    • Imbalzano, A.N.1    Schnitzler, G.R.2    Kingston, R.E.3
  • 48
    • 0029826906 scopus 로고    scopus 로고
    • Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex
    • Owen-Hughes, T.; Utley, R.T.; Cote, J.; Peterson, C.L.; Workman, J.L. Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex. Science 1996, 273, 513-516.
    • (1996) Science , vol.273 , pp. 513-516
    • Owen-Hughes, T.1    Utley, R.T.2    Cote, J.3    Peterson, C.L.4    Workman, J.L.5
  • 51
    • 65249164132 scopus 로고    scopus 로고
    • Mechanisms that specify promoter nucleosome location and identity
    • Hartley, P.D.; Madhani, H.D. Mechanisms that specify promoter nucleosome location and identity. Cell 2009, 137, 445-458.
    • (2009) Cell , vol.137 , pp. 445-458
    • Hartley, P.D.1    Madhani, H.D.2
  • 52
    • 0033564199 scopus 로고    scopus 로고
    • ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly
    • Ito, T.; Levenstein, M.E.; Fyodorov, D.V.; Kutach, A.K.; Kobayashi, R.; Kadonaga, J.T. ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly. Genes Dev. 1999, 13, 1529-1539.
    • (1999) Genes Dev , vol.13 , pp. 1529-1539
    • Ito, T.1    Levenstein, M.E.2    Fyodorov, D.V.3    Kutach, A.K.4    Kobayashi, R.5    Kadonaga, J.T.6
  • 53
    • 0033082238 scopus 로고    scopus 로고
    • Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits
    • Phelan, M.L.; Sif, S.; Narlikar, G.J.; Kingston, R.E. Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits. Mol. Cell 1999, 3, 247-253.
    • (1999) Mol. Cell , vol.3 , pp. 247-253
    • Phelan, M.L.1    Sif, S.2    Narlikar, G.J.3    Kingston, R.E.4
  • 54
    • 33847076248 scopus 로고    scopus 로고
    • Chromatin challenges during DNA replication and repair
    • Groth, A.; Rocha, W.; Verreault, A.; Almouzni, G. Chromatin challenges during DNA replication and repair. Cell 2007, 128, 721-733.
    • (2007) Cell , vol.128 , pp. 721-733
    • Groth, A.1    Rocha, W.2    Verreault, A.3    Almouzni, G.4
  • 55
    • 74549138158 scopus 로고    scopus 로고
    • Chaperoning histones during DNA replication and repair
    • Ransom, M.; Dennehey, B.K.; Tyler, J.K. Chaperoning histones during DNA replication and repair. Cell 2010, 140, 183-195.
    • (2010) Cell , vol.140 , pp. 183-195
    • Ransom, M.1    Dennehey, B.K.2    Tyler, J.K.3
  • 56
    • 18744373022 scopus 로고    scopus 로고
    • Strategies for the reconstitution of chromatin
    • Lusser, A.; Kadonaga, J.T. Strategies for the reconstitution of chromatin. Nat. Methods 2004, 1, 19-26.
    • (2004) Nat. Methods , vol.1 , pp. 19-26
    • Lusser, A.1    Kadonaga, J.T.2
  • 57
    • 0034686020 scopus 로고    scopus 로고
    • Purification and characterization of a human factor that assembles and remodels chromatin
    • LeRoy, G.; Loyola, A.; Lane, W.S.; Reinberg, D. Purification and characterization of a human factor that assembles and remodels chromatin. J. Biol. Chem. 2000, 275, 14787-14790.
    • (2000) J. Biol. Chem , vol.275 , pp. 14787-14790
    • Leroy, G.1    Loyola, A.2    Lane, W.S.3    Reinberg, D.4
  • 58
    • 15544369061 scopus 로고    scopus 로고
    • Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly
    • Lusser, A.; Urwin, D.L.; Kadonaga, J.T. Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly. Nat. Struct. Mol. Biol. 2005, 12, 160-166.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 160-166
    • Lusser, A.1    Urwin, D.L.2    Kadonaga, J.T.3
  • 59
    • 80051748137 scopus 로고    scopus 로고
    • Identification of a Rapidly Formed Nonnucleosomal Histone-DNA Intermediate that Is Converted into Chromatin by ACF
    • Torigoe, S.E.; Urwin, D.L.; Ishii, H.; Smith, D.E.; Kadonaga, J.T. Identification of a Rapidly Formed Nonnucleosomal Histone-DNA Intermediate that Is Converted into Chromatin by ACF. Mol. Cell 2011, 43, 638-648.
