메뉴 건너뛰기




Volumn 16, Issue 3, 2004, Pages 239-246

Polycomb complexes and silencing mechanisms

Author keywords

cellular memory module; CMM; GAF; GAGA factor; HDAC; heterochromatin protein 1; histone deacetylase; histone methyltransferase; HMTase; HP1; mixed lineage leukaemia; MLL; PcG; Polycomb group; Polycomb repressive complex; Polycomb response element; PRC; PRE; RNAi

Indexed keywords

DNA; HISTONE; LYSINE; METHYLTRANSFERASE; POLYCOMB REPRESSIVE COMPLEX PROTEIN; POLYCOMB RESPONSE ELEMENT PROTEIN; PROTEIN; RNA; TRITHORAX GROUP PROTEIN; TRITHORAX RESPONSE ELEMENT PROTEIN; UNCLASSIFIED DRUG;

EID: 2342475666     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.03.010     Document Type: Review
Times cited : (257)

References (78)
  • 1
    • 0038548210 scopus 로고    scopus 로고
    • Assembly of polycomb complexes and silencing mechanisms
    • Pirrotta V., Poux S., Melfi R., Pilyugin M. Assembly of polycomb complexes and silencing mechanisms. Genetica. 117:2003;191-197
    • (2003) Genetica , vol.117 , pp. 191-197
    • Pirrotta, V.1    Poux, S.2    Melfi, R.3    Pilyugin, M.4
  • 2
    • 0037150730 scopus 로고    scopus 로고
    • Polycomb repression: From cellular memory to cellular proliferation and cancer
    • Jacobs J.J., van Lohuizen M. Polycomb repression: from cellular memory to cellular proliferation and cancer. Biochim Biophys Acta. 1602:2002;151-161
    • (2002) Biochim Biophys Acta , vol.1602 , pp. 151-161
    • Jacobs, J.J.1    Van Lohuizen, M.2
  • 3
    • 0141785202 scopus 로고    scopus 로고
    • Gene repression by polycomb group protein complexes: A distinct complex for every occasion?
    • Otte A.P., Kwaks T.H. Gene repression by polycomb group protein complexes: a distinct complex for every occasion? Curr Opin Genet Dev. 13:2003;448-454
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 448-454
    • Otte, A.P.1    Kwaks, T.H.2
  • 4
    • 0037423933 scopus 로고    scopus 로고
    • Polycomb, epigenomes, and control of cell identity
    • Orlando V. Polycomb, epigenomes, and control of cell identity. Cell. 112:2003;599-606
    • (2003) Cell , vol.112 , pp. 599-606
    • Orlando, V.1
  • 5
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in polycomb-group silencing
    • A human PRC2 complex is purified and found to contain HMTase activity directed toward K27 of histone H3. Functional verification is obtained in Drosophila using a temperature-sensitive allele of E(Z); in this manner, enzymatic activity is pinpointed to this protein. Using chromatin immunoprecipitation, it is demonstrated that loss of E(Z) function abolishes K27 methylation of, and Pc binding to, the upstream regulatory region of Ubx.
    • Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y. Role of histone H3 lysine 27 methylation in polycomb-group silencing. Science. 298:2002;1039-1043 A human PRC2 complex is purified and found to contain HMTase activity directed toward K27 of histone H3. Functional verification is obtained in Drosophila using a temperature-sensitive allele of E(Z); in this manner, enzymatic activity is pinpointed to this protein. Using chromatin immunoprecipitation, it is demonstrated that loss of E(Z) function abolishes K27 methylation of, and Pc binding to, the upstream regulatory region of Ubx.
    • (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
  • 6
    • 18644383738 scopus 로고    scopus 로고
    • Histone methyltransferase activity of a Drosophila Polycomb group repressor complex
    • A PRC2 complex containing ESC, E(Z), NURF-55 and SU(Z)12 is purified from Drosophila embryos, reconstituted in vitro, and found to display H3 K27-directed HMTase activity. Mutations in E(Z) are found to abolish HMTase activity. Using a transgene rescue assay in E(Z)-mutant flies, the authors demonstrate that E(Z) is required to maintain silencing of different HOX genes in imaginal discs.
    • Muller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A. Histone methyltransferase activity of a Drosophila Polycomb group repressor complex. Cell. 111:2002;197-208 A PRC2 complex containing ESC, E(Z), NURF-55 and SU(Z)12 is purified from Drosophila embryos, reconstituted in vitro, and found to display H3 K27-directed HMTase activity. Mutations in E(Z) are found to abolish HMTase activity. Using a transgene rescue assay in E(Z)-mutant flies, the authors demonstrate that E(Z) is required to maintain silencing of different HOX genes in imaginal discs.
    • (2002) Cell , vol.111 , pp. 197-208
    • Muller, J.1    Hart, C.M.2    Francis, N.J.3    Vargas, M.L.4    Sengupta, A.5    Wild, B.6    Miller, E.L.7    O'Connor, M.B.8    Kingston, R.E.9    Simon, J.A.10
  • 7
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • A human PRC2 complex is isolated from 293 cells using epitope-tagged EED. The purified complex is found to methylate K9 and K27 of histone H3 in a manner dependent on an intact SET domain in EZH2. In pull-down assays using modified histone H3 peptides, it is demonstrated that methylated K27 provides a binding site for Pc.
    • Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 16:2002;2893-2905 A human PRC2 complex is isolated from 293 cells using epitope-tagged EED. The purified complex is found to methylate K9 and K27 of histone H3 in a manner dependent on an intact SET domain in EZH2. In pull-down assays using modified histone H3 peptides, it is demonstrated that methylated K27 provides a binding site for Pc.
    • (2002) Genes Dev , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 8
  • 9
    • 0035476530 scopus 로고    scopus 로고
    • Establishment of Polycomb silencing requires a transient interaction between PC and ESC
    • Poux S., Melfi R., Pirrotta V. Establishment of Polycomb silencing requires a transient interaction between PC and ESC. Genes Dev. 15:2001;2509-2514
    • (2001) Genes Dev , vol.15 , pp. 2509-2514
    • Poux, S.1    Melfi, R.2    Pirrotta, V.3
  • 10
    • 0346787823 scopus 로고    scopus 로고
    • Anything else but GAGA: A nonhistone protein complex reshapes chromatin structure
    • Lehmann M. Anything else but GAGA: a nonhistone protein complex reshapes chromatin structure. Trends Genet. 20:2004;15-22
    • (2004) Trends Genet , vol.20 , pp. 15-22
    • Lehmann, M.1
  • 11
    • 1242339582 scopus 로고    scopus 로고
    • Propagation of silencing: Recruitment and repression of native chromatin in trans by polycomb repressed chromatin
    • Lavigne M., Francis N.J., King I.F.G., Kingston R.E. Propagation of silencing: recruitment and repression of native chromatin in trans by polycomb repressed chromatin. Mol Cell. 13:2004;415-425
    • (2004) Mol Cell , vol.13 , pp. 415-425
    • Lavigne, M.1    Francis, N.J.2    King, I.F.G.3    Kingston, R.E.4
  • 12
    • 0032169352 scopus 로고    scopus 로고
    • Binding of trithorax and Polycomb proteins to the bithorax complex: Dynamic changes during early Drosophila embryogenesis
    • Orlando V., Jane E.P., Chinwalla V., Harte P.J., Paro R. Binding of trithorax and Polycomb proteins to the bithorax complex: dynamic changes during early Drosophila embryogenesis. EMBO J. 17:1998;5141-5150
    • (1998) EMBO J , vol.17 , pp. 5141-5150
    • Orlando, V.1    Jane, E.P.2    Chinwalla, V.3    Harte, P.J.4    Paro, R.5
  • 13
    • 0038613098 scopus 로고    scopus 로고
    • A global control region defines a chromosomal regulatory landscape containing the HoxD cluster
    • Using an enhancer-trap approach, a novel cis-regulatory element, the global control region, is identified in the mouse HoxD complex. The global control region is highly conserved over the course of evolution, and is found to regulate the expression of structurally and functionally unrelated genes over distances of several 100 kb. In line with previous studies on the β-globin locus control region, this study underlines the importance of regulatory master switches on top of gene-specific regulation.
    • Spitz F., Gonzalez F., Duboule D. A global control region defines a chromosomal regulatory landscape containing the HoxD cluster. Cell. 113:2003;405-417 Using an enhancer-trap approach, a novel cis-regulatory element, the global control region, is identified in the mouse HoxD complex. The global control region is highly conserved over the course of evolution, and is found to regulate the expression of structurally and functionally unrelated genes over distances of several 100 kb. In line with previous studies on the β-globin locus control region, this study underlines the importance of regulatory master switches on top of gene-specific regulation.
    • (2003) Cell , vol.113 , pp. 405-417
    • Spitz, F.1    Gonzalez, F.2    Duboule, D.3
  • 14
    • 0038606976 scopus 로고    scopus 로고
    • The Drosophila Corto protein interacts with Polycomb-group proteins and the GAGA factor
    • Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F. The Drosophila Corto protein interacts with Polycomb-group proteins and the GAGA factor. Nucleic Acids Res. 31:2003;2873-2882
    • (2003) Nucleic Acids Res , vol.31 , pp. 2873-2882
    • Salvaing, J.1    Lopez, A.2    Boivin, A.3    Deutsch, J.S.4    Peronnet, F.5
  • 15
    • 0031595103 scopus 로고    scopus 로고
    • Chromo-domain proteins: Linking chromatin structure to epigenetic regulation
    • Cavalli G., Paro R. Chromo-domain proteins: linking chromatin structure to epigenetic regulation. Curr Opin Cell Biol. 10:1998;354-360
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 354-360
    • Cavalli, G.1    Paro, R.2
  • 16
    • 0036337565 scopus 로고    scopus 로고
    • The Drosophila trithorax protein is a coactivator required to prevent re-establishment of polycomb silencing
    • Poux S., Horard B., Sigrist C.J., Pirrotta V. The Drosophila trithorax protein is a coactivator required to prevent re-establishment of polycomb silencing. Development. 129:2002;2483-2493
    • (2002) Development , vol.129 , pp. 2483-2493
    • Poux, S.1    Horard, B.2    Sigrist, C.J.3    Pirrotta, V.4
  • 17
    • 0036337390 scopus 로고    scopus 로고
    • Pipsqueak encodes a factor essential for sequence-specific targeting of a polycomb group protein complex
    • Huang D.H., Chang Y.L., Yang C.C., Pan I.C., King B. Pipsqueak encodes a factor essential for sequence-specific targeting of a polycomb group protein complex. Mol Cell Biol. 22:2002;6261-6271
    • (2002) Mol Cell Biol , vol.22 , pp. 6261-6271
    • Huang, D.H.1    Chang, Y.L.2    Yang, C.C.3    Pan, I.C.4    King, B.5
  • 18
    • 0242362735 scopus 로고    scopus 로고
    • Genome-wide prediction of Polycomb/Trithorax response elements in Drosophila melanogaster
    • In silico prediction of 167 candidate PREs on the basis of the presence of clustered binding sites for Pho, GAF and Zeste. A subset of the predicted PREs are subsequently verified using chromatin immunoprecipitation and transgenic analysis. Scanning of the predicted PREs reveals three novel sequence motifs, potentially representing binding sites for DNA binding proteins.
