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Volumn 10, Issue 11, 2003, Pages 882-891

Phylogenomics of the nucleosome

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HISTONE; HISTONE H2A; HISTONE H3;

EID: 0242407193     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb996     Document Type: Review
Times cited : (467)

References (70)
  • 1
    • 0025301592 scopus 로고
    • HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones
    • Sandman, K. et al. HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. Proc. Natl. Acad. Sci. USA 87, 5788-5791 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5788-5791
    • Sandman, K.1
  • 2
    • 0032426951 scopus 로고    scopus 로고
    • Diversity of prokaryotic chromosomal proteins and the origin of the nucleosome
    • Sandman, K., Pereira, S.L. & Reeve, J.N. Diversity of prokaryotic chromosomal proteins and the origin of the nucleosome. Cell. Mol. Life Sci. 54, 1350-1364 (1998).
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 1350-1364
    • Sandman, K.1    Pereira, S.L.2    Reeve, J.N.3
  • 3
  • 4
    • 0025885691 scopus 로고
    • DNA binding by the archaeal histone HMf results in positive supercoiling
    • Musgrave, D.R., Sandman, K.M. & Reeve, J.N. DNA binding by the archaeal histone HMf results in positive supercoiling. Proc. Natl. Acad. Sci. USA 88, 10397-10401 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10397-10401
    • Musgrave, D.R.1    Sandman, K.M.2    Reeve, J.N.3
  • 5
    • 0028604578 scopus 로고
    • Growth-phase-dependent synthesis of histones in the archaeon Methanothermus fervidus
    • Sandman, K. et al. Growth-phase-dependent synthesis of histones in the archaeon Methanothermus fervidus. Proc. Natl. Acad. Sci. USA 91, 12624-12628 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12624-12628
    • Sandman, K.1
  • 6
    • 0032518154 scopus 로고    scopus 로고
    • Evidence for an early prokaryotic origin of histones H 2A and H4 prior to the emergence of eukaryotes
    • Slesarev, A.I. et al. Evidence for an early prokaryotic origin of histones H2A and H4 prior to the emergence of eukaryotes. Nucleic Acids Res. 26, 427-430 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 427-430
    • Slesarev, A.I.1
  • 7
    • 12944270421 scopus 로고    scopus 로고
    • Genome sequence of Halobacterium species NRC-1
    • Ng, W.V. et al. Genome sequence of Halobacterium species NRC-1. Proc. Natl. Acad. Sci. USA 97, 12176-12181 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12176-12181
    • Ng, W.V.1
  • 8
    • 0034802612 scopus 로고    scopus 로고
    • An ancestral nuclear protein assembly: Crystal structure of the Methanopyrus kandleri histone
    • Fahrner, R.L. et al. An ancestral nuclear protein assembly: crystal structure of the Methanopyrus kandleri histone. Protein Sci. 10, 2002-2007 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 2002-2007
    • Fahrner, R.L.1
  • 9
    • 0034644722 scopus 로고    scopus 로고
    • Crystal structures of recombinant histones HMfA and HMfB from the hyperthermophilic archaeon Methanothermus fervidus
    • Decanniere, K. et al. Crystal structures of recombinant histones HMfA and HMfB from the hyperthermophilic archaeon Methanothermus fervidus. J. Mol. Biol. 303, 35-47 (2000).
    • (2000) J. Mol. Biol. , vol.303 , pp. 35-47
    • Decanniere, K.1
  • 10
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K. et al. Crystal structure of the nucleosome core particle at 2. 8 Å resolution. Nature 389, 251-260 (1997).
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1
  • 11
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents, G. et al. The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. USA 88, 10148-10152 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10148-10152
    • Arents, G.1
  • 12
    • 0029881897 scopus 로고    scopus 로고
    • Parallel origins of the nucleosome core and eukaryotic transcription from Archaea
    • Ouzounis, C.A. & Kyrpides, N.C. Parallel origins of the nucleosome core and eukaryotic transcription from Archaea. J. Mol. Evol. 42, 234-239 (1996).