    • (2011) Mol. Cell , vol.43 , pp. 638-648
    • Torigoe, S.E.1    Urwin, D.L.2    Ishii, H.3    Smith, D.E.4    Kadonaga, J.T.5
  • 60
    • 0242495784 scopus 로고    scopus 로고
    • Replication-independent assembly of nucleosome arrays in a novel yeast chromatin reconstitution system involves antisilencing factor Asf1p and chromodomain protein Chd1p
    • Robinson, K.M.; Schultz, M.C. Replication-independent assembly of nucleosome arrays in a novel yeast chromatin reconstitution system involves antisilencing factor Asf1p and chromodomain protein Chd1p. Mol. Cell. Biol. 2003, 23, 7937-7946.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7937-7946
    • Robinson, K.M.1    Schultz, M.C.2
  • 61
    • 0942290537 scopus 로고    scopus 로고
    • Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo
    • Fyodorov, D.V.; Blower, M.D.; Karpen, G.H.; Kadonaga, J.T. Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo. Genes Dev. 2004, 18, 170-183.
    • (2004) Genes Dev , vol.18 , pp. 170-183
    • Fyodorov, D.V.1    Blower, M.D.2    Karpen, G.H.3    Kadonaga, J.T.4
  • 63
    • 0036899341 scopus 로고    scopus 로고
    • An ACF1-ISWI chromatin-remodeling complex is required for DNA replication through heterochromatin
    • Collins, N.; Poot, R.A.; Kukimoto, I.; Garcia-Jimenez, C.; Dellaire, G.; Varga-Weisz, P.D. An ACF1-ISWI chromatin-remodeling complex is required for DNA replication through heterochromatin. Nat. Genet. 2002, 32, 627-632.
    • (2002) Nat. Genet , vol.32 , pp. 627-632
    • Collins, N.1    Poot, R.A.2    Kukimoto, I.3    Garcia-Jimenez, C.4    Dellaire, G.5    Varga-Weisz, P.D.6
  • 64
    • 0036565656 scopus 로고    scopus 로고
    • WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci
    • Bozhenok, L.; Wade, P.A.; Varga-Weisz, P. WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci. EMBO J. 2002, 21, 2231-2241.
    • (2002) EMBO J , vol.21 , pp. 2231-2241
    • Bozhenok, L.1    Wade, P.A.2    Varga-Weisz, P.3
  • 66
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma, F.; Koller, T.; Klug, A. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J. Cell Biol. 1979, 83, 403-427.
    • (1979) J. Cell Biol , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 67
    • 0018581746 scopus 로고
    • Metaphase chromosome structure: Evidence for a radial loop model
    • Marsden, M.P.; Laemmli, U.K. Metaphase chromosome structure: evidence for a radial loop model. Cell 1979, 17, 849-858.
    • (1979) Cell , vol.17 , pp. 849-858
    • Marsden, M.P.1    Laemmli, U.K.2
  • 68
    • 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
  • 69
    • 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
  • 70
    • 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
  • 71
    • 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
  • 73
    • 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. 1994, 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
  • 74
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura, H.; Cook, P.R. Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B. J. Cell Biol. 2001, 153, 1341-1353.
    • (2001) J. Cell Biol , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 75
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli, T.; Gunjan, A.; Hock, R.; Bustin, M.; Brown, D.T. Dynamic binding of histone H1 to chromatin in living cells. Nature 2000, 408, 877-881.
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 76
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever, M.A.; Th'Ng, J.P.; Sun, X.; Hendzel, M.J. Rapid exchange of histone H1.1 on chromatin in living human cells. Nature 2000, 408, 873-876.
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'Ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 77
    • 70349323113 scopus 로고    scopus 로고
    • Drosophila ISWI regulates the association of histone H1 with interphase chromosomes in vivo
    • Siriaco, G.; Deuring, R.; Chioda, M.; Becker, P.B.; Tamkun, J.W. Drosophila ISWI regulates the association of histone H1 with interphase chromosomes in vivo. Genetics 2009, 182, 661-669.
