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Volumn 368, Issue 1609, 2013, Pages

Epigenetic inheritance mediated by histone lysine methylation: Maintaining transcriptional states without the precise restoration of marks?

Author keywords

Chromatin modification; Epigenetics; Inheritance; Transcription

Indexed keywords

AMINO ACID; CYTOLOGY; DNA; ENVIRONMENTAL CUE; ENVIRONMENTAL EFFECT; GENOMICS; GERM CELL; HERITABILITY; METHYLATION; PHYSIOLOGICAL RESPONSE; PROTEIN;

EID: 84876539719     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2011.0332     Document Type: Review
Times cited : (52)

References (65)
  • 1
    • 0002021176 scopus 로고    scopus 로고
    • Introduction
    • In, VEA Russo, RA Martienssen, AD Riggs (eds), New York, NY: Cold Spring Harbor Laboratory Press
    • Russo VEA, Martienssen RA, Riggs AD. 1996 Introduction. In Epigenetic mechanisms of gene regulation, VEA Russo, RA Martienssen, AD Riggs (eds), pp. 1-4. New York, NY: Cold Spring Harbor Laboratory Press.
    • (1996) Epigenetic mechanisms of gene regulation , pp. 1-4
    • Russo, V.E.A.1    Martienssen, R.A.2    Riggs, A.D.3
  • 2
    • 36248982297 scopus 로고    scopus 로고
    • Overview and concepts
    • In, CD Allis, T Jenuwein, D Reinberg (eds), New York: Cold Spring Harbor Laboratory
    • Allis CD, Jenuwein T, Reinberg D. 2006 Overview and concepts. In Epigenetics, CD Allis, T Jenuwein, D Reinberg (eds), pp. 23-56. New York: Cold Spring Harbor Laboratory.
    • (2006) Epigenetics , pp. 23-56
    • Allis, C.D.1    Jenuwein, T.2    Reinberg, D.3
  • 3
    • 0016439429 scopus 로고
    • DNA modification mechanisms and gene activity during development
    • (doi:10.1126/science.187. 4173.226)
    • Holliday R, Pugh JE. 1975 DNA modification mechanisms and gene activity during development. Science 187, 226-232. (doi:10.1126/science.187. 4173.226)
    • (1975) Science , vol.187 , pp. 226-232
    • Holliday, R.1    Pugh, J.E.2
  • 4
    • 0026697174 scopus 로고
    • Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain
    • Bestor TH. 1992 Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain. EMBO J. 11, 2611-2617.
    • (1992) EMBO J. , vol.11 , pp. 2611-2617
    • Bestor, T.H.1
  • 5
    • 0030770835 scopus 로고    scopus 로고
    • Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1
    • (doi:10.1126/science.277.5334.1996)
    • Chuang LS, Ian HI, Koh TW, Ng HH, Xu G, Li BF. 1997 Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. Science 277, 1996-2000. (doi:10.1126/science.277.5334.1996)
    • (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
  • 6
    • 9144256125 scopus 로고    scopus 로고
    • The Dnmt1 DNA-(cytosine-C5)-methyltransferase methylates DNA processively with high preference for hemimethylated target sites
    • (doi:10.1074/jbc.M403427200)
    • Hermann A, Goyal R, Jeltsch A. 2004 The Dnmt1 DNA-(cytosine-C5)-methyltransferase methylates DNA processively with high preference for hemimethylated target sites. J. Biol. Chem. 279, 48 350-48 359. (doi:10.1074/jbc.M403427200)
    • (2004) J. Biol. Chem. , vol.279 , pp. 48350-48359
    • Hermann, A.1    Goyal, R.2    Jeltsch, A.3
  • 7
    • 36849072573 scopus 로고    scopus 로고
    • The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA
    • (doi:10.1038/nature06397)
    • Sharif J et al. 2007 The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA. Nature 450, 908-912. (doi:10.1038/nature06397)
    • (2007) Nature , vol.450 , pp. 908-912
    • Sharif, J.1
  • 8
    • 34648833002 scopus 로고    scopus 로고
    • UHRF1 plays a role in maintaining DNA methylation in mammalian cells