    • (1996) J. Mol. Evol. , vol.42 , pp. 234-239
    • Ouzounis, C.A.1    Kyrpides, N.C.2
  • 13
    • 0018267877 scopus 로고
    • The histone core complex: An octamer assembled by two sets of protein-protein interactions
    • Eickbush, T.H. & Moudrianakis, E.N. The histone core complex: an octamer assembled by two sets of protein-protein interactions. Biochemistry 17, 4955-4964 (1978).
    • (1978) Biochemistry , vol.17 , pp. 4955-4964
    • Eickbush, T.H.1    Moudrianakis, E.N.2
  • 15
    • 0020358561 scopus 로고
    • Patterns of histone variant synthesis can distinguish G 0 from G1 cells
    • Wu, R.S., Tsai, S. & Bonner, W.M. Patterns of histone variant synthesis can distinguish G0 from G1 cells. Cell 31, 367-374 (1982).
    • (1982) Cell , vol.31 , pp. 367-374
    • Wu, R.S.1    Tsai, S.2    Bonner, W.M.3
  • 16
    • 0028826921 scopus 로고
    • Changes in core histone variant composition in differentiating neurons: The roles of differential turnover and synthesis rates
    • Bosch, A. & Suau, P. Changes in core histone variant composition in differentiating neurons: the roles of differential turnover and synthesis rates. Eur. J. Cell Biol. 68, 220-225 (1995).
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 220-225
    • Bosch, A.1    Suau, P.2
  • 17
    • 0028270693 scopus 로고
    • Independent evolutionary origin of histone H3.3-like variants of animals and Tetrahymena
    • Thatcher, T.H. et al. Independent evolutionary origin of histone H3.3-like variants of animals and Tetrahymena. Nucleic Acids Res. 22, 180-186 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 180-186
    • Thatcher, T.H.1
  • 18
    • 0029810308 scopus 로고    scopus 로고
    • Common features of analogous replacement histone H3 genes in animals and plants
    • Waterborg, J.H. & Robertson, A.J. Common features of analogous replacement histone H3 genes in animals and plants. J. Mol. Evol. 43, 194-206 (1996).
    • (1996) J. Mol. Evol. , vol.43 , pp. 194-206
    • Waterborg, J.H.1    Robertson, A.J.2
  • 19
    • 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 9, 1191-1200 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 20
    • 0030881925 scopus 로고    scopus 로고
    • Constitutive expression, not a particular primary sequence, is the important feature of the H3 replacement variant hv2 in Tetrahymena thermophila
    • Yu, L. & Gorovsky, M.A. Constitutive expression, not a particular primary sequence, is the important feature of the H3 replacement variant hv2 in Tetrahymena thermophila. Mol. Cell. Biol. 17, 6303-6310 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6303-6310
    • Yu, L.1    Gorovsky, M.A.2
  • 21
    • 0033615555 scopus 로고    scopus 로고
    • Histone H1 and evolution of sperm nuclear basic proteins
    • Ausio, J. Histone H1 and evolution of sperm nuclear basic proteins. J. Biol. Chem. 274, 31115-31118 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31115-31118
    • Ausio, J.1
  • 22
    • 0038718573 scopus 로고    scopus 로고
    • Chromosomal proteins in the spermatogenesis of Drosophila
    • Hennig, W. Chromosomal proteins in the spermatogenesis of Drosophila. Chromosoma 111, 489-494 (2003).
    • (2003) Chromosoma , vol.111 , pp. 489-494
    • Hennig, W.1
  • 23
    • 0023275058 scopus 로고
    • A 17-kD centromere protein (CENP-A) copurifies with nucleosome core particles and with histones
    • Palmer, D.K. et al. A 17-kD centromere protein (CENP-A) copurifies with nucleosome core particles and with histones. J. Cell Biol. 104, 805-815 (1987).
