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Volumn 30, Issue 5, 2014, Pages 199-209

Histone variants at the transcription start-site

Author keywords

Chromatin; Histone variants; Nucleosome mapping; Transcription start site; Transcriptional regulation; Unstable nucleosomes

Indexed keywords

HISTONE H2AZ; HISTONE; ISOPROTEIN; NUCLEOSOME;

EID: 84899916209     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2014.03.002     Document Type: Review
Times cited : (50)

References (100)
  • 1
    • 84862732690 scopus 로고    scopus 로고
    • New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?
    • Luger K., et al. New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?. Nat. Rev. Mol. Cell Biol. 2012, 13:436-447.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 436-447
    • Luger, K.1
  • 2
    • 0023661185 scopus 로고
    • Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II
    • Workman J.L., Roeder R.G. Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II. Cell 1987, 51:613-622.
    • (1987) Cell , vol.51 , pp. 613-622
    • Workman, J.L.1    Roeder, R.G.2
  • 3
    • 84899027001 scopus 로고    scopus 로고
    • Nucleosomes accelerate transcription factor dissociation
    • Luo Y., et al. Nucleosomes accelerate transcription factor dissociation. Nucleic Acids Res. 2013, 42:3017-3027.
    • (2013) Nucleic Acids Res. , vol.42 , pp. 3017-3027
    • Luo, Y.1
  • 4
    • 0023663417 scopus 로고
    • Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones
    • Lorch Y., et al. Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones. Cell 1987, 49:203-210.
    • (1987) Cell , vol.49 , pp. 203-210
    • Lorch, Y.1
  • 5
    • 34249307315 scopus 로고    scopus 로고
    • Nuclear organization of the genome and the potential for gene regulation
    • Fraser P., Bickmore W. Nuclear organization of the genome and the potential for gene regulation. Nature 2007, 447:413-417.
    • (2007) Nature , vol.447 , pp. 413-417
    • Fraser, P.1    Bickmore, W.2
  • 6
    • 80455144479 scopus 로고    scopus 로고
    • Pioneer transcription factors: establishing competence for gene expression
    • Zaret K.S., Carroll J.S. Pioneer transcription factors: establishing competence for gene expression. Genes Dev. 2011, 25:2227-2241.
    • (2011) Genes Dev. , vol.25 , pp. 2227-2241
    • Zaret, K.S.1    Carroll, J.S.2
  • 7
    • 0028363760 scopus 로고
    • Formation and stability of higher order chromatin structures. Contributions of the histone octamer
    • Schwarz P.M., Hansen J.C. Formation and stability of higher order chromatin structures. Contributions of the histone octamer. J. Biol. Chem. 1994, 269:16284-16289.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16284-16289
    • Schwarz, P.M.1    Hansen, J.C.2
  • 8
    • 39749145198 scopus 로고    scopus 로고
    • Dynamic regulation of nucleosome positioning in the human genome
    • Schones D.E., et al. Dynamic regulation of nucleosome positioning in the human genome. Cell 2008, 132:887-898.
    • (2008) Cell , vol.132 , pp. 887-898
    • Schones, D.E.1
  • 9
    • 79959557189 scopus 로고    scopus 로고
    • Determinants of nucleosome organization in primary human cells
    • Valouev A., et al. Determinants of nucleosome organization in primary human cells. Nature 2011, 474:516-520.
    • (2011) Nature , vol.474 , pp. 516-520
    • Valouev, A.1
  • 10
    • 84870674869 scopus 로고    scopus 로고
    • Controls of nucleosome positioning in the human genome
    • Gaffney D.J., et al. Controls of nucleosome positioning in the human genome. PLoS Genet. 2012, 8:e1003036.
    • (2012) PLoS Genet. , vol.8
    • Gaffney, D.J.1
  • 11
    • 84862979650 scopus 로고    scopus 로고
    • A map of nucleosome positions in yeast at base-pair resolution
    • Brogaard K., et al. A map of nucleosome positions in yeast at base-pair resolution. Nature 2012, 486:496-501.
    • (2012) Nature , vol.486 , pp. 496-501
    • Brogaard, K.1
  • 12
    • 76349103252 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe genome-wide nucleosome mapping reveals positioning mechanisms distinct from those of Saccharomyces cerevisiae
    • Lantermann A.B., et al. 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
  • 13
    • 34748826166 scopus 로고    scopus 로고
    • A high-resolution atlas of nucleosome occupancy in yeast
    • Lee W., et al. A high-resolution atlas of nucleosome occupancy in yeast. Nat. Genet. 2007, 39:1235-1244.