    • Ringrose L., Rehmsmeier M., Dura J.M., Paro R. Genome-wide prediction of Polycomb/Trithorax response elements in Drosophila melanogaster. Dev Cell. 5:2003;759-771 In silico prediction of 167 candidate PREs on the basis of the presence of clustered binding sites for Pho, GAF and Zeste. A subset of the predicted PREs are subsequently verified using chromatin immunoprecipitation and transgenic analysis. Scanning of the predicted PREs reveals three novel sequence motifs, potentially representing binding sites for DNA binding proteins.
    • (2003) Dev Cell , vol.5 , pp. 759-771
    • Ringrose, L.1    Rehmsmeier, M.2    Dura, J.M.3    Paro, R.4
  • 19
    • 0032087892 scopus 로고    scopus 로고
    • The Drosophila polycomb group gene pleiohomeotic encodes a DNA binding protein with homology to the transcription factor YY1
    • Brown J.L., Mucci D., Whiteley M., Dirksen M.L., Kassis J.A. The Drosophila polycomb group gene pleiohomeotic encodes a DNA binding protein with homology to the transcription factor YY1. Mol Cell. 1:1998;1057-1064
    • (1998) Mol Cell , vol.1 , pp. 1057-1064
    • Brown, J.L.1    Mucci, D.2    Whiteley, M.3    Dirksen, M.L.4    Kassis, J.A.5
  • 20
    • 0036837870 scopus 로고    scopus 로고
    • Pleiohomeotic can link polycomb to DNA and mediate transcriptional repression
    • Mohd-Sarip A., Venturini F., Chalkley G.E., Verrijzer C.P. Pleiohomeotic can link polycomb to DNA and mediate transcriptional repression. Mol Cell Biol. 22:2002;7473-7483
    • (2002) Mol Cell Biol , vol.22 , pp. 7473-7483
    • Mohd-Sarip, A.1    Venturini, F.2    Chalkley, G.E.3    Verrijzer, C.P.4
  • 21
    • 0035148407 scopus 로고    scopus 로고
    • Recruitment of components of polycomb group chromatin complexes in Drosophila
    • Poux S., McCabe D., Pirrotta V. Recruitment of components of polycomb group chromatin complexes in Drosophila. Development. 128:2001;75-85
    • (2001) Development , vol.128 , pp. 75-85
    • Poux, S.1    McCabe, D.2    Pirrotta, V.3
  • 22
    • 0242380629 scopus 로고    scopus 로고
    • GAGA facilitates binding of pleiohomeotic to a chromatinized Polycomb response element
    • Mahmoudi T., Zuijderduijn L.M., Mohd-Sarip A., Verrijzer C.P. GAGA facilitates binding of pleiohomeotic to a chromatinized Polycomb response element. Nucleic Acids Res. 31:2003;4147-4156
    • (2003) Nucleic Acids Res , vol.31 , pp. 4147-4156
    • Mahmoudi, T.1    Zuijderduijn, L.M.2    Mohd-Sarip, A.3    Verrijzer, C.P.4
  • 23
    • 0037268947 scopus 로고    scopus 로고
    • The Drosophila pho-like gene encodes a YY1-related DNA binding protein that is redundant with pleiohomeotic in homeotic gene silencing
    • Brown J.L., Fritsch C., Mueller J., Kassis J.A. The Drosophila pho-like gene encodes a YY1-related DNA binding protein that is redundant with pleiohomeotic in homeotic gene silencing. Development. 130:2003;285-294
    • (2003) Development , vol.130 , pp. 285-294
    • Brown, J.L.1    Fritsch, C.2    Mueller, J.3    Kassis, J.A.4
  • 24
    • 0035144663 scopus 로고    scopus 로고
    • The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in xenopus embryos
    • Satijn D.P., Hamer K.M., den Blaauwen J., Otte A.P. The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in xenopus embryos. Mol Cell Biol. 21:2001;1360-1369
    • (2001) Mol Cell Biol , vol.21 , pp. 1360-1369
    • Satijn, D.P.1    Hamer, K.M.2    Den Blaauwen, J.3    Otte, A.P.4
  • 25
    • 0344223442 scopus 로고    scopus 로고
    • RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1
    • Garcia E., Marcos-Gutierrez C., del Mar L.M., Moreno J.C., Vidal M. RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1. EMBO J. 18:1999;3404-3418
    • (1999) EMBO J , vol.18 , pp. 3404-3418
    • Garcia, E.1    Marcos-Gutierrez, C.2    Del Mar, L.M.3    Moreno, J.C.4    Vidal, M.5
  • 26
    • 0032880120 scopus 로고    scopus 로고
    • Targeted disruption of mouse Yin Yang 1 transcription factor results in peri-implantation lethality
    • Donohoe M.E., Zhang X., McGinnis L., Biggers J., Li E., Shi Y. Targeted disruption of mouse Yin Yang 1 transcription factor results in peri-implantation lethality. Mol Cell Biol. 19:1999;7237-7244
    • (1999) Mol Cell Biol , vol.19 , pp. 7237-7244
    • Donohoe, M.E.1    Zhang, X.2    McGinnis, L.3    Biggers, J.4    Li, E.5    Shi, Y.6
  • 27
    • 0038095335 scopus 로고    scopus 로고
    • Yin Yang 1, a vertebrate polycomb group gene, regulates antero-posterior neural patterning
    • This paper demonstrates that human YY1 can repress transcription in developing Drosophila embryos in a PcG-dependent manner. The finding that YY1 can functionally compensate for Pho validates YY1 as a PcG protein.