    • (2009) Genetics , vol.182 , pp. 661-669
    • Siriaco, G.1    Deuring, R.2    Chioda, M.3    Becker, P.B.4    Tamkun, J.W.5
  • 78
    • 0348166012 scopus 로고    scopus 로고
    • Chromatin assembly in vitro with purified recombinant ACF and NAP-1
    • Fyodorov, D.V.; Kadonaga, J.T. Chromatin assembly in vitro with purified recombinant ACF and NAP-1. Methods Enzymol. 2003, 371, 499-515.
    • (2003) Methods Enzymol , vol.371 , pp. 499-515
    • Fyodorov, D.V.1    Kadonaga, J.T.2
  • 79
    • 40949150335 scopus 로고    scopus 로고
    • ACF catalyses chromatosome movements in chromatin fibres
    • Maier, V.K.; Chioda, M.; Rhodes, D.; Becker, P.B. ACF catalyses chromatosome movements in chromatin fibres. EMBO J. 2008, 27, 817-826.
    • (2008) EMBO J , vol.27 , pp. 817-826
    • Maier, V.K.1    Chioda, M.2    Rhodes, D.3    Becker, P.B.4
  • 82
    • 0037115473 scopus 로고    scopus 로고
    • Biological functions of the ISWI chromatin remodeling complex NURF
    • Badenhorst, P.; Voas, M.; Rebay, I.; Wu, C. Biological functions of the ISWI chromatin remodeling complex NURF. Genes Dev. 2002, 16, 3186-3198.
    • (2002) Genes Dev , vol.16 , pp. 3186-3198
    • Badenhorst, P.1    Voas, M.2    Rebay, I.3    Wu, C.4
  • 83
    • 34547135224 scopus 로고    scopus 로고
    • Regional control of chromatin organization by noncoding roX RNAs and the NURF remodeling complex in Drosophila melanogaster
    • Bai, X.; Larschan, E.; Kwon, S.Y.; Badenhorst, P.; Kuroda, M.I. Regional control of chromatin organization by noncoding roX RNAs and the NURF remodeling complex in Drosophila melanogaster. Genetics 2007, 176, 1491-1499.
    • (2007) Genetics , vol.176 , pp. 1491-1499
    • Bai, X.1    Larschan, E.2    Kwon, S.Y.3    Badenhorst, P.4    Kuroda, M.I.5
  • 85
    • 61449102557 scopus 로고    scopus 로고
    • Linker histone H1 is essential for Drosophila development, the establishment of pericentric heterochromatin, and a normal polytene chromosome structure
    • Lu, X.; Wontakal, S.N.; Emelyanov, A.V.; Morcillo, P.; Konev, A.Y.; Fyodorov, D.V.; Skoultchi, A.I. Linker histone H1 is essential for Drosophila development, the establishment of pericentric heterochromatin, and a normal polytene chromosome structure. Genes Dev. 2009, 23, 452-465.
    • (2009) Genes Dev , vol.23 , pp. 452-465
    • Lu, X.1    Wontakal, S.N.2    Emelyanov, A.V.3    Morcillo, P.4    Konev, A.Y.5    Fyodorov, D.V.6    Skoultchi, A.I.7
  • 86
    • 21244491441 scopus 로고    scopus 로고
    • Regulation of histone synthesis and nucleosome assembly
    • Gunjan, A.; Paik, J.; Verreault, A. Regulation of histone synthesis and nucleosome assembly. Biochimie 2005, 87, 625-635.
    • (2005) Biochimie , vol.87 , pp. 625-635
    • Gunjan, A.1    Paik, J.2    Verreault, A.3
  • 87
    • 27144544622 scopus 로고    scopus 로고
    • Assembly of variant histones into chromatin
    • Henikoff, S.; Ahmad, K. Assembly of variant histones into chromatin. Annu. Rev. Cell Dev. Biol. 2005, 21, 133-153.
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 133-153
    • Henikoff, S.1    Ahmad, K.2
  • 88
    • 0023404906 scopus 로고
    • Changes in histones H2A and H3 variant composition in differentiating and mature rat brain cortical neurons
    • Pina, B.; Suau, P. Changes in histones H2A and H3 variant composition in differentiating and mature rat brain cortical neurons. Dev. Biol. 1987, 123, 51-58.