    • (2007) Nat. Genet. , vol.39 , pp. 1235-1244
    • Lee, W.1
  • 14
    • 43749099875 scopus 로고    scopus 로고
    • Nucleosome organization in the Drosophila genome
    • Mavrich T.N., et al. Nucleosome organization in the Drosophila genome. Nature 2008, 453:358-362.
    • (2008) Nature , vol.453 , pp. 358-362
    • Mavrich, T.N.1
  • 15
    • 84869089058 scopus 로고    scopus 로고
    • Genome-wide nucleosome positioning during embryonic stem cell development
    • Teif V.B., et al. Genome-wide nucleosome positioning during embryonic stem cell development. Nat. Struct. Mol. Biol. 2012, 19:1185-1192.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1185-1192
    • Teif, V.B.1
  • 16
    • 77956931047 scopus 로고    scopus 로고
    • H2A.Z. maintenance during mitosis reveals nucleosome shifting on mitotically silenced genes
    • Kelly T.K., et al. H2A.Z. maintenance during mitosis reveals nucleosome shifting on mitotically silenced genes. Mol. Cell 2010, 39:901-911.
    • (2010) Mol. Cell , vol.39 , pp. 901-911
    • Kelly, T.K.1
  • 17
    • 84869082555 scopus 로고    scopus 로고
    • Histone H2A.Z. inheritance during the cell cycle and its impact on promoter organization and dynamics
    • Nekrasov M., et al. Histone H2A.Z. inheritance during the cell cycle and its impact on promoter organization and dynamics. Nat. Struct. Mol. Biol. 2012, 19:1076-1083.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1076-1083
    • Nekrasov, M.1
  • 18
    • 68249142923 scopus 로고    scopus 로고
    • Intrinsic histone-DNA interactions are not the major determinant of nucleosome positions in vivo
    • Zhang Y., et al. Intrinsic histone-DNA interactions are not the major determinant of nucleosome positions in vivo. Nat. Struct. Mol. Biol. 2009, 16:847-852.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 847-852
    • Zhang, Y.1
  • 19
    • 0022799080 scopus 로고
    • Removal of positioned nucleosomes from the yeast PHO5 promoter upon PHO5 induction releases additional upstream activating DNA elements
    • Almer A., et al. Removal of positioned nucleosomes from the yeast PHO5 promoter upon PHO5 induction releases additional upstream activating DNA elements. EMBO J. 1986, 5:2689-2696.
    • (1986) EMBO J. , vol.5 , pp. 2689-2696
    • Almer, A.1
  • 20
    • 34547633654 scopus 로고    scopus 로고
    • P21 transcription is regulated by differential localization of histone H2A.Z
    • Gevry N., et al. p21 transcription is regulated by differential localization of histone H2A.Z. Genes Dev. 2007, 21:1869-1881.
    • (2007) Genes Dev. , vol.21 , pp. 1869-1881
    • Gevry, N.1
  • 21
    • 67649668767 scopus 로고    scopus 로고
    • Histone H2A.Z. is essential for estrogen receptor signaling
    • Gevry N., et al. Histone H2A.Z. is essential for estrogen receptor signaling. Genes Dev. 2009, 23:1522-1533.
    • (2009) Genes Dev. , vol.23 , pp. 1522-1533
    • Gevry, N.1
  • 22
    • 0025239781 scopus 로고
    • Nucleosome positioning modulates accessibility of regulatory proteins to the mouse mammary tumor virus promoter
    • Pina B., et al. Nucleosome positioning modulates accessibility of regulatory proteins to the mouse mammary tumor virus promoter. Cell 1990, 60:719-731.
    • (1990) Cell , vol.60 , pp. 719-731
    • Pina, B.1
  • 23
    • 26844511498 scopus 로고    scopus 로고
    • Histone variant H2A.Z. marks the 5' ends of both active and inactive genes in euchromatin
    • Raisner R.M., et al. Histone variant H2A.Z. marks the 5' ends of both active and inactive genes in euchromatin. Cell 2005, 123:233-248.
