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Volumn 25, Issue 7, 2003, Pages 647-656

Epigenomic replication: Linking epigenetics to DNA replication

Author keywords

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Indexed keywords

HISTONE;

EID: 0038505671     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.10305     Document Type: Review
Times cited : (135)

References (98)
  • 1
    • 0036532235 scopus 로고    scopus 로고
    • Heterochromatin: New possibilities for the inheritance of structure
    • Grewal SI, Elgin SC. Heterochromatin: new possibilities for the inheritance of structure. Curr Opin Genet Dev 2002;12:178-187.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 178-187
    • Grewal, S.I.1    Elgin, S.C.2
  • 3
    • 0035313802 scopus 로고    scopus 로고
    • The ins and outs of nucleosome assembly
    • Mello JA, Almouzni G. The ins and outs of nucleosome assembly. Curr Opin Genet Dev 2001;11:136-141.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 136-141
    • Mello, J.A.1    Almouzni, G.2
  • 5
    • 0035377556 scopus 로고    scopus 로고
    • Protein modules that manipulate histone tails for chromatin regulation
    • Marmorstein R. Protein modules that manipulate histone tails for chromatin regulation. Nat Rev Mol Cell Biol 2001;2:422-432.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 422-432
    • Marmorstein, R.1
  • 7
    • 0036842221 scopus 로고    scopus 로고
    • Genome-wide DNA replication profile for Drosophila melanogaster: A link between transcription and replication timing
    • Schubeler D, Scalzo D, Kooperberg C, Van Steensel B, Delrow J, Groudine M. Genome-wide DNA replication profile for Drosophila melanogaster: a link between transcription and replication timing. Nat Genet 2002;32:438-442.
    • (2002) Nat Genet , vol.32 , pp. 438-442
    • Schubeler, D.1    Scalzo, D.2    Kooperberg, C.3    Van Steensel, B.4    Delrow, J.5    Groudine, M.6
  • 8
    • 0036591890 scopus 로고    scopus 로고
    • Replication timing and transcriptional control: Beyond cause and effect
    • Gilbert DM. Replication timing and transcriptional control: beyond cause and effect. Curr Opin Cell Biol 2002;14:377-383.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 377-383
    • Gilbert, D.M.1
  • 9
    • 0036843263 scopus 로고    scopus 로고
    • Replication timing and metazoan evolution
    • Gilbert DM. Replication timing and metazoan evolution. Nat Genet 2002;32:336-337.
    • (2002) Nat Genet , vol.32 , pp. 336-337
    • Gilbert, D.M.1
  • 11
    • 0037220825 scopus 로고    scopus 로고
    • DNA replication: Telling time with microarrays
    • McCune H, Donaldson AD. DNA replication: telling time with microarrays. Genome Biology 2003;4:204.1-204.4.
    • (2003) Genome Biology , vol.4 , pp. 2041-2044
    • McCune, H.1    Donaldson, A.D.2
  • 12
    • 0032731777 scopus 로고    scopus 로고
    • A role for the replication proteins PCNA, RF-C, polymerase epsilon and Cdc45 in transcriptional silencing in Saccharomyces cerevisiae
    • Ehrenhofer-Murray AE, Kamakaka RT, Rine J. A role for the replication proteins PCNA, RF-C, polymerase epsilon and Cdc45 in transcriptional silencing in Saccharomyces cerevisiae. Genetics 1999;153:1171-1182.
    • (1999) Genetics , vol.153 , pp. 1171-1182
    • Ehrenhofer-Murray, A.E.1    Kamakaka, R.T.2    Rine, J.3
  • 13
    • 0034626734 scopus 로고    scopus 로고
    • PCNA connects DNA replication to epigenetic inheritance in yeast
    • Zhang Z, Shibahara K, Stillman B. PCNA connects DNA replication to epigenetic inheritance in yeast. Nature 2000;408:221-225.
    • (2000) Nature , vol.408 , pp. 221-225
    • Zhang, Z.1    Shibahara, K.2    Stillman, B.3
  • 14
    • 0036929125 scopus 로고    scopus 로고
    • DNA polymerase clamp shows little turnover at established replication sites but sequential de novo assembly at adjacent origin clusters
    • Sporbert A, Gahl A, Ankerhold R, Leonhardt H, Cardoso MC. DNA polymerase clamp shows little turnover at established replication sites but sequential de novo assembly at adjacent origin clusters. Mol Cell 2002;10:1355-1365.