    • (1987) J. Cell Biol. , vol.104 , pp. 805-815
    • Palmer, D.K.1
  • 24
    • 0025763392 scopus 로고
    • Purification of the centromere-specific protein CENP-A and demonstration that it is a distinctive histone
    • Palmer, D.K. et al. Purification of the centromere-specific protein CENP-A and demonstration that it is a distinctive histone. Proc. Natl. Acad. Sci. USA 88, 3734-3738 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3734-3738
    • Palmer, D.K.1
  • 25
    • 0035839066 scopus 로고    scopus 로고
    • The centromere paradox: Stable inheritance with rapidly evolving DNA
    • Henikoff, S., Ahmad, K. & Malik, H.S. The centromere paradox: stable inheritance with rapidly evolving DNA. Science 293, 1098-1102 (2001).
    • (2001) Science , vol.293 , pp. 1098-1102
    • Henikoff, S.1    Ahmad, K.2    Malik, H.S.3
  • 26
    • 0037022285 scopus 로고    scopus 로고
    • Recurrent evolution of DNA-binding motifs in the Drosophila centromeric histone
    • Malik, H.S., Vermaak, D. & Henikoff, S. Recurrent evolution of DNA-binding motifs in the Drosophila centromeric histone. Proc. Natl. Acad. Sci. USA 99, 1449-1454 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1449-1454
    • Malik, H.S.1    Vermaak, D.2    Henikoff, S.3
  • 27
    • 0036429193 scopus 로고    scopus 로고
    • The human and mouse replication-dependent histone genes
    • Marzluff, W.F. et al. The human and mouse replication-dependent histone genes. Genomics 80, 487-498 (2002).
    • (2002) Genomics , vol.80 , pp. 487-498
    • Marzluff, W.F.1
  • 28
    • 0028946805 scopus 로고
    • A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis
    • Stoler, S. et al. A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis. Genes Dev. 9, 573-586 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 573-586
    • Stoler, S.1
  • 29
    • 0033533848 scopus 로고    scopus 로고
    • A histone-H3-like protein in C. elegans
    • Buchwitz, B.J. et al. A histone-H3-like protein in C. elegans. Nature 401, 547-548 (1999).
    • (1999) Nature , vol.401 , pp. 547-548
    • Buchwitz, B.J.1
  • 30
    • 0034681115 scopus 로고    scopus 로고
    • Heterochromatic deposition of centromeric histone H3-like proteins
    • Henikoff, S. et al. Heterochromatic deposition of centromeric histone H3-like proteins. Proc. Natl. Acad. Sci. USA 97, 716-721 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 716-721
    • Henikoff, S.1
  • 31
    • 0342646931 scopus 로고    scopus 로고
    • Requirement of Mis6 centromere connector for localizing a CENP-A-like protein in fission yeast
    • Takahashi, K., Chen, E.S. & Yanagida, M. Requirement of Mis6 centromere connector for localizing a CENP-A-like protein in fission yeast. Science 288, 2215-2219 (2000).
    • (2000) Science , vol.288 , pp. 2215-2219
    • Takahashi, K.1    Chen, E.S.2    Yanagida, M.3
  • 32
    • 0036016437 scopus 로고    scopus 로고
    • Centromeric localization and adaptive evolution of an Arabidopsis histone H3 variant
    • Talbert, P.B. et al. Centromeric localization and adaptive evolution of an Arabidopsis histone H3 variant. Plant Cell 14, 1053-1066 (2002).