    • (2005) Cell , vol.123 , pp. 233-248
    • Raisner, R.M.1
  • 24
    • 79956316470 scopus 로고    scopus 로고
    • A packing mechanism for nucleosome organization reconstituted across a eukaryotic genome
    • Zhang Z., et al. 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
  • 25
    • 74949110964 scopus 로고    scopus 로고
    • High-resolution nucleosome mapping reveals transcription-dependent promoter packaging
    • Weiner A., et al. High-resolution nucleosome mapping reveals transcription-dependent promoter packaging. Genome Res. 2010, 20:90-100.
    • (2010) Genome Res. , vol.20 , pp. 90-100
    • Weiner, A.1
  • 26
    • 34047111213 scopus 로고    scopus 로고
    • Translational and rotational settings of H2A.Z. nucleosomes across the Saccharomyces cerevisiae genome
    • Albert I., et al. Translational and rotational settings of H2A.Z. nucleosomes across the Saccharomyces cerevisiae genome. Nature 2007, 446:572-576.
    • (2007) Nature , vol.446 , pp. 572-576
    • Albert, I.1
  • 27
    • 84891523560 scopus 로고    scopus 로고
    • Histone variant selectivity at the transcription start site: H2A.Z. or H2A.Lap1
    • Nekrasov M., et al. Histone variant selectivity at the transcription start site: H2A.Z. or H2A.Lap1. Nucleus 2013, 4:431-438.
    • (2013) Nucleus , vol.4 , pp. 431-438
    • Nekrasov, M.1
  • 28
    • 84876528012 scopus 로고    scopus 로고
    • High-resolution nucleosome mapping of targeted regions using BAC-based enrichment
    • Yigit E., et al. High-resolution nucleosome mapping of targeted regions using BAC-based enrichment. Nucleic Acids Res. 2013, 41:e87.
    • (2013) Nucleic Acids Res. , vol.41
    • Yigit, E.1
  • 29
    • 84870575235 scopus 로고    scopus 로고
    • Histone H2A variants in nucleosomes and chromatin: more or less stable?
    • Bonisch C., Hake S.B. Histone H2A variants in nucleosomes and chromatin: more or less stable?. Nucleic Acids Res. 2012, 40:10719-10741.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10719-10741
    • Bonisch, C.1    Hake, S.B.2
  • 30
    • 84885353806 scopus 로고    scopus 로고
    • H3.3 actively marks enhancers and primes gene transcription via opening higher-ordered chromatin
    • Chen P., et al. H3.3 actively marks enhancers and primes gene transcription via opening higher-ordered chromatin. Genes Dev. 2013, 27:2109-2124.
    • (2013) Genes Dev. , vol.27 , pp. 2109-2124
    • Chen, P.1
  • 31
    • 84868122260 scopus 로고    scopus 로고
    • Deposition of histone variant H2A.Z. within gene bodies regulates responsive genes
    • Coleman-Derr D., Zilberman D. Deposition of histone variant H2A.Z. within gene bodies regulates responsive genes. PLoS Genet. 2012, 8:e1002988.
    • (2012) PLoS Genet. , vol.8
    • Coleman-Derr, D.1    Zilberman, D.2
  • 32
    • 84867692492 scopus 로고    scopus 로고
    • DeltaNp63alpha represses anti-proliferative genes via H2A.Z. deposition
    • Gallant-Behm C.L., et al. DeltaNp63alpha represses anti-proliferative genes via H2A.Z. deposition. Genes Dev. 2012, 26:2325-2336.
    • (2012) Genes Dev. , vol.26 , pp. 2325-2336
    • Gallant-Behm, C.L.1
  • 33
    • 73349098753 scopus 로고    scopus 로고
    • The euchromatic and heterochromatic landscapes are shaped by antagonizing effects of transcription on H2A.Z. deposition
    • Hardy S., et al. 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
  • 34
    • 84873581550 scopus 로고    scopus 로고
    • H2A.Z. facilitates access of active and repressive complexes to chromatin in embryonic stem cell self-renewal and differentiation
    • Hu G., et al. H2A.Z. facilitates access of active and repressive complexes to chromatin in embryonic stem cell self-renewal and differentiation. Cell Stem Cell 2013, 12:180-192.
