메뉴 건너뛰기




Volumn 426, Issue 20, 2014, Pages 3363-3375

Keeping them all together: β-Propeller domains in histone methyltransferase complexes

Author keywords

chromatin biology; epigenetics; histone; WD40 domain; propeller

Indexed keywords

HISTONE H3; HISTONE H4; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; MULTIPROTEIN COMPLEX; POLYCOMB REPRESSIVE COMPLEX 2; RETINOBLASTOMA BINDING PROTEIN; RETINOBLASTOMA BINDING PROTEIN 5; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; WD REPEAT PROTEIN 5; WD REPEAT PROTEIN 82; HISTONE; LYSINE; PROTEIN BINDING;

EID: 84907577977     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.05.010     Document Type: Review
Times cited : (2)

References (89)
  • 1
    • 79960563344 scopus 로고    scopus 로고
    • Determinants and dynamics of genome accessibility
    • O. Bell, V.K. Tiwari, N.H. Thoma, and D. Schubeler Determinants and dynamics of genome accessibility Nat Rev Genet 12 2011 554 564 10.1038/nrg3017
    • (2011) Nat Rev Genet , vol.12 , pp. 554-564
    • Bell, O.1    Tiwari, V.K.2    Thoma, N.H.3    Schubeler, D.4
  • 2
    • 79959484677 scopus 로고    scopus 로고
    • Signals and combinatorial functions of histone modifications
    • T. Suganuma, and J.L. Workman Signals and combinatorial functions of histone modifications Annu Rev Biochem 80 2011 473 499 10.1146/annurev-biochem-061809-175347
    • (2011) Annu Rev Biochem , vol.80 , pp. 473-499
    • Suganuma, T.1    Workman, J.L.2
  • 4
    • 80053338227 scopus 로고    scopus 로고
    • The many blades of the beta-propeller proteins: Conserved but versatile
    • C.K. Chen, N.L. Chan, and A.H. Wang The many blades of the beta-propeller proteins: conserved but versatile Trends Biochem Sci 36 2011 553 561 10.1016/j.tibs.2011.07.004
    • (2011) Trends Biochem Sci , vol.36 , pp. 553-561
    • Chen, C.K.1    Chan, N.L.2    Wang, A.H.3
  • 5
  • 6
    • 0035023445 scopus 로고    scopus 로고
    • Predicting protein-protein interactions from primary structure
    • J.R. Bock, and D.A. Gough Predicting protein-protein interactions from primary structure Bioinformatics 17 2001 455 460
    • (2001) Bioinformatics , vol.17 , pp. 455-460
    • Bock, J.R.1    Gough, D.A.2
  • 7
    • 0036916852 scopus 로고    scopus 로고
    • Interaction and domain networks of yeast
    • [2-O]
    • S. Wuchty Interaction and domain networks of yeast Proteomics 2 2002 1715 1723 [2-O]
    • (2002) Proteomics , vol.2 , pp. 1715-1723
    • Wuchty, S.1
  • 8
    • 0035824690 scopus 로고    scopus 로고
    • Cloning and characterization of a novel WD-40 repeat protein that dramatically accelerates osteoblastic differentiation
    • F. Gori, P. Divieti, and M.B. Demay Cloning and characterization of a novel WD-40 repeat protein that dramatically accelerates osteoblastic differentiation J Biol Chem 276 2001 46515 46522 10.1074/jbc.M105757200
    • (2001) J Biol Chem , vol.276 , pp. 46515-46522
    • Gori, F.1    Divieti, P.2    Demay, M.B.3
  • 9
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development
    • J. Wysocka, T. Swigut, T.A. Milne, Y. Dou, X. Zhang, and A.L. Burlingame WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development Cell 121 2005 859 872 10.1016/j.cell.2005.03.036
    • (2005) Cell , vol.121 , pp. 859-872
    • Wysocka, J.1    Swigut, T.2    Milne, T.A.3    Dou, Y.4    Zhang, X.5    Burlingame, A.L.6
  • 10
    • 33748949071 scopus 로고    scopus 로고
    • Structural basis for molecular recognition and presentation of histone H3 by WDR5
    • A. Schuetz, A. Allali-Hassani, F. Martin, P. Loppnau, M. Vedadi, and A. Bochkarev Structural basis for molecular recognition and presentation of histone H3 by WDR5 EMBO J 25 2006 4245 4252 10.1038/sj.emboj.7601316
    • (2006) EMBO J , vol.25 , pp. 4245-4252
    • Schuetz, A.1    Allali-Hassani, A.2    Martin, F.3    Loppnau, P.4    Vedadi, M.5    Bochkarev, A.6
  • 11
    • 33646083683 scopus 로고    scopus 로고
    • Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5
    • Z. Han, L. Guo, H. Wang, Y. Shen, X.W. Deng, and J. Chai Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5 Mol Cell 22 2006 137 144 10.1016/j.molcel.2006.03.018
    • (2006) Mol Cell , vol.22 , pp. 137-144
    • Han, Z.1    Guo, L.2    Wang, H.3    Shen, Y.4    Deng, X.W.5    Chai, J.6