    • (1987) Dev. Biol , vol.123 , pp. 51-58
    • Pina, B.1    Suau, P.2
  • 89
    • 0037058948 scopus 로고    scopus 로고
    • Histone H3 variants specify modes of chromatin assembly
    • Ahmad, K.; Henikoff, S. Histone H3 variants specify modes of chromatin assembly. Proc. Natl. Acad. Sci. USA 2002, 99, 16477-16484.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16477-16484
    • Ahmad, K.1    Henikoff, S.2
  • 90
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly
    • Ahmad, K.; Henikoff, S. The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol. Cell 2002, 9, 1191-1200.
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 91
    • 33750740399 scopus 로고    scopus 로고
    • The nucleosome: A little variation goes a long way
    • Bernstein, E.; Hake, S.B. The nucleosome: a little variation goes a long way. Biochem. Cell Biol. 2006, 84, 505-517.
    • (2006) Biochem. Cell Biol , vol.84 , pp. 505-517
    • Bernstein, E.1    Hake, S.B.2
  • 92
    • 77949874234 scopus 로고    scopus 로고
    • Histone variants-ancient wrap artists of the epigenome
    • Talbert, P.B.; Henikoff, S. Histone variants-ancient wrap artists of the epigenome. Nat. Rev. Mol. Cell Biol. 2010, 11, 264-275.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 264-275
    • Talbert, P.B.1    Henikoff, S.2
  • 95
    • 65249119727 scopus 로고    scopus 로고
    • Frodos found: Behold the CENP-a ''Ring'' bearers
    • Mellone, B.G.; Zhang, W.; Karpen, G.H. Frodos found: Behold the CENP-a ''Ring'' bearers. Cell 2009, 137, 409-412.
    • (2009) Cell , vol.137 , pp. 409-412
    • Mellone, B.G.1    Zhang, W.2    Karpen, G.H.3
  • 96
    • 33644866511 scopus 로고    scopus 로고
    • Chromatin assembly: A basic recipe with various flavours
    • Polo, S.E.; Almouzni, G. Chromatin assembly: a basic recipe with various flavours. Curr. Opin. Genet. Dev. 2006, 16, 104-111.
    • (2006) Curr. Opin. Genet. Dev , vol.16 , pp. 104-111
    • Polo, S.E.1    Almouzni, G.2
  • 97
    • 34548433964 scopus 로고    scopus 로고
    • Marking histone H3 variants: How, when and why?
    • Loyola, A.; Almouzni, G. Marking histone H3 variants: how, when and why? Trends Biochem. Sci. 2007, 32, 425-433.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 425-433
    • Loyola, A.1    Almouzni, G.2
  • 99
    • 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
  • 101
    • 68149150830 scopus 로고    scopus 로고
    • H3.3/H2A.Z double variant-containing nucleosomes mark ''nucleosome-free regions'' of active promoters and other regulatory regions
    • Jin, C.; Zang, C.; Wei, G.; Cui, K.; Peng, W.; Zhao, K.; Felsenfeld, G. H3.3/H2A.Z double variant-containing nucleosomes mark ''nucleosome-free regions'' of active promoters and other regulatory regions. Nat. Genet. 2009, 41, 941-945.
    • (2009) Nat. Genet , vol.41 , pp. 941-945
    • Jin, C.1    Zang, C.2    Wei, G.3    Cui, K.4    Peng, W.5    Zhao, K.6    Felsenfeld, G.7
  • 102
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profiling of histone H3.3 replacement patterns
    • Mito, Y.; Henikoff, J.G.; Henikoff, S. Genome-scale profiling of histone H3.3 replacement patterns. Nat. Genet. 2005, 37, 1090-1097.
    • (2005) Nat. Genet , vol.37 , pp. 1090-1097
    • Mito, Y.1    Henikoff, J.G.2    Henikoff, S.3
  • 103
    • 71849103121 scopus 로고    scopus 로고
    • Transcriptional and developmental functions of the H3.3 histone variant in Drosophila
    • Sakai, A.; Schwartz, B.E.; Goldstein, S.; Ahmad, K. Transcriptional and developmental functions of the H3.3 histone variant in Drosophila. Curr. Biol. 2009, 19, 1816-1820.