    • (2002) Mol Cell , vol.10 , pp. 1355-1365
    • Sporbert, A.1    Gahl, A.2    Ankerhold, R.3    Leonhardt, H.4    Cardoso, M.C.5
  • 16
    • 0033369515 scopus 로고    scopus 로고
    • The spatial position and replication timing of chromosomal domains are both established in early G1 phase
    • Dimitrova DS, Gilbert DM. The spatial position and replication timing of chromosomal domains are both established in early G1 phase. Mol Cell 1999;4:983-993.
    • (1999) Mol Cell , vol.4 , pp. 983-993
    • Dimitrova, D.S.1    Gilbert, D.M.2
  • 17
    • 0031663505 scopus 로고    scopus 로고
    • The DNA replication fork in eukaryotic cells
    • Waga S, Stillman B. The DNA replication fork in eukaryotic cells. Annu Rev Biochem 1998;67:721-751.
    • (1998) Annu Rev Biochem , vol.67 , pp. 721-751
    • Waga, S.1    Stillman, B.2
  • 18
    • 0033945861 scopus 로고    scopus 로고
    • DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci
    • Rountree MR, Bachman KE, Baylin SB. DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat Genet 2000;25:269-277.
    • (2000) Nat Genet , vol.25 , pp. 269-277
    • Rountree, M.R.1    Bachman, K.E.2    Baylin, S.B.3
  • 19
    • 0033582544 scopus 로고    scopus 로고
    • Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin
    • Shibahara K, Stillman B. Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin. Cell 1999;96:575-585.
    • (1999) Cell , vol.96 , pp. 575-585
    • Shibahara, K.1    Stillman, B.2
  • 20
    • 0030770835 scopus 로고    scopus 로고
    • Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1
    • Chuang LS, Ian HI, Koh TW, Ng HH, Xu G, Li BF. Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. Science 1997;277:1996-2000.
    • (1997) Science , vol.277 , pp. 1996-2000
    • Chuang, L.S.1    Ian, H.I.2    Koh, T.W.3    Ng, H.H.4    Xu, G.5    Li, B.F.6
  • 21
    • 0037174948 scopus 로고    scopus 로고
    • A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12RFCs2-5 complex as a novel PCNA-binding protein
    • Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T. A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12RFCs2-5 complex as a novel PCNA-binding protein. J Biol Chem 2002;277:40362-40367.
    • (2002) J Biol Chem , vol.277 , pp. 40362-40367
    • Ohta, S.1    Shiomi, Y.2    Sugimoto, K.3    Obuse, C.4    Tsurimoto, T.5
  • 23
    • 0034100123 scopus 로고    scopus 로고
    • A human homologue of yeast anti-silencing factor has histone chaperone activity
    • Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M. A human homologue of yeast anti-silencing factor has histone chaperone activity. Genes Cells 2000;5:221-233.
    • (2000) Genes Cells , vol.5 , pp. 221-233
    • Munakata, T.1    Adachi, N.2    Yokoyama, N.3    Kuzuhara, T.4    Horikoshi, M.5
  • 24
    • 0036091117 scopus 로고    scopus 로고
    • Chromatin assembly. Cooperation between histone chaperones and ATP-dependent nucleosome remodeling machines
    • Tyler JK. Chromatin assembly. Cooperation between histone chaperones and ATP-dependent nucleosome remodeling machines. Eur J Biochem 2002;269:2268-2274
    • (2002) Eur J Biochem , vol.269 , pp. 2268-2274
    • Tyler, J.K.1
  • 25
    • 0034724563 scopus 로고    scopus 로고
    • NAP-2: Histone chaperone function and phosphorylation state through the cell cycle
    • Rodriguez P, Pelletier J, Price GB, Zannis-Hadjopoulos M. NAP-2: histone chaperone function and phosphorylation state through the cell cycle. J Mol Biol 2000;298:225-238.
    • (2000) J Mol Biol , vol.298 , pp. 225-238
    • Rodriguez, P.1    Pelletier, J.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 26
    • 0034686020 scopus 로고    scopus 로고
    • Purification and characterization of a human factor that assembles and remodels chromatin
    • LeRoy G, Loyola A, Lane WS, 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
  • 27
    • 0029946736 scopus 로고    scopus 로고
    • Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays
    • Ito T, Bulger M, Kobayashi R, Kadonaga JT. Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays. Mol Cell Biol 1996;16:3112-3124.