  • 12
    • 33746828109 scopus 로고    scopus 로고
    • Molecular recognition of histone H3 by the WD40 protein WDR5
    • J.F. Couture, E. Collazo, and R.C. Trievel Molecular recognition of histone H3 by the WD40 protein WDR5 Nat Struct Mol Biol 13 2006 698 703 10.1038/nsmb1116
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 698-703
    • Couture, J.F.1    Collazo, E.2    Trievel, R.C.3
  • 14
    • 35349030188 scopus 로고    scopus 로고
    • Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive
    • E. Guccione, C. Bassi, F. Casadio, F. Martinato, M. Cesaroni, and H. Schuchlautz Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive Nature 449 2007 933 937 10.1038/nature06166
    • (2007) Nature , vol.449 , pp. 933-937
    • Guccione, E.1    Bassi, C.2    Casadio, F.3    Martinato, F.4    Cesaroni, M.5    Schuchlautz, H.6
  • 15
    • 37249026306 scopus 로고    scopus 로고
    • PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation
    • D. Hyllus, C. Stein, K. Schnabel, E. Schiltz, A. Imhof, and Y. Dou PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation Genes Dev 21 2007 3369 3380 10.1101/gad.447007
    • (2007) Genes Dev , vol.21 , pp. 3369-3380
    • Hyllus, D.1    Stein, C.2    Schnabel, K.3    Schiltz, E.4    Imhof, A.5    Dou, Y.6
  • 16
    • 84856733701 scopus 로고    scopus 로고
    • Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance
    • V. Migliori, J. Muller, S. Phalke, D. Low, M. Bezzi, and W.C. Mok Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance Nat Struct Mol Biol 19 2012 136 144 10.1038/nsmb.2209
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 136-144
    • Migliori, V.1    Muller, J.2    Phalke, S.3    Low, D.4    Bezzi, M.5    Mok, W.C.6
  • 17
    • 84861121994 scopus 로고    scopus 로고
    • Histone H3R2 symmetric dimethylation and histone H3K4 trimethylation are tightly correlated in eukaryotic genomes
    • C.C. Yuan, A.G. Matthews, Y. Jin, C.F. Chen, B.A. Chapman, and T.K. Ohsumi Histone H3R2 symmetric dimethylation and histone H3K4 trimethylation are tightly correlated in eukaryotic genomes Cell Rep 1 2012 83 90 10.1016/j.celrep.2011.12.008
    • (2012) Cell Rep , vol.1 , pp. 83-90
    • Yuan, C.C.1    Matthews, A.G.2    Jin, Y.3    Chen, C.F.4    Chapman, B.A.5    Ohsumi, T.K.6
  • 18
    • 57749108294 scopus 로고    scopus 로고
    • A conserved arginine-containing motif crucial for the assembly and enzymatic activity of the mixed lineage leukemia protein-1 core complex
    • A. Patel, V.E. Vought, V. Dharmarajan, and M.S. Cosgrove A conserved arginine-containing motif crucial for the assembly and enzymatic activity of the mixed lineage leukemia protein-1 core complex J Biol Chem 283 2008 32162 32175 10.1074/jbc.M806317200
    • (2008) J Biol Chem , vol.283 , pp. 32162-32175
    • Patel, A.1    Vought, V.E.2    Dharmarajan, V.3    Cosgrove, M.S.4
  • 19
    • 58049201719 scopus 로고    scopus 로고
    • WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket
    • J.J. Song, and R.E. Kingston WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket J Biol Chem 283 2008 35258 35264 10.1074/jbc.M806900200
    • (2008) J Biol Chem , vol.283 , pp. 35258-35264
    • Song, J.J.1    Kingston, R.E.2
  • 20
    • 84861357093 scopus 로고    scopus 로고
    • The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases
    • P. Zhang, H. Lee, J.S. Brunzelle, and J.F. Couture The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases Nucleic Acids Res 40 2012 4237 4246 10.1093/nar/gkr1235
    • (2012) Nucleic Acids Res , vol.40 , pp. 4237-4246
    • Zhang, P.1    Lee, H.2    Brunzelle, J.S.3    Couture, J.F.4
  • 21
    • 57749084606 scopus 로고    scopus 로고
    • Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide
    • A. Patel, V. Dharmarajan, and M.S. Cosgrove Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide J Biol Chem 283 2008 32158 32161 10.1074/jbc.C800164200
    • (2008) J Biol Chem , vol.283 , pp. 32158-32161
    • Patel, A.1    Dharmarajan, V.2    Cosgrove, M.S.3
  • 22
    • 84864723459 scopus 로고    scopus 로고
    • Structural basis for WDR5 interaction (Win) motif recognition in human SET1 family histone methyltransferases