    • (2013) Cell Stem Cell , vol.12 , pp. 180-192
    • Hu, G.1
  • 35
    • 73149085055 scopus 로고    scopus 로고
    • H2A.Z-containing nucleosomes mediate the thermosensory response in Arabidopsis
    • Kumar S.V., Wigge P.A. H2A.Z-containing nucleosomes mediate the thermosensory response in Arabidopsis. Cell 2010, 140:136-147.
    • (2010) Cell , vol.140 , pp. 136-147
    • Kumar, S.V.1    Wigge, P.A.2
  • 36
    • 84884651635 scopus 로고    scopus 로고
    • H2A.Z. acidic patch couples chromatin dynamics to regulation of gene expression programs during ESC differentiation
    • Subramanian V., et al. H2A.Z. acidic patch couples chromatin dynamics to regulation of gene expression programs during ESC differentiation. PLoS Genet. 2013, 9:e1003725.
    • (2013) PLoS Genet. , vol.9
    • Subramanian, V.1
  • 37
    • 84856518449 scopus 로고    scopus 로고
    • Acetylation of H2A.Z. is a key epigenetic modification associated with gene deregulation and epigenetic remodeling in cancer
    • Valdes-Mora F., et al. Acetylation of H2A.Z. is a key epigenetic modification associated with gene deregulation and epigenetic remodeling in cancer. Genome Res. 2012, 22:307-321.
    • (2012) Genome Res. , vol.22 , pp. 307-321
    • Valdes-Mora, F.1
  • 38
    • 26844489856 scopus 로고    scopus 로고
    • Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss
    • Zhang H., et al. Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss. Cell 2005, 123:219-231.
    • (2005) Cell , vol.123 , pp. 219-231
    • Zhang, H.1
  • 39
    • 70349292569 scopus 로고    scopus 로고
    • Histone H2A.Z. cooperates with RNAi and heterochromatin factors to suppress antisense RNAs
    • Zofall M., et al. Histone H2A.Z. cooperates with RNAi and heterochromatin factors to suppress antisense RNAs. Nature 2009, 461:419-422.
    • (2009) Nature , vol.461 , pp. 419-422
    • Zofall, M.1
  • 40
    • 84870904979 scopus 로고    scopus 로고
    • Histone H2A.Z. controls a critical chromatin remodeling step required for DNA double-strand break repair
    • Xu Y., et al. Histone H2A.Z. controls a critical chromatin remodeling step required for DNA double-strand break repair. Mol. Cell 2012, 48:723-733.
    • (2012) Mol. Cell , vol.48 , pp. 723-733
    • Xu, Y.1
  • 41
    • 55549148715 scopus 로고    scopus 로고
    • H2AZ is enriched at polycomb complex target genes in ES cells and is necessary for lineage commitment
    • Creyghton M.P., et al. H2AZ is enriched at polycomb complex target genes in ES cells and is necessary for lineage commitment. Cell 2008, 135:649-661.
    • (2008) Cell , vol.135 , pp. 649-661
    • Creyghton, M.P.1
  • 42
    • 0035822687 scopus 로고    scopus 로고
    • Histone variant H2A.Z. is required for early mammalian development
    • Faast R., et al. Histone variant H2A.Z. is required for early mammalian development. Curr. Biol. 2001, 11:1183-1187.
    • (2001) Curr. Biol. , vol.11 , pp. 1183-1187
    • Faast, R.1
  • 43
    • 84864487629 scopus 로고    scopus 로고
    • H2A.Z.2.2 is an alternatively spliced histone H2A.Z. variant that causes severe nucleosome destabilization
    • Bonisch C., et al. H2A.Z.2.2 is an alternatively spliced histone H2A.Z. variant that causes severe nucleosome destabilization. Nucleic Acids Res. 2012, 40:5951-5964.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5951-5964
    • Bonisch, C.1
  • 44
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profiling of histone methylations in the human genome
    • Barski A., et al. High-resolution profiling of histone methylations in the human genome. Cell 2007, 129:823-837.
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1
  • 45
    • 73649087947 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe JmjC-protein, Msc1, prevents H2A.Z. localization in centromeric and subtelomeric chromatin domains
    • Buchanan L., et al. The Schizosaccharomyces pombe JmjC-protein, Msc1, prevents H2A.Z. localization in centromeric and subtelomeric chromatin domains. PLoS Genet. 2009, 5:e1000726.