    • (1996) Mol Cell Biol , vol.16 , pp. 3112-3124
    • Ito, T.1    Bulger, M.2    Kobayashi, R.3    Kadonaga, J.T.4
  • 28
    • 0036250827 scopus 로고    scopus 로고
    • Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway
    • Mello JA, Sillje HH, Roche DM, Kirschner DB, Nigg EA, Almouzni G. Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway. EMBO Rep 2002;3:329-334.
    • (2002) EMBO Rep , vol.3 , pp. 329-334
    • Mello, J.A.1    Sillje, H.H.2    Roche, D.M.3    Kirschner, D.B.4    Nigg, E.A.5    Almouzni, G.6
  • 31
    • 0034659231 scopus 로고    scopus 로고
    • De novo nucleosome assembly: New pieces in an old puzzle
    • Verreault A. De novo nucleosome assembly: new pieces in an old puzzle. Genes Dev 2000;14:1430-1438.
    • (2000) Genes Dev , vol.14 , pp. 1430-1438
    • Verreault, A.1
  • 32
    • 0034669029 scopus 로고    scopus 로고
    • Nuclear organization of DNA replication in primary mammalian cells
    • Kennedy BK, Barbie DA, Classon M, Dyson N, Harlow E. Nuclear organization of DNA replication in primary mammalian cells. Genes Dev 2000;14:2855-2868
    • (2000) Genes Dev , vol.14 , pp. 2855-2868
    • Kennedy, B.K.1    Barbie, D.A.2    Classon, M.3    Dyson, N.4    Harlow, E.5
  • 33
    • 0035092886 scopus 로고    scopus 로고
    • DNA replication control through interaction of E2F-RB and the origin recognition complex
    • Bosco G, Du W, Orr-Weaver TL. DNA replication control through interaction of E2F-RB and the origin recognition complex. Nat Cell Biol 2001;3:289-295.
    • (2001) Nat Cell Biol , vol.3 , pp. 289-295
    • Bosco, G.1    Du, W.2    Orr-Weaver, T.L.3
  • 37
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001;410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 39
    • 0035797384 scopus 로고    scopus 로고
    • Rb targets histone H3 methylation and HP1 to promoters
    • Nielsen SJ, et al. Rb targets histone H3 methylation and HP1 to promoters. Nature 2001;412:561-565.
    • (2001) Nature , vol.412 , pp. 561-565
    • Nielsen, S.J.1
  • 40
    • 0036860727 scopus 로고    scopus 로고
    • The spatio-temporal organization of DNA replication sites is identical in primary, immortalized and transformed mammalian cells
    • Dimitrova DS, Berezney R. The spatio-temporal organization of DNA replication sites is identical in primary, immortalized and transformed mammalian cells. J Cell Sci 2002;115:4037-4051.
    • (2002) J Cell Sci , vol.115 , pp. 4037-4051
    • Dimitrova, D.S.1    Berezney, R.2
  • 41
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • Bird A. DNA methylation patterns and epigenetic memory. Genes Dev 2002;16:6-21.
    • (2002) Genes Dev , vol.16 , pp. 6-21
    • Bird, A.1
  • 42
    • 0033883260 scopus 로고    scopus 로고
    • MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase
    • Tatematsu KI, Yamazaki T, Ishikawa F. MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. Genes Cells 2000;5:677-688.
    • (2000) Genes Cells , vol.5 , pp. 677-688
    • Tatematsu, K.I.1    Yamazaki, T.2    Ishikawa, F.3
  • 43
    • 0037144441 scopus 로고    scopus 로고
    • The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2
    • Saito M, Ishikawa F. The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2. J Biol Chem 2002;277:35434-35439.
    • (2002) J Biol Chem , vol.277 , pp. 35434-35439
    • Saito, M.1    Ishikawa, F.2
  • 44
    • 0035943709 scopus 로고    scopus 로고
    • Dnmt3a and Dnmt3b are transcriptional repressors that exhibit unique localization properties to heterochromatin
    • Bachman KE, Rountree MR, Baylin SB. Dnmt3a and Dnmt3b are transcriptional repressors that exhibit unique localization properties to heterochromatin. J Biol Chem 2001;276:32282-32287.