    • (doi:10.1126/science.1147939)
    • Bostick M, Kim JK, Esteve PO, Clark A, Pradhan S, Jacobsen SE. 2007 UHRF1 plays a role in maintaining DNA methylation in mammalian cells. Science 317, 1760-1764. (doi:10.1126/science.1147939)
    • (2007) Science , vol.317 , pp. 1760-1764
    • Bostick, M.1    Kim, J.K.2    Esteve, P.O.3    Clark, A.4    Pradhan, S.5    Jacobsen, S.E.6
  • 9
    • 2942746179 scopus 로고    scopus 로고
    • Histone variants, nucleosome assembly and epigenetic inheritance
    • (doi:10. 1016/j.tig.2004.05.004)
    • Henikoff S, Furuyama T, Ahmad K. 2004 Histone variants, nucleosome assembly and epigenetic inheritance. Trends Genet. 20, 320-326. (doi:10. 1016/j.tig.2004.05.004)
    • (2004) Trends Genet. , vol.20 , pp. 320-326
    • Henikoff, S.1    Furuyama, T.2    Ahmad, K.3
  • 10
    • 34250192537 scopus 로고    scopus 로고
    • Mechanisms of epigenetic inheritance
    • (doi:10.1016/j.ceb.2007.04.002)
    • Martin C, Zhang Y. 2007 Mechanisms of epigenetic inheritance. Curr. Opin. Cell Biol. 19, 266-272. (doi:10.1016/j.ceb.2007.04.002)
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 266-272
    • Martin, C.1    Zhang, Y.2
  • 11
    • 60949096069 scopus 로고    scopus 로고
    • Epigenetic inheritance during the cell cycle
    • (doi:10.1038/nrm2640)
    • Probst AV, Dunleavy E, Almouzni G. 2009 Epigenetic inheritance during the cell cycle. Nat. Rev. Mol. Cell Biol. 10, 192-206. (doi:10.1038/nrm2640)
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 192-206
    • Probst, A.V.1    Dunleavy, E.2    Almouzni, G.3
  • 12
    • 79952536795 scopus 로고    scopus 로고
    • Epigenetic inheritance: Uncontested?
    • (doi:10.1038/cr.2011.26)
    • Zhu B, Reinberg D. 2011 Epigenetic inheritance: uncontested? Cell Res. 21, 435-441. (doi:10.1038/cr.2011.26)
    • (2011) Cell Res. , vol.21 , pp. 435-441
    • Zhu, B.1    Reinberg, D.2
  • 13
    • 84857108841 scopus 로고    scopus 로고
    • Histone variants and epigenetic inheritance
    • (doi:10.1016/j.bbagrm.2011.06.007)
    • Yuan G, Zhu B. 2012 Histone variants and epigenetic inheritance. Biochim. Biophys. Acta 1819, 222-229. (doi:10.1016/j.bbagrm.2011.06.007)
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 222-229
    • Yuan, G.1    Zhu, B.2
  • 14
    • 79952283000 scopus 로고    scopus 로고
    • Nucleosome assembly and epigenetic inheritance
    • (doi:10.1007/s13238-010-0104-0)
    • Xu M, Zhu B. 2010 Nucleosome assembly and epigenetic inheritance. Protein Cell 1, 820-829. (doi:10.1007/s13238-010-0104-0)
    • (2010) Protein Cell , vol.1 , pp. 820-829
    • Xu, M.1    Zhu, B.2
  • 15
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • (doi:10.1038/cr.2011.22)
    • Bannister AJ, Kouzarides T. 2011 Regulation of chromatin by histone modifications. Cell Res. 21, 381-395. (doi:10.1038/cr.2011.22)
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 16
    • 80052942443 scopus 로고    scopus 로고
    • Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification
    • (doi:10. 1016/j.cell.2011.08.008)
    • Tan M et al. 2011 Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146, 1016-1028. (doi:10. 1016/j.cell.2011.08.008)
    • (2011) Cell , vol.146 , pp. 1016-1028
    • Tan, M.1
  • 17
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • (doi:10.1016/j.cell.2007.01.015)
    • Li B, Carey M, Workman JL. 2007 The role of chromatin during transcription. Cell 128, 707-719. (doi:10.1016/j.cell.2007.01.015)
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 18
    • 80052805267 scopus 로고    scopus 로고
    • Histone modification: Cause or cog?