    • (2009) PLoS Genet. , vol.5
    • Buchanan, L.1
  • 46
    • 58049191558 scopus 로고    scopus 로고
    • Chromatin signatures in multipotent human hematopoietic stem cells indicate the fate of bivalent genes during differentiation
    • Cui K., et al. Chromatin signatures in multipotent human hematopoietic stem cells indicate the fate of bivalent genes during differentiation. Cell Stem Cell 2009, 4:80-93.
    • (2009) Cell Stem Cell , vol.4 , pp. 80-93
    • Cui, K.1
  • 47
    • 84855457949 scopus 로고    scopus 로고
    • A unique H2A histone variant occupies the transcriptional start site of active genes
    • Soboleva T.A., et al. A unique H2A histone variant occupies the transcriptional start site of active genes. Nat. Struct. Mol. Biol. 2012, 19:25-30.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 25-30
    • Soboleva, T.A.1
  • 48
    • 29144531244 scopus 로고    scopus 로고
    • Variant histone H2A.Z. is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning
    • Guillemette B., et al. Variant histone H2A.Z. is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning. PLoS Biol. 2005, 3:e384.
    • (2005) PLoS Biol. , vol.3
    • Guillemette, B.1
  • 49
    • 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
  • 50
    • 70350701809 scopus 로고    scopus 로고
    • Cooperative action of TIP48 and TIP49 in H2A.Z. exchange catalyzed by acetylation of nucleosomal H2A
    • Choi J., et al. Cooperative action of TIP48 and TIP49 in H2A.Z. exchange catalyzed by acetylation of nucleosomal H2A. Nucleic Acids Res. 2009, 37:5993-6007.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5993-6007
    • Choi, J.1
  • 51
    • 70349662183 scopus 로고    scopus 로고
    • NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components
    • Lu P.Y., et al. NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components. Biochem. Cell Biol. 2009, 87:799-815.
    • (2009) Biochem. Cell Biol. , vol.87 , pp. 799-815
    • Lu, P.Y.1
  • 52
    • 84884225242 scopus 로고    scopus 로고
    • Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1
    • Nguyen V.Q., et al. Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1. Cell 2013, 154:1220-1231.
    • (2013) Cell , vol.154 , pp. 1220-1231
    • Nguyen, V.Q.1
  • 53
    • 84884214357 scopus 로고    scopus 로고
    • Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z. replacement
    • Ranjan A., et al. Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z. replacement. Cell 2013, 154:1232-1245.
    • (2013) Cell , vol.154 , pp. 1232-1245
    • Ranjan, A.1
  • 54
    • 84884234697 scopus 로고    scopus 로고
    • SWR-C and INO80 chromatin remodelers recognize nucleosome-free regions near +1 nucleosomes
    • Yen K., et al. SWR-C and INO80 chromatin remodelers recognize nucleosome-free regions near +1 nucleosomes. Cell 2013, 154:1246-1256.
    • (2013) Cell , vol.154 , pp. 1246-1256
    • Yen, K.1
  • 55
    • 84898021821 scopus 로고    scopus 로고
    • Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z
    • Mao Z., et al. Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. Cell Res. 2014, 24:389-399.
    • (2014) Cell Res. , vol.24 , pp. 389-399
    • Mao, Z.1
  • 56
    • 84895910164 scopus 로고    scopus 로고
    • ANP32E is a histone chaperone that removes H2A.Z. from chromatin
    • Obri A., et al. ANP32E is a histone chaperone that removes H2A.Z. from chromatin. Nature 2014, 505:648-653.
    • (2014) Nature , vol.505 , pp. 648-653
    • Obri, A.1
  • 57
    • 57849109058 scopus 로고    scopus 로고
    • Nascent RNA sequencing reveals widespread pausing and divergent initiation at human promoters
    • Core L.J., et al. Nascent RNA sequencing reveals widespread pausing and divergent initiation at human promoters. Science 2008, 322:1845-1848.
    • (2008) Science , vol.322 , pp. 1845-1848
    • Core, L.J.1
  • 58
    • 78649884849 scopus 로고    scopus 로고
    • H2A.Z. nucleosomes enriched over active genes are homotypic
    • Weber C.M., et al. H2A.Z. nucleosomes enriched over active genes are homotypic. Nat. Struct. Mol. Biol. 2010, 17:1500-1507.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1500-1507
    • Weber, C.M.1
  • 59
    • 84874175008 scopus 로고    scopus 로고
    • Precise maps of RNA polymerase reveal how promoters direct initiation and pausing
    • Kwak H., et al. Precise maps of RNA polymerase reveal how promoters direct initiation and pausing. Science 2013, 339:950-953.