    • (2001) J Biol Chem , vol.276 , pp. 32282-32287
    • Bachman, K.E.1    Rountree, M.R.2    Baylin, S.B.3
  • 45
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner BM, Birley AJ, Lavender J. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 1992;69:375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 46
    • 0035577669 scopus 로고    scopus 로고
    • The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae
    • Meijsing SH, Ehrenhofer-Murray AE. The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae. Genes Dev 2001;15:3169-3182.
    • (2001) Genes Dev , vol.15 , pp. 3169-3182
    • Meijsing, S.H.1    Ehrenhofer-Murray, A.E.2
  • 48
    • 0035576789 scopus 로고    scopus 로고
    • The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1
    • Osada S, Sutton A, Muster N, Brown CE, Yates JR 3rd, Sternglanz R, Workman JL. The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1. Genes Dev 2001;15:3155-3168.
    • (2001) Genes Dev , vol.15 , pp. 3155-3168
    • Osada, S.1    Sutton, A.2    Muster, N.3    Brown, C.E.4    Yates J.R. III5    Sternglanz, R.6    Workman, J.L.7
  • 49
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • Kimura A, Umehara T, Horikoshi M. Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing. Nat Genet 2002.
    • (2002) Nat Genet
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 50
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
    • Suka N, Luo K, Grunstein M. Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin. Nat Genet 2002;32:378-383.
    • (2002) Nat Genet , vol.32 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 52
    • 0030939235 scopus 로고    scopus 로고
    • The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function
    • Ehrenhofer-Murray AE, Rivier DH, Rine J. The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function. Genetics 1997;145:923-934.
    • (1997) Genetics , vol.145 , pp. 923-934
    • Ehrenhofer-Murray, A.E.1    Rivier, D.H.2    Rine, J.3
  • 53
    • 0033551686 scopus 로고    scopus 로고
    • Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein
    • Iizuka M, Stillman B. Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein. J Biol Chem 1999;274:23027-23034.
    • (1999) J Biol Chem , vol.274 , pp. 23027-23034
    • Iizuka, M.1    Stillman, B.2
  • 54
    • 0035805606 scopus 로고    scopus 로고
    • Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1
    • Burke TW, Cook JG, Asano M, Nevins JR. Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1. J Biol Chem 2001;276:15397-15408.
    • (2001) J Biol Chem , vol.276 , pp. 15397-15408
    • Burke, T.W.1    Cook, J.G.2    Asano, M.3    Nevins, J.R.4
  • 55
    • 0036791653 scopus 로고    scopus 로고
    • Single-molecule analysis reveals clustering and epigenetic regulation of replication origins at the yeast rDNA locus
    • Pasero P, Bensimon A, Schwob E. Single-molecule analysis reveals clustering and epigenetic regulation of replication origins at the yeast rDNA locus. Genes Dev 2002;16:2479-2484.
    • (2002) Genes Dev , vol.16 , pp. 2479-2484
    • Pasero, P.1    Bensimon, A.2    Schwob, E.3
  • 56
    • 0033556028 scopus 로고    scopus 로고
    • Telomeric chromatin modulates replication timing near chromosome ends
    • Stevenson JB, Gottschling DE. Telomeric chromatin modulates replication timing near chromosome ends. Genes Dev 1999;13:146-151.
    • (1999) Genes Dev , vol.13 , pp. 146-151
    • Stevenson, J.B.1    Gottschling, D.E.2
  • 57
    • 0036791764 scopus 로고    scopus 로고
    • Ku complex controls the replication time of DNA in telomere regions
    • Cosgrove AJ, Nieduszynski CA, Donaldson AD. Ku complex controls the replication time of DNA in telomere regions. Genes Dev 2002;16:2485-2490.
    • (2002) Genes Dev , vol.16 , pp. 2485-2490
    • Cosgrove, A.J.1    Nieduszynski, C.A.2    Donaldson, A.D.3
  • 58
    • 0036863542 scopus 로고    scopus 로고
    • Histone acetylation regulates the time of replication origin firing
    • Vogelauer M, Rubbi L, Lucas I, Brewer BJ, Grunstein M. Histone acetylation regulates the time of replication origin firing. Mol Cell 2002;10:1223-1233.