    • Kwon H.J., Chung H.M. Yin Yang 1, a vertebrate polycomb group gene, regulates antero-posterior neural patterning. Biochem Biophys Res Commun. 306:2003;1008-1013 This paper demonstrates that human YY1 can repress transcription in developing Drosophila embryos in a PcG-dependent manner. The finding that YY1 can functionally compensate for Pho validates YY1 as a PcG protein.
    • (2003) Biochem Biophys Res Commun , vol.306 , pp. 1008-1013
    • Kwon, H.J.1    Chung, H.M.2
  • 28
  • 29
    • 0035852632 scopus 로고    scopus 로고
    • The E2F6 transcription factor is a component of the mammalian Bmi1-containing polycomb complex
    • Trimarchi J.M., Fairchild B., Wen J., Lees J.A. The E2F6 transcription factor is a component of the mammalian Bmi1-containing polycomb complex. Proc Natl Acad Sci USA. 98:2001;1519-1524
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1519-1524
    • Trimarchi, J.M.1    Fairchild, B.2    Wen, J.3    Lees, J.A.4
  • 30
    • 0037052539 scopus 로고    scopus 로고
    • A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells
    • Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y. A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. Science. 296:2002;1132-1136
    • (2002) Science , vol.296 , pp. 1132-1136
    • Ogawa, H.1    Ishiguro, K.2    Gaubatz, S.3    Livingston, D.M.4    Nakatani, Y.5
  • 31
    • 0036023975 scopus 로고    scopus 로고
    • Homeotic transformations of the axial skeleton that accompany a targeted deletion of E2f6
    • Storre J., Elsasser H.P., Fuchs M., Ullmann D., Livingston D.M., Gaubatz S. Homeotic transformations of the axial skeleton that accompany a targeted deletion of E2f6. EMBO Rep. 3:2002;695-700
    • (2002) EMBO Rep , vol.3 , pp. 695-700
    • Storre, J.1    Elsasser, H.P.2    Fuchs, M.3    Ullmann, D.4    Livingston, D.M.5    Gaubatz, S.6
  • 34
    • 0031699524 scopus 로고    scopus 로고
    • The polycomb-group gene eed is required for normal morphogenetic movements during gastrulation in the mouse embryo
    • Faust C., Lawson K.A., Schork N.J., Thiel B., Magnuson T. The polycomb-group gene eed is required for normal morphogenetic movements during gastrulation in the mouse embryo. Development. 125:1998;4495-4506
    • (1998) Development , vol.125 , pp. 4495-4506
    • Faust, C.1    Lawson, K.A.2    Schork, N.J.3    Thiel, B.4    Magnuson, T.5
  • 35
    • 0037314175 scopus 로고    scopus 로고
    • Sequential recruitment of HAT and SWI/SNF components to condensed chromatin by VP16
    • Memedula S., Belmont A.S. Sequential recruitment of HAT and SWI/SNF components to condensed chromatin by VP16. Curr Biol. 13:2003;241-246
    • (2003) Curr Biol , vol.13 , pp. 241-246
    • Memedula, S.1    Belmont, A.S.2
  • 36
    • 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 A.H., Quivy J.P., 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. 30:2002;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
  • 37
    • 0036184188 scopus 로고    scopus 로고
    • RNAi related mechanisms affect both transcriptional and posttranscriptional transgene silencing in Drosophila
    • Pal-Bhadra M., Bhadra U., Birchler J.A. RNAi related mechanisms affect both transcriptional and posttranscriptional transgene silencing in Drosophila. Mol Cell. 9:2002;315-327
    • (2002) Mol Cell , vol.9 , pp. 315-327
    • Pal-Bhadra, M.1    Bhadra, U.2    Birchler, J.A.3
  • 38
    • 0037007007 scopus 로고    scopus 로고
    • Using RNA interference to identify genes required for RNA interference
    • Dudley N.R., Labbe J.C., Goldstein B. Using RNA interference to identify genes required for RNA interference. Proc Natl Acad Sci USA. 99:2002;4191-4196
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4191-4196
    • Dudley, N.R.1    Labbe, J.C.2    Goldstein, B.3
  • 39
    • 0031926583 scopus 로고    scopus 로고
    • Chromatin silencing and the maintenance of a functional germline in Caenorhabditis elegans
    • Kelly W.G., Fire A. Chromatin silencing and the maintenance of a functional germline in Caenorhabditis elegans. Development. 125:1998;2451-2456
    • (1998) Development , vol.125 , pp. 2451-2456
    • Kelly, W.G.1    Fire, A.2
  • 40
    • 0038530976 scopus 로고    scopus 로고
    • Telomeric associated sequences of Drosophila recruit polycomb-group proteins in vivo and can induce pairing-sensitive repression
    • Boivin A., Gally C., Netter S., Anxolabehere D., Ronsseray S. Telomeric associated sequences of Drosophila recruit polycomb-group proteins in vivo and can induce pairing-sensitive repression. Genetics. 164:2003;195-208
    • (2003) Genetics , vol.164 , pp. 195-208
    • Boivin, A.1    Gally, C.2    Netter, S.3    Anxolabehere, D.4    Ronsseray, S.5