    • (doi:10. 1016/j.tig.2011.06.006)
    • Henikoff S, Shilatifard A. 2011 Histone modification: cause or cog? Trends Genet. 27, 389-396. (doi:10. 1016/j.tig.2011.06.006)
    • (2011) Trends Genet. , vol.27 , pp. 389-396
    • Henikoff, S.1    Shilatifard, A.2
  • 19
    • 33947693747 scopus 로고    scopus 로고
    • On the use of the word 'epigenetic'
    • (doi:10. 1016/j.cub.2007.02.030)
    • Ptashne M. 2007 On the use of the word 'epigenetic'. Curr. Biol. 17, R233-R236. (doi:10. 1016/j.cub.2007.02.030)
    • (2007) Curr. Biol. , vol.17
    • Ptashne, M.1
  • 20
    • 77449086407 scopus 로고    scopus 로고
    • In vivo residue-specific histone methylation dynamics
    • (doi:10.1074/jbc.M109.063784)
    • Zee BM, Levin RS, Xu B, LeRoy G, Wingreen NS, Garcia BA. 2010 In vivo residue-specific histone methylation dynamics. J. Biol. Chem. 285, 3341-3350. (doi:10.1074/jbc.M109.063784)
    • (2010) J. Biol. Chem. , vol.285 , pp. 3341-3350
    • Zee, B.M.1    Levin, R.S.2    Xu, B.3    LeRoy, G.4    Wingreen, N.S.5    Garcia, B.A.6
  • 21
    • 0016835983 scopus 로고
    • Studies on highly metabolically active acetylation and phosphorylation of histones
    • Jackson V, Shires A, Chalkley R, Granner DK. 1975 Studies on highly metabolically active acetylation and phosphorylation of histones. J. Biol. Chem. 250, 4856-4863.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4856-4863
    • Jackson, V.1    Shires, A.2    Chalkley, R.3    Granner, D.K.4
  • 22
    • 0018403034 scopus 로고
    • Rapid turnover of acetyl groups in the four core histones of simian virus 40 minichromosomes
    • (doi:10.1073/pnas.76.1.46)
    • Chestier A, Yaniv M. 1979 Rapid turnover of acetyl groups in the four core histones of simian virus 40 minichromosomes. Proc. Natl Acad. Sci. USA 76, 46-50. (doi:10.1073/pnas.76.1.46)
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 46-50
    • Chestier, A.1    Yaniv, M.2
  • 23
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • (doi:10.1038/35020506)
    • Rea S et al. 2000 Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406, 593-599. (doi:10.1038/35020506)
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 24
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • (doi:10.1038/35065132)
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T. 2001 Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410, 116-120. (doi:10.1038/35065132)
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 26
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • (doi:10.1126/science. 1076997)
    • Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, Jones RS, Zhang Y. 2002 Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298, 1039-1043. (doi:10.1126/science. 1076997)
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6    Jones, R.S.7    Zhang, Y.8
  • 27
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • (doi:10.1016/S0092-8674(02)00975-3)
    • Czermin B, Melfi R, McCabe D, Seitz V, Imhof A, Pirrotta V. 2002 Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 111, 185-196. (doi:10.1016/S0092-8674(02)00975-3)
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5    Pirrotta, V.6
  • 28
    • 18644383738 scopus 로고    scopus 로고
    • Histone methyltransferase activity of a Drosophila Polycomb group repressor complex
    • (doi:10.1016/S0092-8674(02)00976-5)
    • Muller J et al. 2002 Histone methyltransferase activity of a Drosophila Polycomb group repressor complex. Cell 111, 197-208. (doi:10.1016/S0092-8674(02)00976-5)
    • (2002) Cell , vol.111 , pp. 197-208
    • Muller, J.1
  • 29
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the enhancer of Zeste protein