    • (2002) Mol Cell , vol.10 , pp. 1223-1233
    • Vogelauer, M.1    Rubbi, L.2    Lucas, I.3    Brewer, B.J.4    Grunstein, M.5
  • 59
    • 0037019025 scopus 로고    scopus 로고
    • Control of replication timing by a transcriptional silencer
    • Zappulla DC, Sternglanz R, Leatherwood J. Control of replication timing by a transcriptional silencer. Curr Biol 2002;12:869-875.
    • (2002) Curr Biol , vol.12 , pp. 869-875
    • Zappulla, D.C.1    Sternglanz, R.2    Leatherwood, J.3
  • 60
    • 0029089444 scopus 로고
    • Factors affecting the timing and imprinting of replication on a mammalian chromosome
    • Bickmore WA, Carothers AD. Factors affecting the timing and imprinting of replication on a mammalian chromosome. J Cell Sci 1995;108(Pt 8): 2801-2809.
    • (1995) J Cell Sci , vol.108 , Issue.PART 8 , pp. 2801-2809
    • Bickmore, W.A.1    Carothers, A.D.2
  • 61
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker PB, Horz W. ATP-dependent nucleosome remodeling. Annu Rev Biochem 2002;71:247-273.
    • (2002) Annu Rev Biochem , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 62
    • 0036565656 scopus 로고    scopus 로고
    • WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci
    • Bozhenok L, Wade PA, 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
  • 64
    • 0036723627 scopus 로고    scopus 로고
    • Binding of Acf1 to DNA involves a WAC motif and is important for ACF-mediated chromatin assembly
    • Fyodorov DV, Kadonaga JT. Binding of Acf1 to DNA involves a WAC motif and is important for ACF-mediated chromatin assembly. Mol Cell Biol 2002;22:6344-6353.
    • (2002) Mol Cell Biol , vol.22 , pp. 6344-6353
    • Fyodorov, D.V.1    Kadonaga, J.T.2
  • 65
    • 0036153807 scopus 로고    scopus 로고
    • ISWI remodeling complexes in Xenopus egg extracts: Identification as major chromosomal components that are regulated by INCENP-aurora B
    • MacCallum DE, Losada A, Kobayashi R, Hirano T. ISWI remodeling complexes in Xenopus egg extracts: identification as major chromosomal components that are regulated by INCENP-aurora B. Mol Biol Cell 2002;13:25-39.
    • (2002) Mol Biol Cell , vol.13 , pp. 25-39
    • MacCallum, D.E.1    Losada, A.2    Kobayashi, R.3    Hirano, T.4
  • 66
    • 0027429520 scopus 로고
    • Chromatin transitions during early Xenopus embryogenesis: Changes in histone H4 ace-tylation and in linker histone type
    • Dimitrov S, Almouzni G, Dasso M, Wolffe AP. Chromatin transitions during early Xenopus embryogenesis: changes in histone H4 ace-tylation and in linker histone type. Dev Biol 1993;160:214-227.
    • (1993) Dev Biol , vol.160 , pp. 214-227
    • Dimitrov, S.1    Almouzni, G.2    Dasso, M.3    Wolffe, A.P.4
  • 68
    • 0033964661 scopus 로고    scopus 로고
    • Mammalian chromodomain proteins: Their role in genome organisation and expression
    • Jones DO, Cowell IG, Singh PB. Mammalian chromodomain proteins: their role in genome organisation and expression. Bioessays 2000;22:124-137.
    • (2000) Bioessays , vol.22 , pp. 124-137
    • Jones, D.O.1    Cowell, I.G.2    Singh, P.B.3
  • 69
    • 0036558280 scopus 로고    scopus 로고
    • Loss of Heterochromatin Protein 1 (HP1) chromodomain function in mammalian cells by intracellular antibodies causes cell death
    • Filesi I, Cardinale A, van Der Sar S, Cowell IG, Singh PB, Biocca S. Loss of Heterochromatin Protein 1 (HP1) chromodomain function in mammalian cells by intracellular antibodies causes cell death. J Cell Sci 2002;115:1803-1813.
    • (2002) J Cell Sci , vol.115 , pp. 1803-1813
    • Filesi, I.1    Cardinale, A.2    Van Der Sar, S.3    Cowell, I.G.4    Singh, P.B.5    Biocca, S.6
  • 70
    • 0034461595 scopus 로고    scopus 로고
    • Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression
    • O'Carroll D, et al. Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression. Mol Cell Biol 2000;20:9423-9433.