  • 41
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal polycomb sites
    • A Drosophila PRC2 complex is isolated and E(Z) is found to methylate histone H3 at positions K9 and K27. It is furthermore shown that recombinant Pc binds a K27-methylated histone H3 peptide.
    • Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V. Drosophila enhancer of zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal polycomb sites. Cell. 111:2002;185-196 A Drosophila PRC2 complex is isolated and E(Z) is found to methylate histone H3 at positions K9 and K27. It is furthermore shown that recombinant Pc binds a K27-methylated histone H3 peptide.
    • (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
  • 42
    • 0033398254 scopus 로고    scopus 로고
    • Chromatin-association of the polycomb group protein BMI1 is cell-cycle-regulated and correlates with its phosphorylation status
    • Voncken J.W., Schweizer D., Aagaard L., Sattler L., Jantsch M.F., van Lohuizen M. Chromatin-association of the polycomb group protein BMI1 is cell-cycle-regulated and correlates with its phosphorylation status. J Cell Sci. 112:1999;4627-4639
    • (1999) J Cell Sci , vol.112 , pp. 4627-4639
    • Voncken, J.W.1    Schweizer, D.2    Aagaard, L.3    Sattler, L.4    Jantsch, M.F.5    Van Lohuizen, M.6
  • 43
    • 0032563598 scopus 로고    scopus 로고
    • The human polycomb group complex associates with pericentromeric heterochromatin to form a novel nuclear domain
    • Saurin A.J., Shiels C., Williamson J., Satijn D.P., Otte A.P., Sheer D., Freemont P.S. The human polycomb group complex associates with pericentromeric heterochromatin to form a novel nuclear domain. J Cell Biol. 142:1998;887-898
    • (1998) J Cell Biol , vol.142 , pp. 887-898
    • Saurin, A.J.1    Shiels, C.2    Williamson, J.3    Satijn, D.P.4    Otte, A.P.5    Sheer, D.6    Freemont, P.S.7
  • 45
    • 0036848563 scopus 로고    scopus 로고
    • Transcription through the iab-7 cis-regulatory domain of the bithorax complex interferes with maintenance of polycomb-mediated silencing
    • Hogga I., Karch F. Transcription through the iab-7 cis-regulatory domain of the bithorax complex interferes with maintenance of polycomb-mediated silencing. Development. 129:2002;4915-4922
    • (2002) Development , vol.129 , pp. 4915-4922
    • Hogga, I.1    Karch, F.2
  • 46
    • 0036841029 scopus 로고    scopus 로고
    • Transcription through intergenic chromosomal memory elements of the Drosophila bithorax complex correlates with an epigenetic switch
    • Rank G., Prestel M., Paro R. Transcription through intergenic chromosomal memory elements of the Drosophila bithorax complex correlates with an epigenetic switch. Mol Cell Biol. 22:2002;8026-8034
    • (2002) Mol Cell Biol , vol.22 , pp. 8026-8034
    • Rank, G.1    Prestel, M.2    Paro, R.3
  • 47
    • 0037168637 scopus 로고    scopus 로고
    • Characterization of the intergenic RNA profile at abdominal-A and abdominal-B in the Drosophila bithorax complex
    • Bae E., Calhoun V.C., Levine M., Lewis E.B., Drewell R.A. Characterization of the intergenic RNA profile at abdominal-A and abdominal-B in the Drosophila bithorax complex. Proc Natl Acad Sci USA. 99:2002;16847-16852
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16847-16852
    • Bae, E.1    Calhoun, V.C.2    Levine, M.3    Lewis, E.B.4    Drewell, R.A.5
  • 48
    • 0037168536 scopus 로고    scopus 로고
    • Transcription defines the embryonic domains of cis-regulatory activity at the Drosophila bithorax complex
    • Drewell R.A., Bae E., Burr J., Lewis E.B. Transcription defines the embryonic domains of cis-regulatory activity at the Drosophila bithorax complex. Proc Natl Acad Sci USA. 99:2002;16853-16858
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16853-16858
    • Drewell, R.A.1    Bae, E.2    Burr, J.3    Lewis, E.B.4
  • 49
    • 0024456509 scopus 로고
    • Spatially ordered transcription of regulatory DNA in the bithorax complex of Drosophila
    • Sanchez-Herrero E., Akam M. Spatially ordered transcription of regulatory DNA in the bithorax complex of Drosophila. Development. 107:1989;321-329
    • (1989) Development , vol.107 , pp. 321-329
    • Sanchez-Herrero, E.1    Akam, M.2
  • 50
    • 0038374526 scopus 로고    scopus 로고
    • Transcriptional elongation by RNA polymerase II and histone methylation
    • Gerber M., Shilatifard A. Transcriptional elongation by RNA polymerase II and histone methylation. J Biol Chem. 278:2003;26303-26306
    • (2003) J Biol Chem , vol.278 , pp. 26303-26306
    • Gerber, M.1    Shilatifard, A.2
  • 52
    • 0027445713 scopus 로고
    • The Drosophila polycomb-group gene enhancer of zeste contains a region with sequence similarity to trithorax