    • (2002) Plant Cell , vol.14 , pp. 1053-1066
    • Talbert, P.B.1
  • 33
    • 0031049028 scopus 로고    scopus 로고
    • Assembly of CENP-A into centromeric chromatin requires a cooperative array of nucleosomal DNA contact sites
    • Shelby, R.D., Vafa, O. & Sullivan, K.F. Assembly of CENP-A into centromeric chromatin requires a cooperative array of nucleosomal DNA contact sites. J. Cell Biol. 136, 501-513 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 501-513
    • Shelby, R.D.1    Vafa, O.2    Sullivan, K.F.3
  • 34
    • 0036837686 scopus 로고    scopus 로고
    • Centromere targeting element within the histone fold domain of Cid
    • Vermaak, D., Hayden, H.S. & Henikoff, S. Centromere targeting element within the histone fold domain of Cid. Mol. Cell. Biol. 22, 7553-7561 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7553-7561
    • Vermaak, D.1    Hayden, H.S.2    Henikoff, S.3
  • 35
    • 0035103847 scopus 로고    scopus 로고
    • Adaptive evolution of Cid, a centromere-specific histone in Drosophila
    • Malik, H.S. & Henikoff, S. Adaptive evolution of Cid, a centromere-specific histone in Drosophila. Genetics 157, 1293-1298 (2001).
    • (2001) Genetics , vol.157 , pp. 1293-1298
    • Malik, H.S.1    Henikoff, S.2
  • 36
    • 0033811682 scopus 로고    scopus 로고
    • The N terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain
    • Chen, Y. et al. The N terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain. Mol. Cell. Biol. 20, 7037-7048 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7037-7048
    • Chen, Y.1
  • 37
    • 0033977617 scopus 로고    scopus 로고
    • Evidence from β-tubulin phylogeny that microsporidia evolved from within the fungi
    • Keeling, P.J., Luker, M.A. & Palmer, J.D. Evidence from β-tubulin phylogeny that microsporidia evolved from within the fungi. Mol. Biol. Evol. 17, 23-31 (2000).
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 23-31
    • Keeling, P.J.1    Luker, M.A.2    Palmer, J.D.3
  • 38
    • 0034049167 scopus 로고    scopus 로고
    • Unusual core histones specifically expressed in male gametic cells of Lilium longiflorum
    • Ueda, K. et al. Unusual core histones specifically expressed in male gametic cells of Lilium longiflorum. Chromosoma 108, 491-500 (2000).
    • (2000) Chromosoma , vol.108 , pp. 491-500
    • Ueda, K.1
  • 39
    • 0031037692 scopus 로고    scopus 로고
    • An unusual histone H 3 specific for early macronuclear development in Euplotes crassus
    • Jahn, C.L. et al. An unusual histone H3 specific for early macronuclear development in Euplotes crassus. Proc. Natl. Acad. Sci. USA 94, 1332-1337 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1332-1337
    • Jahn, C.L.1
  • 40
    • 0035953753 scopus 로고    scopus 로고
    • The highly reduced genome of an enslaved algal nucleus
    • Douglas, S. et al. The highly reduced genome of an enslaved algal nucleus. Nature 410, 1091-1096 (2001).
    • (2001) Nature , vol.410 , pp. 1091-1096
    • Douglas, S.1
  • 41
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R.K. et al. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 7, 1121-1124 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1
  • 42
    • 0019319471 scopus 로고
    • Histone 2A, a heteromorphous family of eight protein species
    • West, M.H. & Bonner, W.M. Histone 2A, a heteromorphous family of eight protein species. Biochemistry 19, 3238-3245 (1980).
    • (1980) Biochemistry , vol.19 , pp. 3238-3245
    • West, M.H.1    Bonner, W.M.2
  • 43
    • 0026737922 scopus 로고
    • MacroH 2A, a core histone containing a large nonhistone region
    • Pehrson, J.R. & Fried, V.A. MacroH2A, a core histone containing a large nonhistone region. Science 257, 1398-1400 (1992).
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 44
    • 0035931749 scopus 로고    scopus 로고
    • A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
    • Chadwick, B.P. & Willard, H.F. A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. J. Cell Biol. 152, 375-384 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 375-384
    • Chadwick, B.P.1    Willard, H.F.2
  • 45
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou, E.P. et al. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273, 5858-5868 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1
  • 46
    • 0034623860 scopus 로고    scopus 로고
    • Response to RAG-mediated VDJ cleavage by NBS1 and γ-H2AX
    • Chen, H.T. et al. Response to RAG-mediated VDJ cleavage by NBS1 and γ-H2AX. Science 290, 1962-1965 (2000).