    • (2000) Mol Cell Biol , vol.20 , pp. 9423-9433
    • O'Carroll, D.1
  • 72
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 2000;406:593-599.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 73
    • 0033118322 scopus 로고    scopus 로고
    • Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
    • Aagaard L, et al. Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J 1999;18:1923-1938.
    • (1999) EMBO J , vol.18 , pp. 1923-1938
    • Aagaard, L.1
  • 74
    • 18744374942 scopus 로고    scopus 로고
    • Heterochromatin, HP1 and methylation at lysine 9 of histone H3 in animals
    • Cowell IG, et al. Heterochromatin, HP1 and methylation at lysine 9 of histone H3 in animals. Chromosoma 2002;111:22-36.
    • (2002) Chromosoma , vol.111 , pp. 22-36
    • Cowell, I.G.1
  • 76
    • 0035904395 scopus 로고    scopus 로고
    • Molecular biology of HMGA proteins: Hubs of nuclear function
    • Reeves R. Molecular biology of HMGA proteins: hubs of nuclear function. Gene 2001;277:63-81.
    • (2001) Gene , vol.277 , pp. 63-81
    • Reeves, R.1
  • 77
    • 0034699391 scopus 로고    scopus 로고
    • Chromodomains are protein-RNA interaction modules
    • Akhtar A, Zink D, Becker PB. Chromodomains are protein-RNA interaction modules. Nature 2000;407:405-409.
    • (2000) Nature , vol.407 , pp. 405-409
    • Akhtar, A.1    Zink, D.2    Becker, P.B.3
  • 78
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison C, Bailly D, Peters AH, Quivy JP, Roche D, Taddei A, Lachner M, Jenuwein T, Almouzni G. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat Genet 2002;30:329-334.
    • (2002) Nat Genet , vol.30 , pp. 329-334
    • Maison, C.1    Bailly, D.2    Peters, A.H.3    Quivy, J.P.4    Roche, D.5    Taddei, A.6    Lachner, M.7    Jenuwein, T.8    Almouzni, G.9
  • 79
    • 0036775704 scopus 로고    scopus 로고
    • Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1{alpha}
    • Muchardt C, Guilleme M, Seeler JS, Trouche D, Dejean A, Yaniv M. Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1{alpha}. EMBO Rep 2002;3:975-981.
    • (2002) EMBO Rep , vol.3 , pp. 975-981
    • Muchardt, C.1    Guilleme, M.2    Seeler, J.S.3    Trouche, D.4    Dejean, A.5    Yaniv, M.6
  • 80
    • 0037072661 scopus 로고    scopus 로고
    • Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi
    • Volpe TA, Kidner C, Hall IM, Teng G, Grewal SI, Martienssen RA. Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi. Science 2002;297:1833-1837.
    • (2002) Science , vol.297 , pp. 1833-1837
    • Volpe, T.A.1    Kidner, C.2    Hall, I.M.3    Teng, G.4    Grewal, S.I.5    Martienssen, R.A.6
  • 81
    • 0036641071 scopus 로고    scopus 로고
    • X-chromosome inactivation: Closing in on proteins that bind Xist RNA
    • Brockdorff N. X-chromosome inactivation: closing in on proteins that bind Xist RNA. Trends Genet 2002;18:352-358.
    • (2002) Trends Genet , vol.18 , pp. 352-358
    • Brockdorff, N.1
  • 82
    • 0033613361 scopus 로고    scopus 로고
    • Asynchronous replication of imprinted genes is established in the gametes and maintained during development
    • Simon I, Tenzen T, Reubinoff BE, Hillman D, McCarrey JR, Cedar H. Asynchronous replication of imprinted genes is established in the gametes and maintained during development. Nature 1999;401:929-932.
    • (1999) Nature , vol.401 , pp. 929-932
    • Simon, I.1    Tenzen, T.2    Reubinoff, B.E.3    Hillman, D.4    McCarrey, J.R.5    Cedar, H.6
  • 84
    • 0035777024 scopus 로고    scopus 로고
    • Genome organization, function, and imprinting in Prader-Willi and Angelman syndromes
    • Nicholls RD, Knepper JL. Genome organization, function, and imprinting in Prader-Willi and Angelman syndromes. Annu Rev Genomics Hum Genet 2001;2:153-175.