    • (2013) Science , vol.339 , pp. 950-953
    • Kwak, H.1
  • 60
    • 21644468242 scopus 로고    scopus 로고
    • Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z
    • Farris S.D., et al. Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z. J. Biol. Chem. 2005, 280:25298-25303.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25298-25303
    • Farris, S.D.1
  • 61
    • 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., et al. 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
  • 62
    • 35848931678 scopus 로고    scopus 로고
    • The nucleosome surface regulates chromatin compaction and couples it with transcriptional repression
    • Zhou J., et al. 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
  • 63
    • 77954670503 scopus 로고    scopus 로고
    • Reconciling the positive and negative roles of histone H2A.Z. in gene transcription
    • Marques M., et al. Reconciling the positive and negative roles of histone H2A.Z. in gene transcription. Epigenetics 2010, 5:267-272.
    • (2010) Epigenetics , vol.5 , pp. 267-272
    • Marques, M.1
  • 64
    • 84876831128 scopus 로고    scopus 로고
    • TIP48/Reptin and H2A.Z. requirement for initiating chromatin remodeling in estrogen-activated transcription
    • Dalvai M., et al. TIP48/Reptin and H2A.Z. requirement for initiating chromatin remodeling in estrogen-activated transcription. PLoS Genet. 2013, 9:e1003387.
    • (2013) PLoS Genet. , vol.9
    • Dalvai, M.1
  • 65
    • 34548777017 scopus 로고    scopus 로고
    • Monoubiquitylation of H2A.Z. distinguishes its association with euchromatin or facultative heterochromatin
    • Sarcinella E., et al. Monoubiquitylation of H2A.Z. distinguishes its association with euchromatin or facultative heterochromatin. Mol. Cell. Biol. 2007, 27:6457-6468.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6457-6468
    • Sarcinella, E.1
  • 66
    • 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
  • 67
    • 4444312848 scopus 로고    scopus 로고
    • Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA
    • Bao Y., et al. Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA. EMBO J. 2004, 23:3314-3324.
    • (2004) EMBO J. , vol.23 , pp. 3314-3324
    • Bao, Y.1
  • 68
    • 79960652605 scopus 로고    scopus 로고
    • Chromatoid body and small RNAs in male germ cells
    • Meikar O., et al. Chromatoid body and small RNAs in male germ cells. Reproduction 2011, 142:195-209.
    • (2011) Reproduction , vol.142 , pp. 195-209
    • Meikar, O.1
  • 69
    • 61849170193 scopus 로고    scopus 로고
    • Genome-wide profiling of salt fractions maps physical properties of chromatin
    • Henikoff S., et al. 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
  • 70
    • 79955559703 scopus 로고    scopus 로고
    • Nucleosome fragility reveals novel functional states of chromatin and poises genes for activation
    • Xi Y., et al. Nucleosome fragility reveals novel functional states of chromatin and poises genes for activation. Genome Res. 2011, 21:718-724.
    • (2011) Genome Res. , vol.21 , pp. 718-724
    • Xi, Y.1
  • 71
    • 0027716843 scopus 로고
    • Effects of histone acetylation, ubiquitination and variants on nucleosome stability
    • Li W., et al. Effects of histone acetylation, ubiquitination and variants on nucleosome stability. Biochem. J. 1993, 296:737-744.
    • (1993) Biochem. J. , vol.296 , pp. 737-744
    • Li, W.1
  • 72
    • 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., et al. 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
  • 73
    • 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. 2002, 9:172-176.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 172-176
    • Fan, J.Y.1
  • 74
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White C.L., et al. Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J. 2001, 20:5207-5218.
    • (2001) EMBO J. , vol.20 , pp. 5207-5218
    • White, C.L.1
  • 75
    • 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. 2000, 7:1121-1124.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1
  • 76
    • 33846293581 scopus 로고    scopus 로고
    • H2A.Z. contributes to the unique 3D structure of the centromere
    • Greaves I.K., et al. H2A.Z. contributes to the unique 3D structure of the centromere. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:525-530.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 525-530
    • Greaves, I.K.1
  • 77
    • 84889813232 scopus 로고    scopus 로고
    • Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2
    • Horikoshi N., et al. Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2. Acta Crystallogr. D: Biol. Crystallogr. 2013, 69:2431-2439.