    • (2009) Curr. Biol , vol.19 , pp. 1816-1820
    • Sakai, A.1    Schwartz, B.E.2    Goldstein, S.3    Ahmad, K.4
  • 104
    • 67650960676 scopus 로고    scopus 로고
    • Transcription in the absence of histone H3.3
    • Hodl, M.; Basler, K. Transcription in the absence of histone H3.3. Curr. Biol. 2009, 19, 1221-1226.
    • (2009) Curr. Biol , vol.19 , pp. 1221-1226
    • Hodl, M.1    Basler, K.2
  • 105
    • 27644515513 scopus 로고    scopus 로고
    • The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus
    • Loppin, B.; Bonnefoy, E.; Anselme, C.; Laurencon, A.; Karr, T.L.; Couble, P. The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus. Nature 2005, 437, 1386-1390.
    • (2005) Nature , vol.437 , pp. 1386-1390
    • Loppin, B.1    Bonnefoy, E.2    Anselme, C.3    Laurencon, A.4    Karr, T.L.5    Couble, P.6
  • 107
    • 35948990898 scopus 로고    scopus 로고
    • The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization
    • Bonnefoy, E.; Orsi, G.A.; Couble, P.; Loppin, B. The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization. PLoS Genet. 2007, 3, 1991-2006.
    • (2007) PLoS Genet , vol.3 , pp. 1991-2006
    • Bonnefoy, E.1    Orsi, G.A.2    Couble, P.3    Loppin, B.4
  • 111
    • 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
  • 112
    • 77953955724 scopus 로고    scopus 로고
    • The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3
    • Drane, P.; Ouararhni, K.; Depaux, A.; Shuaib, M.; Hamiche, A. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 2010, 24, 1253-1265.
    • (2010) Genes Dev , vol.24 , pp. 1253-1265
    • Drane, P.1    Ouararhni, K.2    Depaux, A.3    Shuaib, M.4    Hamiche, A.5
  • 113
    • 69249203534 scopus 로고    scopus 로고
    • Focus on the centre: The role of chromatin on the regulation of centromere identity and function
    • Torras-Llort, M.; Moreno-Moreno, O.; Azorin, F. Focus on the centre: the role of chromatin on the regulation of centromere identity and function. EMBO J. 2009, 28, 2337-2348.
    • (2009) EMBO J , vol.28 , pp. 2337-2348
    • Torras-Llort, M.1    Moreno-Moreno, O.2    Azorin, F.3
  • 115
    • 0035432975 scopus 로고    scopus 로고
    • Determining centromere identity: Cyclical stories and forking paths
    • Sullivan, B.A.; Blower, M.D.; Karpen, G.H. Determining centromere identity: cyclical stories and forking paths. Nat. Rev. Genet. 2001, 2, 584-596.
    • (2001) Nat. Rev. Genet , vol.2 , pp. 584-596
    • Sullivan, B.A.1    Blower, M.D.2    Karpen, G.H.3
  • 116
    • 56549108407 scopus 로고    scopus 로고
    • Epigenetic regulation of centromeric chromatin: Old dogs, new tricks?
    • Allshire, R.C.; Karpen, G.H. Epigenetic regulation of centromeric chromatin: old dogs, new tricks? Nat. Rev. Genet. 2008, 9, 923-937.
    • (2008) Nat. Rev. Genet , vol.9 , pp. 923-937
    • Allshire, R.C.1    Karpen, G.H.2
  • 120
    • 59649107021 scopus 로고    scopus 로고
    • Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin
    • Williams, J.S.; Hayashi, T.; Yanagida, M.; Russell, P. Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin. Mol. Cell 2009, 33, 287-298.
    • (2009) Mol. Cell , vol.33 , pp. 287-298
    • Williams, J.S.1    Hayashi, T.2    Yanagida, M.3    Russell, P.4
  • 122
    • 67549104312 scopus 로고    scopus 로고
    • Common ancestry of the CENP-A chaperones Scm3 and HJURP
    • Sanchez-Pulido, L.; Pidoux, A.L.; Ponting, C.P.; Allshire, R.C. Common ancestry of the CENP-A chaperones Scm3 and HJURP. Cell 2009, 137, 1173-1174.