    • (2001) Annu Rev Genomics Hum Genet , vol.2 , pp. 153-175
    • Nicholls, R.D.1    Knepper, J.L.2
  • 85
    • 0035656688 scopus 로고    scopus 로고
    • Non-coding RNA genes and the modern RNA world
    • Eddy SR. Non-coding RNA genes and the modern RNA world. Nat Rev Genet 2001;2:919-929.
    • (2001) Nat Rev Genet , vol.2 , pp. 919-929
    • Eddy, S.R.1
  • 86
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001;293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 87
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000;403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 88
    • 0037123767 scopus 로고    scopus 로고
    • Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases
    • Robyr D, Suka Y, Xenarios I, Kurdistani SK, Wang A, Suka N, Grunstein M. Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 2002;109:437-446.
    • (2002) Cell , vol.109 , pp. 437-446
    • Robyr, D.1    Suka, Y.2    Xenarios, I.3    Kurdistani, S.K.4    Wang, A.5    Suka, N.6    Grunstein, M.7
  • 89
    • 0035816682 scopus 로고    scopus 로고
    • Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3
    • Tachibana M, Sugimoto K, Fukushima T, Shinkai Y. Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J Biol Chem 2001;276:25309-25317.
    • (2001) J Biol Chem , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 90
    • 0003328368 scopus 로고    scopus 로고
    • Evidence for large domains of similarly expressed genes in the Drosophila genome
    • Spellman PT, Rubin GM. Evidence for large domains of similarly expressed genes in the Drosophila genome. J Biol 2002;1:5.
    • (2002) J Biol , vol.1 , pp. 5
    • Spellman, P.T.1    Rubin, G.M.2
  • 91
    • 0025134076 scopus 로고
    • In vivo studies on the dynamics of histone-DNA interaction: Evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both
    • Jackson V. In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both. Biochemistry 1990;29:719-731.
    • (1990) Biochemistry , vol.29 , pp. 719-731
    • Jackson, V.1
  • 92
    • 0027715686 scopus 로고
    • Parental nucleosomes segregated to newly replicated chromatin are underacetylated relative to those assembled de novo
    • Perry CA, Allis CD, Annunziato AT. Parental nucleosomes segregated to newly replicated chromatin are underacetylated relative to those assembled de novo. Biochemistry 1993;32:13615-13623.
    • (1993) Biochemistry , vol.32 , pp. 13615-13623
    • Perry, C.A.1    Allis, C.D.2    Annunziato, A.T.3
  • 93
    • 0023248714 scopus 로고
    • Deposition of newly synthesized histones: New histones H2A and H2B do not deposit in the same nucleosome with new histones H3 and H4
    • Jackson V. Deposition of newly synthesized histones: new histones H2A and H2B do not deposit in the same nucleosome with new histones H3 and H4. Biochemistry 1987;26:2315-2325.
    • (1987) Biochemistry , vol.26 , pp. 2315-2325
    • Jackson, V.1
  • 94
    • 0023945277 scopus 로고
    • Deposition of newly synthesized histones: Hybrid nucleosomes are not tandemly arranged on daughter DNA strands
    • Jackson V. Deposition of newly synthesized histones: hybrid nucleosomes are not tandemly arranged on daughter DNA strands. Biochemistry 1988;27:2109-2120.
    • (1988) Biochemistry , vol.27 , pp. 2109-2120
    • Jackson, V.1
  • 95
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • Ng HH, Xu RM, Zhang Y, Struhl K. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J Biol Chem 2002;277:34655-34657.
    • (2002) J Biol Chem , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 97
    • 0037078986 scopus 로고    scopus 로고
    • Establishment of transcriptional competence in early and late S phase
    • Zhang J, Xu F, Hashimshony T, Keshet I, Cedar H. Establishment of transcriptional competence in early and late S phase. Nature 2002;420:198-202.
    • (2002) Nature , vol.420 , pp. 198-202
    • Zhang, J.1    Xu, F.2    Hashimshony, T.3    Keshet, I.4    Cedar, H.5
  • 98
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • Sobel RE, Cook RG, Perry CA, Annunziato AT, Allis CD. Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Proc Natl Acad Sci USA 1995:92:1237-1241.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1237-1241
    • Sobel, R.E.1    Cook, R.G.2    Perry, C.A.3    Annunziato, A.T.4    Allis, C.D.5


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