    • Jones R.S., Gelbart W.M. The Drosophila polycomb-group gene enhancer of zeste contains a region with sequence similarity to trithorax. Mol Cell Biol. 13:1993;6357-6366
    • (1993) Mol Cell Biol , vol.13 , pp. 6357-6366
    • Jones, R.S.1    Gelbart, W.M.2
  • 56
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by polycomb and HP1 chromodomains
    • Fischle W., Wang Y., Jacobs S.A., Kim Y., Allis C.D., Khorasanizadeh S. Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by polycomb and HP1 chromodomains. Genes Dev. 17:2003;1870-1881
    • (2003) Genes Dev , vol.17 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 58
    • 0041624288 scopus 로고    scopus 로고
    • Structural basis for specific binding of polycomb chromodomain to histone H3 methylated at Lys 27
    • The crystal structure of the chromodomain of Pc in complex with a histone H3 peptide methylated at K27 is solved. The ability of Pc to discriminate between methylation marks at K9 and K27 is found to reside in an extended binding groove in PC, creating additional contact points to the histone tail. Importantly, Pc is found to have the propensity for dimerization, leading the authors to propose a model in which Pc facilitates a more repressive chromatin structure through the linkage of neighboring nucleosomes.
    • Min J., Zhang Y., Xu R.M. Structural basis for specific binding of polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 17:2003;1823-1828 The crystal structure of the chromodomain of Pc in complex with a histone H3 peptide methylated at K27 is solved. The ability of Pc to discriminate between methylation marks at K9 and K27 is found to reside in an extended binding groove in PC, creating additional contact points to the histone tail. Importantly, Pc is found to have the propensity for dimerization, leading the authors to propose a model in which Pc facilitates a more repressive chromatin structure through the linkage of neighboring nucleosomes.
    • (2003) Genes Dev , vol.17 , pp. 1823-1828
    • Min, J.1    Zhang, Y.2    Xu, R.M.3
  • 59
    • 0036839671 scopus 로고    scopus 로고
    • Native and recombinant polycomb group complexes establish a selective block to template accessibility to repress transcription in vitro
    • King I.F., Francis N.J., Kingston R.E. Native and recombinant polycomb group complexes establish a selective block to template accessibility to repress transcription in vitro. Mol Cell Biol. 22:2002;7919-7928
    • (2002) Mol Cell Biol , vol.22 , pp. 7919-7928
    • King, I.F.1    Francis, N.J.2    Kingston, R.E.3
  • 60
    • 0036310641 scopus 로고    scopus 로고
    • Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins
    • Sewalt R.G., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P. Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins. Mol Cell Biol. 22:2002;5539-5553
    • (2002) Mol Cell Biol , vol.22 , pp. 5539-5553
    • Sewalt, R.G.1    Lachner, M.2    Vargas, M.3    Hamer, K.M.4    Den Blaauwen, J.L.5    Hendrix, T.6    Melcher, M.7    Schweizer, D.8    Jenuwein, T.9    Otte, A.P.10
  • 62
    • 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
    • Tachibana M., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M., Fukuda M., Takeda N., Niida H., Kato H., Shinkai Y. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16:2002;1779-1791
    • (2002) Genes Dev , vol.16 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6    Fukuda, M.7    Takeda, N.8    Niida, H.9    Kato, H.10    Shinkai, Y.11
  • 63
    • 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. 276:2001;25309-25317
    • (2001) J Biol Chem , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 64
    • 9144268924 scopus 로고    scopus 로고
    • Partitioning and plasticity of repressive histone methylation states in mammalian chromatin
    • Peters A.H., et al. Partitioning and plasticity of repressive histone methylation states in mammalian chromatin. Mol Cell. 12:2003;1577-1589
    • (2003) Mol Cell , vol.12 , pp. 1577-1589
    • Peters, A.H.1
  • 67
    • 18744410349 scopus 로고    scopus 로고
    • ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation
    • An ALL-1 complex is purified from human K562 cells and found to contain >27 proteins including chromatin remodeling factors, HDACs and members of the TFIID transcriptional initiation complex. ALL-1 is found to have HMTase activity directed towards K4 of histone H3. Using chromatin immunoprecipitation experiments, the ALL-1 complex is localized to the Hoxa9 locus in HeLa cells; transfection with siRNAs against ALL-1 abolishes complex formation and K4 methylation at Hoxa9.
    • Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T., Wassell R., Dubois G., Mazo A., Croce C.M., Canaani E. ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol Cell. 10:2002;1119-1128 An ALL-1 complex is purified from human K562 cells and found to contain >27 proteins including chromatin remodeling factors, HDACs and members of the TFIID transcriptional initiation complex. ALL-1 is found to have HMTase activity directed towards K4 of histone H3. Using chromatin immunoprecipitation experiments, the ALL-1 complex is localized to the Hoxa9 locus in HeLa cells; transfection with siRNAs against ALL-1 abolishes complex formation and K4 methylation at Hoxa9.
    • (2002) Mol Cell , vol.10 , pp. 1119-1128
    • Nakamura, T.1    Mori, T.2    Tada, S.3    Krajewski, W.4    Rozovskaia, T.5    Wassell, R.6    Dubois, G.7    Mazo, A.8    Croce, C.M.9    Canaani, E.10
  • 68
    • 18744373853 scopus 로고    scopus 로고
    • MLL targets SET domain methyltransferase activity to Hox gene promoters
    • -/- fibroblasts, the positive effect of MLL on Hox gene expression is demonstrated and found to correlate with the presence of MLL, acetylated histones and K4-methylated histone H3 on Hox gene promoters. MLL is demonstrated to be a histone-H3-K4-specific HMTase, the activity of which is stimulated by H3 acetylation.
    • -/- fibroblasts, the positive effect of MLL on Hox gene expression is demonstrated and found to correlate with the presence of MLL, acetylated histones and K4-methylated histone H3 on Hox gene promoters. MLL is demonstrated to be a histone-H3-K4-specific HMTase, the activity of which is stimulated by H3 acetylation.
    • (2002) Mol Cell , vol.10 , pp. 1107-1117
    • Milne, T.A.1    Briggs, S.D.2    Brock, H.W.3    Martin, M.E.4    Gibbs, D.5    Allis, C.D.6    Hess, J.L.7
  • 69
    • 0037167839 scopus 로고    scopus 로고
    • Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1
    • The TrxG protein Ash1 is identified as a HMTase capable of methylating histone K4 and K9 and histone H4 K20. The importance of the Ash1-encoded HMTase activity is demonstrated using transgenic flies holding Ash1-dependent reporters. Using chromatin immunoprecipitation from Drosophila S2 cells holding Ash1-Gal4 fusions tethered to reporter constructs reporter activation is found to correlate with, and depend upon, methylation of histone K4 and K9 and histone H4 K20. Importantly, the methylation imprint imposed by Ash1 was identified as a binding site for chromatin remodeling factors Brm and Mor and to inhibit binding of the epigenetic repressors HP1 and Pc.
    • Beisel C., Imhof A., Greene J., Kremmer E., Sauer F. Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1. Nature. 419:2002;857-862 The TrxG protein Ash1 is identified as a HMTase capable of methylating histone K4 and K9 and histone H4 K20. The importance of the Ash1-encoded HMTase activity is demonstrated using transgenic flies holding Ash1-dependent reporters. Using chromatin immunoprecipitation from Drosophila S2 cells holding Ash1-Gal4 fusions tethered to reporter constructs reporter activation is found to correlate with, and depend upon, methylation of histone K4 and K9 and histone H4 K20. Importantly, the methylation imprint imposed by Ash1 was identified as a binding site for chromatin remodeling factors Brm and Mor and to inhibit binding of the epigenetic repressors HP1 and Pc.
    • (2002) Nature , vol.419 , pp. 857-862
    • Beisel, C.1    Imhof, A.2    Greene, J.3    Kremmer, E.4    Sauer, F.5
  • 70
    • 0037298162 scopus 로고    scopus 로고
    • Polycomb group proteins ESC and E(Z) are present in multiple distinct complexes that undergo dynamic changes during development
    • Furuyama T., Tie F., Harte P.J. Polycomb group proteins ESC and E(Z) are present in multiple distinct complexes that undergo dynamic changes during development. Genesis. 35:2003;114-124
    • (2003) Genesis. , vol.35 , pp. 114-124
    • Furuyama, T.1    Tie, F.2    Harte, P.J.3
  • 71
    • 0038492426 scopus 로고    scopus 로고
    • MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein
    • Xia Z.B., Anderson M., Diaz M.O., Zeleznik L. MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein. Proc Natl Acad Sci USA. 100:2003;8342-8347
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8342-8347
    • Xia, Z.B.1    Anderson, M.2    Diaz, M.O.3    Zeleznik, L.4
  • 72
    • 0035093828 scopus 로고    scopus 로고
    • Chromatin profiling using targeted DNA adenine methyltransferase
    • van Steensel B., Delrow J., Henikoff S. Chromatin profiling using targeted DNA adenine methyltransferase. Nat Genet. 27:2001;304-308
    • (2001) Nat Genet , vol.27 , pp. 304-308
    • Van Steensel, B.1    Delrow, J.2    Henikoff, S.3
  • 74
    • 0742304304 scopus 로고    scopus 로고
    • Histone h3.1 and h3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • Epitope-tagged histone H3.1 and H3.3 complexes are purified from HeLa cells. The two complexes are found to contain distinct histone deposition chaperones, CAF-1 and HIRA, respectively, indicating that H3.1 and H3.3 are deposited via distinct nucleosome assembly pathways. Using nucleosome assembly assays, it is shown that H3.1 and H3.3 are deposited via DNA replication-dependent and -independent pathways, respectively. Most interestingly, H3.1 and H3.3 in predeposition complexes are found as heterodimers with histone H4. A model is proposed for semi-conservative nucleosomal assembly in which the parental H3-H4 tetramer is disrupted and segregated evenly onto the daughter DNA strands as H3-H4 dimers.
    • Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y. Histone h3.1 and h3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell. 116:2004;51-61 Epitope-tagged histone H3.1 and H3.3 complexes are purified from HeLa cells. The two complexes are found to contain distinct histone deposition chaperones, CAF-1 and HIRA, respectively, indicating that H3.1 and H3.3 are deposited via distinct nucleosome assembly pathways. Using nucleosome assembly assays, it is shown that H3.1 and H3.3 are deposited via DNA replication-dependent and -independent pathways, respectively. Most interestingly, H3.1 and H3.3 in predeposition complexes are found as heterodimers with histone H4. A model is proposed for semi-conservative nucleosomal assembly in which the parental H3-H4 tetramer is disrupted and segregated evenly onto the daughter DNA strands as H3-H4 dimers.
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 75
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Using microarray analysis it is demonstrated that many genes positively regulated by HTZ1 (the yeast homologue of H2A.Z) cluster near telomeres, thereby suggesting that HTZ1 may have an anti-silencing effect acting to prevent Sir-dependent telomeric silencing. This model is sustained in expression analysis studies using htz1/sir2 double mutants and by chromatin immunoprecipitation experiments showing spreading of repressive histone methylation imprints and Sir proteins in htz1 mutant cells. It is shown that HTZ1 is enriched in euchromatic region and synergizes with boundary elements to prevent spreading of heterochromatin.
    • Meneghini M.D., Wu M., Madhani H.D. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell. 112:2003;725-736 Using microarray analysis it is demonstrated that many genes positively regulated by HTZ1 (the yeast homologue of H2A.Z) cluster near telomeres, thereby suggesting that HTZ1 may have an anti-silencing effect acting to prevent Sir-dependent telomeric silencing. This model is sustained in expression analysis studies using htz1/sir2 double mutants and by chromatin immunoprecipitation experiments showing spreading of repressive histone methylation imprints and Sir proteins in htz1 mutant cells. It is shown that HTZ1 is enriched in euchromatic region and synergizes with boundary elements to prevent spreading of heterochromatin.
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 76
    • 0037961635 scopus 로고    scopus 로고
    • The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling
    • Using reconstituted chromatin templates, the authors demonstrate that macroH2A limits the NF-κB transcription factor's access to chromatin and impairs the SWI/SNF chromatin remodeling complex. The authors speculate that, in contrast to (reversible?) enzymatic modifications of canonical histones, incorporation of variant histones may constitute a long-term epigenetic imprint.
    • Angelov D., Molla A., Perche P.Y., Hans F., Cote J., Khochbin S., Bouvet P., Dimitrov S. The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling. Mol Cell. 11:2003;1033-1041 Using reconstituted chromatin templates, the authors demonstrate that macroH2A limits the NF-κB transcription factor's access to chromatin and impairs the SWI/SNF chromatin remodeling complex. The authors speculate that, in contrast to (reversible?) enzymatic modifications of canonical histones, incorporation of variant histones may constitute a long-term epigenetic imprint.
    • (2003) Mol Cell , vol.11 , pp. 1033-1041
    • Angelov, D.1    Molla, A.2    Perche, P.Y.3    Hans, F.4    Cote, J.5    Khochbin, S.6    Bouvet, P.7    Dimitrov, S.8
  • 77
    • 1442305333 scopus 로고    scopus 로고
    • The cell-cycle regulator geminin inhibits Hox gene function through direct and Polycomb-mediated interactions
    • Luo L., Yang X., Takihara Y., Knoetgen H., Kessel M. The cell-cycle regulator geminin inhibits Hox gene function through direct and Polycomb-mediated interactions. Nature. 427:2004;749-753
    • (2004) Nature , vol.427 , pp. 749-753
    • Luo, L.1    Yang, X.2    Takihara, Y.3    Knoetgen, H.4    Kessel, M.5
  • 78
    • 0942290537 scopus 로고    scopus 로고
    • Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo
    • Fyodorov D.V., Blower M.D., Karpen G.H., Kadonaga J.T. Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo. Genes Dev. 18:2004;170-183
    • (2004) Genes Dev , vol.18 , pp. 170-183
    • Fyodorov, D.V.1    Blower, M.D.2    Karpen, G.H.3    Kadonaga, J.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.