    • (2009) Cell , vol.137 , pp. 1173-1174
    • Sanchez-Pulido, L.1    Pidoux, A.L.2    Ponting, C.P.3    Allshire, R.C.4
  • 123
    • 65649124957 scopus 로고    scopus 로고
    • Active establishment of centromeric CENP-A chromatin by RSF complex
    • Perpelescu, M.; Nozaki, N.; Obuse, C.; Yang, H.; Yoda, K. Active establishment of centromeric CENP-A chromatin by RSF complex. J. Cell Biol. 2009, 185, 397-407.
    • (2009) J. Cell Biol , vol.185 , pp. 397-407
    • Perpelescu, M.1    Nozaki, N.2    Obuse, C.3    Yang, H.4    Yoda, K.5
  • 124
    • 70350234665 scopus 로고    scopus 로고
    • CENP-H-containing complex facilitates centromere deposition of CENP-A in cooperation with FACT and CHD1
    • Okada, M.; Okawa, K.; Isobe, T.; Fukagawa, T. CENP-H-containing complex facilitates centromere deposition of CENP-A in cooperation with FACT and CHD1. Mol. Biol. Cell 2009, 20, 3986-3995.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3986-3995
    • Okada, M.1    Okawa, K.2    Isobe, T.3    Fukagawa, T.4
  • 127
    • 40149087385 scopus 로고    scopus 로고
    • RSF governs silent chromatin formation via histone H2Av replacement
    • Hanai, K.; Furuhashi, H.; Yamamoto, T.; Akasaka, K.; Hirose, S. RSF governs silent chromatin formation via histone H2Av replacement. PLoS Genet. 2008, 4, e1000011.
    • (2008) PLoS Genet , vol.4
    • Hanai, K.1    Furuhashi, H.2    Yamamoto, T.3    Akasaka, K.4    Hirose, S.5
  • 128
    • 58149305928 scopus 로고    scopus 로고
    • Genome-wide analysis reveals a cell cycle-dependent mechanism controlling centromere propagation
    • Erhardt, S.; Mellone, B.G.; Betts, C.M.; Zhang, W.; Karpen, G.H.; Straight, A.F. Genome-wide analysis reveals a cell cycle-dependent mechanism controlling centromere propagation. J. Cell Biol. 2008, 183, 805-818.
    • (2008) J. Cell Biol , vol.183 , pp. 805-818
    • Erhardt, S.1    Mellone, B.G.2    Betts, C.M.3    Zhang, W.4    Karpen, G.H.5    Straight, A.F.6
  • 129
    • 0029982345 scopus 로고    scopus 로고
    • Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae
    • Liu, X.; Bowen, J.; Gorovsky, M.A. Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 1996, 16, 2878-2887.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 2878-2887
    • Liu, X.1    Bowen, J.2    Gorovsky, M.A.3
  • 131
    • 0027058961 scopus 로고
    • A histone variant, H2AvD, is essential in Drosophila melanogaster
    • van Daal, A.; Elgin, S.C. A histone variant, H2AvD, is essential in Drosophila melanogaster. Mol. Biol. Cell 1992, 3, 593-602.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 593-602
    • van Daal, A.1    Elgin, S.C.2
  • 132
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R.K.; Clarkson, M.J.; Tremethick, D.J.; Luger, K. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 2000, 7, 1121-1124.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 133
    • 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
  • 134
    • 79959588969 scopus 로고    scopus 로고
    • Genomic Organization of H2Av Containing Nucleosomes in Drosophila Heterochromatin
    • Zhang, Z.; Pugh, B.F. Genomic Organization of H2Av Containing Nucleosomes in Drosophila Heterochromatin. PLoS One 2011, 6, e20511.
    • (2011) PLoS One , vol.6
    • Zhang, Z.1    Pugh, B.F.2
  • 135
    • 73349098753 scopus 로고    scopus 로고
    • The euchromatic and heterochromatic landscapes are shaped by antagonizing effects of transcription on H2A.Z deposition
    • Hardy, S.; Jacques, P.E.; Gevry, N.; Forest, A.; Fortin, M.E.; Laflamme, L.; Gaudreau, L.; Robert, F. The euchromatic and heterochromatic landscapes are shaped by antagonizing effects of transcription on H2A.Z deposition. PLoS Genet. 2009, 5, e1000687.