    • (doi:10. 1101/gad.1035902)
    • Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D. 2002 Histone methyltransferase activity associated with a human multiprotein complex containing the enhancer of Zeste protein. Genes Dev. 16, 2893-2905. (doi:10. 1101/gad.1035902)
    • (2002) Genes Dev. , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 30
    • 0242668706 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in X inactivation
    • (doi:10.1126/science.1084274)
    • Plath K et al. 2003 Role of histone H3 lysine 27 methylation in X inactivation. Science 300, 131-135. (doi:10.1126/science.1084274)
    • (2003) Science , vol.300 , pp. 131-135
    • Plath, K.1
  • 31
    • 0942268864 scopus 로고    scopus 로고
    • Epigenetic dynamics of imprinted X inactivation during early mouse development
    • (doi:10.1126/science.1092727)
    • Okamoto I, Otte AP, Allis CD, Reinberg D, Heard E. 2004 Epigenetic dynamics of imprinted X inactivation during early mouse development. Science 303, 644-649. (doi:10.1126/science.1092727)
    • (2004) Science , vol.303 , pp. 644-649
    • Okamoto, I.1    Otte, A.P.2    Allis, C.D.3    Reinberg, D.4    Heard, E.5
  • 32
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • (doi:10.1126/science. 1060118)
    • Nakayama J, Rice JC, Strahl BD, Allis CD, Grewal SI. 2001 Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110-113. (doi:10.1126/science. 1060118)
    • (2001) Science , vol.292 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.5
  • 33
    • 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
    • (doi:10.1074/jbc. M101914200)
    • Tachibana M, Sugimoto K, Fukushima T, Shinkai Y. 2001 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. 276, 25 309-25 317. (doi:10.1074/jbc. M101914200)
    • (2001) J. Biol. Chem. , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 34
    • 0037099413 scopus 로고    scopus 로고
    • G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
    • (doi:10.1101/gad.989402)
    • Tachibana M et al. 2002 G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16, 1779-1791. (doi:10.1101/gad.989402)
    • (2002) Genes Dev. , vol.16 , pp. 1779-1791
    • Tachibana, M.1
  • 35
    • 33751209468 scopus 로고    scopus 로고
    • Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication
    • (doi:10. 1101/gad.1463706)
    • Esteve PO, Chin HG, Smallwood A, Feehery GR, Gangisetty O, Karpf AR, Carey MF, Pradhan S. 2006 Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication. Genes Dev. 20, 3089-3103. (doi:10. 1101/gad.1463706)
    • (2006) Genes Dev. , vol.20 , pp. 3089-3103
    • Esteve, P.O.1    Chin, H.G.2    Smallwood, A.3    Feehery, G.R.4    Gangisetty, O.5    Karpf, A.R.6    Carey, M.F.7    Pradhan, S.8
  • 37
    • 70349952171 scopus 로고    scopus 로고
    • Role of the polycomb protein EED in the propagation of repressive histone marks
    • (doi:10.1038/nature08398)
    • Margueron R et al. 2009 Role of the polycomb protein EED in the propagation of repressive histone marks. Nature 461, 762-767. (doi:10.1038/nature08398)
    • (2009) Nature , vol.461 , pp. 762-767
    • Margueron, R.1
  • 38
    • 49649099991 scopus 로고    scopus 로고
    • Polycomb group protein-associated chromatin is reproduced in post-mitotic G1 phase and is required for S phase progression
    • (doi:10.1074/jbc.M709322200)
    • Aoto T, Saitoh N, Sakamoto Y, Watanabe S, Nakao M. 2008 Polycomb group protein-associated chromatin is reproduced in post-mitotic G1 phase and is required for S phase progression. J. Biol. Chem. 283, 18 905-18 915. (doi:10.1074/jbc.M709322200)
    • (2008) J. Biol. Chem. , vol.283 , pp. 18905-18915