    • (2000) Science , vol.290 , pp. 1962-1965
    • Chen, H.T.1
  • 47
    • 0035097808 scopus 로고    scopus 로고
    • Recombinational DNA double-strand breaks in mice precede synapsis
    • Mahadevaiah, S.K. et al. Recombinational DNA double-strand breaks in mice precede synapsis. Nat. Genet. 27, 271-276 (2001).
    • (2001) Nat. Genet. , vol.27 , pp. 271-276
    • Mahadevaiah, S.K.1
  • 48
    • 0034737439 scopus 로고    scopus 로고
    • Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139
    • Rogakou, E.P. et al. Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139. J. Biol. Chem. 275, 9390-9395 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 9390-9395
    • Rogakou, E.P.1
  • 49
    • 0037711771 scopus 로고    scopus 로고
    • Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks
    • Celeste, A. et al. Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks. Nat. Cell Biol. 5, 675-679 (2003).
    • (2003) Nat. Cell Biol. , vol.5 , pp. 675-679
    • Celeste, A.1
  • 50
    • 0032861343 scopus 로고    scopus 로고
    • Megabase chromatin domains involved in DNA double-strand breaks in vivo
    • Rogakou, E.P. et al. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol. 146, 905-916 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 905-916
    • Rogakou, E.P.1
  • 51
    • 0028231021 scopus 로고
    • Phylogenetic analysis of the core histones H2A, H2B, H3, and H4
    • Thatcher, T.H. & Gorovsky, M.A. Phylogenetic analysis of the core histones H2A, H2B, H3, and H4. Nucleic Acids Res. 22, 174-179 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 174-179
    • Thatcher, T.H.1    Gorovsky, M.A.2
  • 52
    • 0024041943 scopus 로고
    • Circular ribosomal DNA plasmids transform Tetrahymena thermophila by homologous recombination with endogenous macronuclear ribosomal DNA
    • Yu, G.L., Hasson, M. & Blackburn, E.H. Circular ribosomal DNA plasmids transform Tetrahymena thermophila by homologous recombination with endogenous macronuclear ribosomal DNA. Proc. Natl. Acad. Sci. USA 85, 5151-5155 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5151-5155
    • Yu, G.L.1    Hasson, M.2    Blackburn, E.H.3
  • 53
    • 0346634937 scopus 로고    scopus 로고
    • H2AX is required for chromatin remodeling and inactivation of sex chromosomes in male mouse meiosis
    • Fernandez-Capetillo, O. et al. H2AX is required for chromatin remodeling and inactivation of sex chromosomes in male mouse meiosis. Dev. Cell 4, 497-508 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 497-508
    • Fernandez-Capetillo, O.1
  • 54
    • 0023032792 scopus 로고
    • hv1 is an evolutionarily conserved H2A variant that is preferentially associated with active genes
    • Allis, C.D. et al. hv1 is an evolutionarily conserved H2A variant that is preferentially associated with active genes. J. Biol. Chem. 261, 1941-1948 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 1941-1948
    • Allis, C.D.1
  • 55
    • 0034307468 scopus 로고    scopus 로고
    • Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants
    • Jackson, J.D. & Gorovsky, M.A. Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucleic Acids Res. 28, 3811-3816 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3811-3816
    • Jackson, J.D.1    Gorovsky, M.A.2
  • 56
    • 0027759372 scopus 로고
    • Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila
    • Stargell, L.A. et al. Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila. Genes Dev. 7, 2641-2651 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 2641-2651
    • Stargell, L.A.1
  • 57
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Meneghini, M.D., Wu, M. & Madhani, H.D. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell 112, 725-736 (2003).