    • (2009) PLoS Genet , vol.5
    • Hardy, S.1    Jacques, P.E.2    Gevry, N.3    Forest, A.4    Fortin, M.E.5    Laflamme, L.6    Gaudreau, L.7    Robert, F.8
  • 136
    • 61849170193 scopus 로고    scopus 로고
    • Genome-wide profiling of salt fractions maps physical properties of chromatin
    • Henikoff, S.; Henikoff, J.G.; Sakai, A.; Loeb, G.B.; Ahmad, K. Genome-wide profiling of salt fractions maps physical properties of chromatin. Genome Res. 2009, 19, 460-469.
    • (2009) Genome Res , vol.19 , pp. 460-469
    • Henikoff, S.1    Henikoff, J.G.2    Sakai, A.3    Loeb, G.B.4    Ahmad, K.5
  • 137
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi, G.; Shen, X.; Landry, J.; Wu, W.H.; Sen, S.; Wu, C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 2004, 303, 343-348.
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 141
    • 78751536862 scopus 로고    scopus 로고
    • Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome
    • Luk, E.; Ranjan, A.; Fitzgerald, P.C.; Mizuguchi, G.; Huang, Y.; Wei, D.; Wu, C. Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome. Cell 2010, 143, 725-736.
    • (2010) Cell , vol.143 , pp. 725-736
    • Luk, E.1    Ranjan, A.2    Fitzgerald, P.C.3    Mizuguchi, G.4    Huang, Y.5    Wei, D.6    Wu, C.7
  • 142
    • 28544442465 scopus 로고    scopus 로고
    • Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
    • Wu, W.H.; Alami, S.; Luk, E.; Wu, C.H.; Sen, S.; Mizuguchi, G.; Wei, D.; Wu, C. Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat. Struct. Mol. Biol. 2005, 12, 1064-1071.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 1064-1071
    • Wu, W.H.1    Alami, S.2    Luk, E.3    Wu, C.H.4    Sen, S.5    Mizuguchi, G.6    Wei, D.7    Wu, C.8
  • 143
    • 78651510784 scopus 로고    scopus 로고
    • Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity
    • Papamichos-Chronakis, M.; Watanabe, S.; Rando, O.J.; Peterson, C.L. Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity. Cell 2011, 144, 200-213.
    • (2011) Cell , vol.144 , pp. 200-213
    • Papamichos-Chronakis, M.1    Watanabe, S.2    Rando, O.J.3    Peterson, C.L.4
  • 144
    • 12544258222 scopus 로고    scopus 로고
    • Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
    • Park, Y.J.; Chodaparambil, J.V.; Bao, Y.; McBryant, S.J.; Luger, K. Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding. J. Biol. Chem. 2005, 280, 1817-1825.
    • (2005) J. Biol. Chem , vol.280 , pp. 1817-1825
    • Park, Y.J.1    Chodaparambil, J.V.2    Bao, Y.3    McBryant, S.J.4    Luger, K.5
  • 146
    • 73549118786 scopus 로고    scopus 로고
    • Nap1 and Chz1 have separate Htz1 nuclear import and assembly functions
    • Straube, K.; Blackwell, J.S., Jr.; Pemberton, L.F. Nap1 and Chz1 have separate Htz1 nuclear import and assembly functions. Traffic 2010, 11, 185-197.
    • (2010) Traffic , vol.11 , pp. 185-197
    • Straube, K.1    Blackwell Jr., J.S.2    Pemberton, L.F.3
  • 147
    • 74549187994 scopus 로고    scopus 로고
    • Nuclear functions of the HMG proteins
    • Reeves, R. Nuclear functions of the HMG proteins. Biochim. Biophys. Acta 2010, 1799, 3-14.
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 3-14
    • Reeves, R.1
  • 148
    • 24344498241 scopus 로고    scopus 로고
    • HMG proteins: Dynamic players in gene regulation and differentiation
    • Bianchi, M.E.; Agresti, A. HMG proteins: dynamic players in gene regulation and differentiation. Curr. Opin. Genet. Dev. 2005, 15, 496-506.