    • Aoto, T.1    Saitoh, N.2    Sakamoto, Y.3    Watanabe, S.4    Nakao, M.5
  • 39
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • (doi:10.1074/mcp.M200025-MCP200)
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M. 2002 Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386. (doi:10.1074/mcp.M200025-MCP200)
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 40
    • 37549014575 scopus 로고    scopus 로고
    • Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle
    • (doi:10.1128/MCB.01517-07)
    • Pesavento JJ, Yang H, Kelleher NL, Mizzen CA. 2008 Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle. Mol. Cell Biol. 28, 468-486. (doi:10.1128/MCB.01517-07)
    • (2008) Mol. Cell Biol. , vol.28 , pp. 468-486
    • Pesavento, J.J.1    Yang, H.2    Kelleher, N.L.3    Mizzen, C.A.4
  • 41
    • 69849087056 scopus 로고    scopus 로고
    • Establishment of histone modifications after chromatin assembly
    • (doi:10.1093/nar/gkp518)
    • Scharf AN, Barth TK, Imhof A. 2009 Establishment of histone modifications after chromatin assembly. Nucleic Acids Res. 37, 5032-5040. (doi:10.1093/nar/gkp518).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5032-5040
    • Scharf, A.N.1    Barth, T.K.2    Imhof, A.3
  • 42
    • 77958452889 scopus 로고    scopus 로고
    • Kinetics of re-establishing H3K79 methylation marks in global human chromatin
    • (doi:10.1074/jbc.M110.145094)
    • Sweet SM, Li M, Thomas PM, Durbin KR, Kelleher NL. 2010 Kinetics of re-establishing H3K79 methylation marks in global human chromatin. J. Biol. Chem. 285, 32 778-32 786. (doi:10.1074/jbc.M110.145094)
    • (2010) J. Biol. Chem. , vol.285 , pp. 32778-32786
    • Sweet, S.M.1    Li, M.2    Thomas, P.M.3    Durbin, K.R.4    Kelleher, N.L.5
  • 43
    • 79952281056 scopus 로고    scopus 로고
    • Symmetrical modification within a nucleosome is not required globally for histone lysine methylation
    • (doi:10.1038/embor.2011.6)
    • Chen X, Xiong J, Xu M, Chen S, Zhu B. 2011 Symmetrical modification within a nucleosome is not required globally for histone lysine methylation. EMBO Rep. 12, 244-251. (doi:10.1038/embor.2011.6)
    • (2011) EMBO Rep. , vol.12 , pp. 244-251
    • Chen, X.1    Xiong, J.2    Xu, M.3    Chen, S.4    Zhu, B.5
  • 44
    • 84655170009 scopus 로고    scopus 로고
    • A model for mitotic inheritance of histone lysine methylation
    • (doi:10.1038/embor.2011.206)
    • Xu M, Wang W, Chen S, Zhu B. 2012 A model for mitotic inheritance of histone lysine methylation. EMBO Rep. 13, 60-67. (doi:10.1038/embor.2011.206)
    • (2012) EMBO Rep. , vol.13 , pp. 60-67
    • Xu, M.1    Wang, W.2    Chen, S.3    Zhu, B.4
  • 45
    • 33749657892 scopus 로고    scopus 로고
    • PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state
    • (doi:10.1016/j.molcel. 2006.08.019)
    • Loyola A, Bonaldi T, Roche D, Imhof A, Almouzni G. 2006 PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state. Mol. Cell 24, 309-316. (doi:10.1016/j.molcel. 2006.08.019)
    • (2006) Mol. Cell , vol.24 , pp. 309-316
    • Loyola, A.1    Bonaldi, T.2    Roche, D.3    Imhof, A.4    Almouzni, G.5
  • 46
    • 77950462427 scopus 로고    scopus 로고
    • Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly
    • (doi:10.1126/science.1178994)
    • Xu M, Long C, Chen X, Huang C, Chen S, Zhu B. 2010 Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly. Science 328, 94-98. (doi:10.1126/science.1178994)
    • (2010) Science , vol.328 , pp. 94-98
    • Xu, M.1    Long, C.2    Chen, X.3    Huang, C.4    Chen, S.5    Zhu, B.6
  • 47
    • 80255130208 scopus 로고    scopus 로고
    • Split decision: Why it matters?