    • (2013) Acta Crystallogr. D: Biol. Crystallogr. , vol.69 , pp. 2431-2439
    • Horikoshi, N.1
  • 78
    • 74549209522 scopus 로고    scopus 로고
    • Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
    • Dryhurst D., et al. Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates. BMC Biol. 2009, 7:86.
    • (2009) BMC Biol. , vol.7 , pp. 86
    • Dryhurst, D.1
  • 79
    • 43749088127 scopus 로고    scopus 로고
    • Two strategies for gene regulation by promoter nucleosomes
    • Tirosh I., Barkai N. Two strategies for gene regulation by promoter nucleosomes. Genome Res. 2008, 18:1084-1091.
    • (2008) Genome Res. , vol.18 , pp. 1084-1091
    • Tirosh, I.1    Barkai, N.2
  • 80
    • 79851485916 scopus 로고    scopus 로고
    • Transcription initiation patterns indicate divergent strategies for gene regulation at the chromatin level
    • Rach E.A., et al. Transcription initiation patterns indicate divergent strategies for gene regulation at the chromatin level. PLoS Genet. 2011, 7:e1001274.
    • (2011) PLoS Genet. , vol.7
    • Rach, E.A.1
  • 81
    • 75349098018 scopus 로고    scopus 로고
    • A compiled and systematic reference map of nucleosome positions across the Saccharomyces cerevisiae genome
    • Jiang C., Pugh B.F. A compiled and systematic reference map of nucleosome positions across the Saccharomyces cerevisiae genome. Genome Biol. 2009, 10:R109.
    • (2009) Genome Biol. , vol.10
    • Jiang, C.1    Pugh, B.F.2
  • 82
    • 33745851176 scopus 로고    scopus 로고
    • The X and Y chromosomes assemble into H2A.Z-containing facultative heterochromatin following meiosis
    • Greaves I.K., et al. The X and Y chromosomes assemble into H2A.Z-containing facultative heterochromatin following meiosis. Mol. Cell. Biol. 2006, 26:5394-5405.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5394-5405
    • Greaves, I.K.1
  • 83
    • 84886298616 scopus 로고    scopus 로고
    • Developmental roles of histone H3 variants and their chaperones
    • Filipescu D., et al. Developmental roles of histone H3 variants and their chaperones. Trends Genet. 2013, 29:630-640.
    • (2013) Trends Genet. , vol.29 , pp. 630-640
    • Filipescu, D.1
  • 84
    • 77649099092 scopus 로고    scopus 로고
    • Distinct factors control histone variant H3.3 localization at specific genomic regions
    • Goldberg A.D., et al. Distinct factors control histone variant H3.3 localization at specific genomic regions. Cell 2010, 140:678-691.
    • (2010) Cell , vol.140 , pp. 678-691
    • Goldberg, A.D.1
  • 85
    • 84881604151 scopus 로고    scopus 로고
    • Histone variant H3.3 maintains a decondensed chromatin state essential for mouse preimplantation development
    • Lin C.J., et al. Histone variant H3.3 maintains a decondensed chromatin state essential for mouse preimplantation development. Development 2013, 140:3624-3634.
    • (2013) Development , vol.140 , pp. 3624-3634
    • Lin, C.J.1
  • 86
    • 27644515513 scopus 로고    scopus 로고
    • The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus
    • Loppin B., et al. 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
  • 87
    • 37749051130 scopus 로고    scopus 로고
    • Epigenetic memory of an active gene state depends on histone H3.3 incorporation into chromatin in the absence of transcription
    • Ng R.K., Gurdon J.B. Epigenetic memory of an active gene state depends on histone H3.3 incorporation into chromatin in the absence of transcription. Nat. Cell Biol. 2008, 10:102-109.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 102-109
    • Ng, R.K.1    Gurdon, J.B.2
  • 88
    • 84873999534 scopus 로고    scopus 로고
    • Conditional allelic replacement applied to genes encoding the histone variant H3.3 in the mouse
    • Tang M.C., et al. Conditional allelic replacement applied to genes encoding the histone variant H3.3 in the mouse. Genesis 2013, 51:142-146.