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 496-506
    • Bianchi, M.E.1    Agresti, A.2
  • 149
    • 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
  • 150
    • 2942596544 scopus 로고    scopus 로고
    • Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin
    • Catez, F.; Yang, H.; Tracey, K.J.; Reeves, R.; Misteli, T.; Bustin, M. Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin. Mol. Cell. Biol. 2004, 24, 4321-4328.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 4321-4328
    • Catez, F.1    Yang, H.2    Tracey, K.J.3    Reeves, R.4    Misteli, T.5    Bustin, M.6
  • 151
    • 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
  • 152
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: Three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • Phair, R.D.; Scaffidi, P.; Elbi, C.; Vecerova, J.; Dey, A.; Ozato, K.; Brown, D.T.; Hager, G.; Bustin, M.; Misteli, T. Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins. Mol. Cell. Biol. 2004, 24, 6393-6402.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerova, J.4    Dey, A.5    Ozato, K.6    Brown, D.T.7    Hager, G.8    Bustin, M.9    Misteli, T.10
  • 153
    • 66449110070 scopus 로고    scopus 로고
    • HMGN proteins act in opposition to ATP-dependent chromatin remodeling factors to restrict nucleosome mobility
    • Rattner, B.P.; Yusufzai, T.; Kadonaga, J.T. HMGN proteins act in opposition to ATP-dependent chromatin remodeling factors to restrict nucleosome mobility. Mol. Cell 2009, 34, 620-626.
    • (2009) Mol. Cell , vol.34 , pp. 620-626
    • Rattner, B.P.1    Yusufzai, T.2    Kadonaga, J.T.3
  • 154
    • 0342514792 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of the ATRX protein correlates with changes in nuclear matrix and chromatin association
    • Berube, N.G.; Smeenk, C.A.; Picketts, D.J. Cell cycle-dependent phosphorylation of the ATRX protein correlates with changes in nuclear matrix and chromatin association. Hum. Mol. Genet. 2000, 9, 539-547.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 539-547
    • Berube, N.G.1    Smeenk, C.A.2    Picketts, D.J.3
  • 155
    • 18844432121 scopus 로고    scopus 로고
    • The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain
    • Lechner, M.S.; Schultz, D.C.; Negorev, D.; Maul, G.G.; Rauscher, F.J., 3rd. The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain. Biochem. Biophys. Res. Commun. 2005, 331, 929-937.
    • (2005) Biochem. Biophys. Res. Commun , vol.331 , pp. 929-937
    • Lechner, M.S.1    Schultz, D.C.2    Negorev, D.3    Maul, G.G.4    Rauscher III, F.J.5
  • 157
    • 77952025217 scopus 로고    scopus 로고
    • Protein complex of Drosophila ATRX/XNP and HP1a is required for the formation of pericentric beta-heterochromatin in vivo
    • Emelyanov, A.V.; Konev, A.Y.; Vershilova, E.; Fyodorov, D.V. Protein complex of Drosophila ATRX/XNP and HP1a is required for the formation of pericentric beta-heterochromatin in vivo. J. Biol. Chem. 2010, 285, 15027-15037.
    • (2010) J. Biol. Chem , vol.285 , pp. 15027-15037
    • Emelyanov, A.V.1    Konev, A.Y.2    Vershilova, E.3    Fyodorov, D.V.4
  • 158
    • 33846130043 scopus 로고    scopus 로고
    • HP1 binding to chromatin methylated at H3K9 is enhanced by auxiliary factors
    • Eskeland, R.; Eberharter, A.; Imhof, A. HP1 binding to chromatin methylated at H3K9 is enhanced by auxiliary factors. Mol. Cell. Biol. 2007, 27, 453-465.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 453-465
    • Eskeland, R.1    Eberharter, A.2    Imhof, A.3
  • 159
    • 33646239638 scopus 로고    scopus 로고
    • Histone H3 variants and their potential role in indexing mammalian genomes: The ''H3 barcode hypothesis
    • Hake, S.B.; Allis, C.D. Histone H3 variants and their potential role in indexing mammalian genomes: the ''H3 barcode hypothesis''. Proc. Natl. Acad. Sci. USA 2006, 103, 6428-6435.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6428-6435
    • Hake, S.B.1    Allis, C.D.2
  • 160
    • 2942746179 scopus 로고    scopus 로고
    • Histone variants, nucleosome assembly and epigenetic inheritance
    • Henikoff, S.; Furuyama, T.; Ahmad, K. Histone variants, nucleosome assembly and epigenetic inheritance. Trends Genet. 2004, 20, 320-326.
    • (2004) Trends Genet , vol.20 , pp. 320-326
    • Henikoff, S.1    Furuyama, T.2    Ahmad, K.3


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