    • (doi:10.1007/s11515-011-1040-y)
    • Wu H, Zhu B. 2011 Split decision: why it matters? Front. Biol. 6, 88-92. (doi:10.1007/s11515-011-1040-y)
    • (2011) Front. Biol. , vol.6 , pp. 88-92
    • Wu, H.1    Zhu, B.2
  • 48
    • 79953163378 scopus 로고    scopus 로고
    • Chromatin higher-order structures and gene regulation
    • (doi:10.1016/j.gde.2011.01.022)
    • Li G, Reinberg D. 2011 Chromatin higher-order structures and gene regulation. Curr. Opin. Genet. Dev. 21, 175-186. (doi:10.1016/j.gde.2011.01.022)
    • (2011) Curr. Opin. Genet. Dev. , vol.21 , pp. 175-186
    • Li, G.1    Reinberg, D.2
  • 50
    • 33646882068 scopus 로고    scopus 로고
    • Polycomb complexes repress developmental regulators in murine embryonic stem cells
    • (doi:10.1038/nature04733)
    • Boyer LA et al. 2006 Polycomb complexes repress developmental regulators in murine embryonic stem cells. Nature 441, 349-353. (doi:10.1038/nature04733)
    • (2006) Nature , vol.441 , pp. 349-353
    • Boyer, L.A.1
  • 51
    • 33646865180 scopus 로고    scopus 로고
    • Control of developmental regulators by Polycomb in human embryonic stem cells
    • (doi:10.1016/j.cell.2006.02.043)
    • Lee TI et al. 2006 Control of developmental regulators by Polycomb in human embryonic stem cells. Cell 125, 301-313. (doi:10.1016/j.cell.2006.02.043)
    • (2006) Cell , vol.125 , pp. 301-313
    • Lee, T.I.1
  • 52
    • 33746324216 scopus 로고    scopus 로고
    • Chromatin modifications by methylation and ubiquitination: Implications in the regulation of gene expression
    • (doi:10.1146/annurev.biochem.75. 103004.142422)
    • Shilatifard A. 2006 Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression. Annu. Rev. Biochem. 75, 243-269. (doi:10.1146/annurev.biochem.75. 103004.142422)
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 243-269
    • Shilatifard, A.1
  • 53
    • 2642542643 scopus 로고    scopus 로고
    • A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • (doi:10.1101/gad.300704)
    • Schotta G, Lachner M, Sarma K, Ebert A, Sengupta R, Reuter G, Reinberg D, Jenuwein T. 2004 A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev. 18, 1251-1262. (doi:10.1101/gad.300704)
    • (2004) Genes Dev. , vol.18 , pp. 1251-1262
    • Schotta, G.1    Lachner, M.2    Sarma, K.3    Ebert, A.4    Sengupta, R.5    Reuter, G.6    Reinberg, D.7    Jenuwein, T.8
  • 54
    • 17944380227 scopus 로고    scopus 로고
    • Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability
    • (doi:10.1016/S0092-8674(01)00542-6)
    • Peters AH et al. 2001 Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 107, 323-337. (doi:10.1016/S0092-8674(01)00542-6)
    • (2001) Cell , vol.107 , pp. 323-337
    • Peters, A.H.1
  • 55
    • 10744230544 scopus 로고    scopus 로고
    • Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin
    • (doi:10.1016/s0960-9822(03)00432-9)
    • Lehnertz B et al. 2003 Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin. Curr. Biol. 13, 1192-1200. (doi:10.1016/s0960-9822(03)00432-9)
    • (2003) Curr. Biol. , vol.13 , pp. 1192-1200
    • Lehnertz, B.1
  • 56
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: Knowns and unknowns
    • (doi:10.1038/nrm2763)
    • Simon JA, Kingston RE. 2009 Mechanisms of polycomb gene silencing: knowns and unknowns. Nat. Rev. Mol. Cell Biol. 10, 697-708. (doi:10.1038/nrm2763)
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 57
    • 84857367297 scopus 로고    scopus 로고
    • RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3
    • (doi:10.1016/j.cell. 2011.12.029)