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 58
    • 0036712095 scopus 로고    scopus 로고
    • DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis
    • Madigan, J.P., Chotkowski, H.L. & Glaser, R.L. DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis. Nucleic Acids Res. 30, 3698-3705 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3698-3705
    • Madigan, J.P.1    Chotkowski, H.L.2    Glaser, R.L.3
  • 59
    • 0033578004 scopus 로고    scopus 로고
    • Regions of variant histone His2AvD required for Drosophila development
    • Clarkson, M.J. et al. Regions of variant histone His2AvD required for Drosophila development. Nature399, 694-697 (1999).
    • (1999) Nature , vol.399 , pp. 694-697
    • Clarkson, M.J.1
  • 60
    • 0036183219 scopus 로고    scopus 로고
    • The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states
    • Fan, J.Y. et al. The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states. Nat. Struct. Biol. 9, 172-176 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 172-176
    • Fan, J.Y.1
  • 61
    • 0034721645 scopus 로고    scopus 로고
    • Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes
    • Santisteban, M.S., Kalashnikova, T. & Smith, M.M. Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes. Cell 103, 411-422 (2000).
    • (2000) Cell , vol.103 , pp. 411-422
    • Santisteban, M.S.1    Kalashnikova, T.2    Smith, M.M.3
  • 62
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi, C. & Pehrson, J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393, 599-601 (1998).
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 63
    • 0033945166 scopus 로고    scopus 로고
    • Histone macroH2A1.2 is concentrated in the XY compartment of mammalian male meiotic nuclei
    • Richler, C., Dhara, S.K. & Wahrman, J. Histone macroH2A1.2 is concentrated in the XY compartment of mammalian male meiotic nuclei. Cyt. Cell. Genet. 89, 118-120 (2000).
    • (2000) Cyt. Cell. Genet. , vol.89 , pp. 118-120
    • Richler, C.1    Dhara, S.K.2    Wahrman, J.3
  • 64
    • 0035877759 scopus 로고    scopus 로고
    • MACROH2A2, a new member of the MARCOH2A core histone family
    • Costanzi, C. & Pehrson, J.R. MACROH2A2, a new member of the MARCOH2A core histone family. J. Biol. Chem. 276, 21776-21784 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21776-21784
    • Costanzi, C.1    Pehrson, J.R.2
  • 65
    • 0036139265 scopus 로고    scopus 로고
    • Dosage compensation: Do birds do it as well?
    • Ellegren, H. Dosage compensation: do birds do it as well? Trends Genet. 18, 25-28 (2002).
    • (2002) Trends Genet. , vol.18 , pp. 25-28
    • Ellegren, H.1
  • 66
    • 0032526621 scopus 로고    scopus 로고
    • Evolutionary conservation of histone macroH2A subtypes and domains
    • Pehrson, J.R. & Fuji, R.N. Evolutionary conservation of histone macroH2A subtypes and domains. Nucleic Acids Res. 26, 2837-2842 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2837-2842
    • Pehrson, J.R.1    Fuji, R.N.2
  • 67
    • 0033527694 scopus 로고    scopus 로고
    • A biochemical genomics approach for identifying genes by the activity of their products
    • Martzen, M.R. et al. A biochemical genomics approach for identifying genes by the activity of their products. Science 286, 1153-1155 (1999).
    • (1999) Science , vol.286 , pp. 1153-1155
    • Martzen, M.R.1
  • 68
    • 0037961635 scopus 로고    scopus 로고
    • The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling
    • Angelov, D. et al. The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling. Mol. Cell 11, 1033-1041 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1033-1041
    • Angelov, D.1
  • 69
    • 0035891432 scopus 로고    scopus 로고
    • The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis
    • Aul, R.B. & Oko, R.J. The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis. Dev. Biol. 242, 376-387 (2002).
    • (2002) Dev. Biol. , vol.242 , pp. 376-387
    • Aul, R.B.1    Oko, R.J.2
  • 70
    • 0029301290 scopus 로고
    • Centromeric chromatin. Histone deviants
    • Wolffe, A.P. Centromeric chromatin. Histone deviants. Curr. Biol. 5, 452-454 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 452-454
    • Wolffe, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.