    • (2013) Genesis , vol.51 , pp. 142-146
    • Tang, M.C.1
  • 89
    • 84884889017 scopus 로고    scopus 로고
    • Transcription recovery after DNA damage requires chromatin priming by the H3.3 histone chaperone HIRA
    • Adam S., et al. Transcription recovery after DNA damage requires chromatin priming by the H3.3 histone chaperone HIRA. Cell 2013, 155:94-106.
    • (2013) Cell , vol.155 , pp. 94-106
    • Adam, S.1
  • 90
    • 77956409475 scopus 로고    scopus 로고
    • Heterochromatin formation in the mouse embryo requires critical residues of the histone variant H3.3
    • Santenard A., et al. Heterochromatin formation in the mouse embryo requires critical residues of the histone variant H3.3. Nat. Cell Biol. 2010, 12:853-862.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 853-862
    • Santenard, A.1
  • 91
    • 61849118594 scopus 로고    scopus 로고
    • Histone H3.3 incorporation provides a unique and functionally essential telomeric chromatin in embryonic stem cells
    • Wong L.H., et al. Histone H3.3 incorporation provides a unique and functionally essential telomeric chromatin in embryonic stem cells. Genome Res. 2009, 19:404-414.
    • (2009) Genome Res. , vol.19 , pp. 404-414
    • Wong, L.H.1
  • 92
    • 84861647319 scopus 로고    scopus 로고
    • A unified phylogeny-based nomenclature for histone variants
    • Talbert P.B., et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin 2012, 5:7.
    • (2012) Epigenetics Chromatin , vol.5 , pp. 7
    • Talbert, P.B.1
  • 93
    • 84865378667 scopus 로고    scopus 로고
    • Histone variant H2A.Bbd is associated with active transcription and mRNA processing in human cells
    • Tolstorukov M.Y., et al. Histone variant H2A.Bbd is associated with active transcription and mRNA processing in human cells. Mol. Cell 2012, 47:596-607.
    • (2012) Mol. Cell , vol.47 , pp. 596-607
    • Tolstorukov, M.Y.1
  • 94
    • 23044453722 scopus 로고    scopus 로고
    • Structural characterization of histone H2A variants
    • Chakravarthy S., et al. Structural characterization of histone H2A variants. Cold Spring Harb. Symp. Quant. Biol. 2004, 69:227-234.
    • (2004) Cold Spring Harb. Symp. Quant. Biol. , vol.69 , pp. 227-234
    • Chakravarthy, S.1
  • 95
    • 33748931801 scopus 로고    scopus 로고
    • Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome
    • Doyen C.M., et al. Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome. EMBO J. 2006, 25:4234-4244.
    • (2006) EMBO J. , vol.25 , pp. 4234-4244
    • Doyen, C.M.1
  • 96
    • 4444378379 scopus 로고    scopus 로고
    • Histone variant H2ABbd confers lower stability to the nucleosome
    • Gautier T., et al. Histone variant H2ABbd confers lower stability to the nucleosome. EMBO Rep. 2004, 5:715-720.
    • (2004) EMBO Rep. , vol.5 , pp. 715-720
    • Gautier, T.1
  • 97
    • 68949136888 scopus 로고    scopus 로고
    • The dynamics of individual nucleosomes controls the chromatin condensation pathway: direct atomic force microscopy visualization of variant chromatin
    • Montel F., et al. The dynamics of individual nucleosomes controls the chromatin condensation pathway: direct atomic force microscopy visualization of variant chromatin. Biophys. J. 2009, 97:544-553.
    • (2009) Biophys. J. , vol.97 , pp. 544-553
    • Montel, F.1
  • 98
    • 20844434027 scopus 로고    scopus 로고
    • SWI/SNF remodeling and p300-dependent transcription of histone variant H2ABbd nucleosomal arrays
    • Angelov D., et al. SWI/SNF remodeling and p300-dependent transcription of histone variant H2ABbd nucleosomal arrays. EMBO J. 2004, 23:3815-3824.
    • (2004) EMBO J. , vol.23 , pp. 3815-3824
    • Angelov, D.1
  • 99
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8Å resolution
    • Luger K., et al. Crystal structure of the nucleosome core particle at 2.8Å resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1
  • 100
    • 8844281536 scopus 로고    scopus 로고
    • H2A.Z. alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding
    • Fan J.Y., et al. 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


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