    • Tavares L et al. 2012 RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3. Cell 148, 664-678. (doi:10.1016/j.cell. 2011.12.029)
    • (2012) Cell , vol.148 , pp. 664-678
    • Tavares, L.1
  • 58
    • 55449105221 scopus 로고    scopus 로고
    • Genomewide analysis of PRC1 and PRC2 occupancy identifies two classes of bivalent domains
    • (doi:10.1371/journal.pgen.1000242)
    • Ku M et al. 2008 Genomewide analysis of PRC1 and PRC2 occupancy identifies two classes of bivalent domains. PLoS Genet. 4, e1000242. (doi:10.1371/journal.pgen.1000242)
    • (2008) PLoS Genet. , vol.4
    • Ku, M.1
  • 59
    • 67651022266 scopus 로고    scopus 로고
    • Genome-wide uH2A localization analysis highlights Bmi1-dependent deposition of the mark at repressed genes
    • (doi:10.1371/journal.pgen.1000506)
    • Kallin EM, Cao R, Jothi R, Xia K, Cui K, Zhao K, Zhang Y. 2009 Genome-wide uH2A localization analysis highlights Bmi1-dependent deposition of the mark at repressed genes. PLoS Genet. 5, e1000506. (doi:10.1371/journal.pgen.1000506)
    • (2009) PLoS Genet. , vol.5
    • Kallin, E.M.1    Cao, R.2    Jothi, R.3    Xia, K.4    Cui, K.5    Zhao, K.6    Zhang, Y.7
  • 60
    • 80052009948 scopus 로고    scopus 로고
    • Mechanisms for the inheritance of chromatin states
    • (doi:10.1016/j.cell.2011.07.013)
    • Moazed D. 2011 Mechanisms for the inheritance of chromatin states. Cell 146, 510-518. (doi:10.1016/j.cell.2011.07.013)
    • (2011) Cell , vol.146 , pp. 510-518
    • Moazed, D.1
  • 61
    • 0028004378 scopus 로고
    • Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1
    • (doi:10.1101/gad. 8.19.2257)
    • Moretti P, Freeman K, Coodly L, Shore D. 1994 Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1. Genes Dev. 8, 2257-2269. (doi:10.1101/gad. 8.19.2257)
    • (1994) Genes Dev. , vol.8 , pp. 2257-2269
    • Moretti, P.1    Freeman, K.2    Coodly, L.3    Shore, D.4
  • 62
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • (doi:10.1038/35001622)
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. 2000 Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795-800. (doi:10.1038/35001622)
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 63
    • 0030951007 scopus 로고    scopus 로고
    • Silent information regulator protein complexes in Saccharomyces cerevisiae: A SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3
    • (doi:10.1073/pnas.94.6.2186)
    • Moazed D, Kistler A, Axelrod A, Rine J, Johnson AD. 1997 Silent information regulator protein complexes in Saccharomyces cerevisiae: a SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3. Proc. Natl Acad. Sci. USA 94, 2186-2191. (doi:10.1073/pnas.94.6.2186)
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2186-2191
    • Moazed, D.1    Kistler, A.2    Axelrod, A.3    Rine, J.4    Johnson, A.D.5
  • 64
    • 0031027431 scopus 로고    scopus 로고
    • SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast
    • (doi:10.1101/gad. 11.1.83)
    • Strahl-Bolsinger S, Hecht A, Luo K, Grunstein M. 1997 SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast. Genes Dev. 11, 83-93. (doi:10.1101/gad. 11.1.83)
    • (1997) Genes Dev. , vol.11 , pp. 83-93
    • Strahl-Bolsinger, S.1    Hecht, A.2    Luo, K.3    Grunstein, M.4
  • 65
    • 0028919756 scopus 로고
    • Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
    • (doi:10.1016/0092-8674(95)90512-X)
    • Hecht A, Laroche T, Strahl-Bolsinger S, Gasser SM, Grunstein M. 1995 Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell 80, 583-592. (doi:10.1016/0092-8674(95)90512-X)
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5


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