    • V. Dharmarajan, J.H. Lee, A. Patel, D.G. Skalnik, and M.S. Cosgrove Structural basis for WDR5 interaction (Win) motif recognition in human SET1 family histone methyltransferases J Biol Chem 287 2012 27275 27289 10.1074/jbc.M112.364125
    • (2012) J Biol Chem , vol.287 , pp. 27275-27289
    • Dharmarajan, V.1    Lee, J.H.2    Patel, A.3    Skalnik, D.G.4    Cosgrove, M.S.5
  • 24
    • 77649275506 scopus 로고    scopus 로고
    • Regulation of HOXA2 gene expression by the ATP-dependent chromatin remodeling enzyme CHD8
    • J.A. Yates, T. Menon, B.A. Thompson, and D.A. Bochar Regulation of HOXA2 gene expression by the ATP-dependent chromatin remodeling enzyme CHD8 FEBS Lett 584 2010 689 693 10.1016/j.febslet.2010.01.022
    • (2010) FEBS Lett , vol.584 , pp. 689-693
    • Yates, J.A.1    Menon, T.2    Thompson, B.A.3    Bochar, D.A.4
  • 25
    • 44949144048 scopus 로고    scopus 로고
    • CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes
    • B.A. Thompson, V. Tremblay, G. Lin, and D.A. Bochar CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes Mol Cell Biol 28 2008 3894 3904 10.1128/MCB.00322-08
    • (2008) Mol Cell Biol , vol.28 , pp. 3894-3904
    • Thompson, B.A.1    Tremblay, V.2    Lin, G.3    Bochar, D.A.4
  • 26
    • 57749113198 scopus 로고    scopus 로고
    • Human ATAC is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein
    • Y.L. Wang, F. Faiola, M. Xu, S. Pan, and E. Martinez Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein J Biol Chem 283 2008 33808 33815 10.1074/jbc.M806936200
    • (2008) J Biol Chem , vol.283 , pp. 33808-33815
    • Wang, Y.L.1    Faiola, F.2    Xu, M.3    Pan, S.4    Martinez, E.5
  • 27
    • 20444397430 scopus 로고    scopus 로고
    • Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
    • Y. Dou, T.A. Milne, A.J. Tackett, E.R. Smith, A. Fukuda, and J. Wysocka Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF Cell 121 2005 873 885 10.1016/j.cell.2005.04.031
    • (2005) Cell , vol.121 , pp. 873-885
    • Dou, Y.1    Milne, T.A.2    Tackett, A.J.3    Smith, E.R.4    Fukuda, A.5    Wysocka, J.6
  • 28
    • 77951182263 scopus 로고    scopus 로고
    • Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex
    • Y. Cai, J. Jin, S.K. Swanson, M.D. Cole, S.H. Choi, and L. Florens Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex J Biol Chem 285 2010 4268 4272 10.1074/jbc.C109.087981
    • (2010) J Biol Chem , vol.285 , pp. 4268-4272
    • Cai, Y.1    Jin, J.2    Swanson, S.K.3    Cole, M.D.4    Choi, S.H.5    Florens, L.6
  • 29
    • 84878199030 scopus 로고    scopus 로고
    • Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes
    • R. van Nuland, A.H. Smits, P. Pallaki, P.W. Jansen, M. Vermeulen, and H.T. Timmers Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes Mol Cell Biol 33 2013 2067 2077 10.1128/MCB.01742-12
    • (2013) Mol Cell Biol , vol.33 , pp. 2067-2077
    • Van Nuland, R.1    Smits, A.H.2    Pallaki, P.3    Jansen, P.W.4    Vermeulen, M.5    Timmers, H.T.6
  • 30
    • 58649110597 scopus 로고    scopus 로고
    • Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks
    • S.M. Southall, P.S. Wong, Z. Odho, S.M. Roe, and J.R. Wilson Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks Mol Cell 33 2009 181 191 10.1016/j.molcel.2008.12.029
    • (2009) Mol Cell , vol.33 , pp. 181-191
    • Southall, S.M.1    Wong, P.S.2    Odho, Z.3    Roe, S.M.4    Wilson, J.R.5
  • 33
    • 77958477957 scopus 로고    scopus 로고
    • Characterization of a novel WDR5-binding site that recruits RbBP5 through a conserved motif to enhance methylation of histone H3 lysine 4 by mixed lineage leukemia protein-1
    • Z. Odho, S.M. Southall, and J.R. Wilson Characterization of a novel WDR5-binding site that recruits RbBP5 through a conserved motif to enhance methylation of histone H3 lysine 4 by mixed lineage leukemia protein-1 J Biol Chem 285 2010 32967 32976 10.1074/jbc.M110.159921
    • (2010) J Biol Chem , vol.285 , pp. 32967-32976
    • Odho, Z.1    Southall, S.M.2    Wilson, J.R.3
  • 34
    • 78651240842 scopus 로고    scopus 로고
    • Structural and biochemical insights into MLL1 core complex assembly
    • V. Avdic, P. Zhang, S. Lanouette, A. Groulx, V. Tremblay, and J. Brunzelle Structural and biochemical insights into MLL1 core complex assembly Structure 19 2011 101 108 10.1016/j.str.2010.09.022
    • (2011) Structure , vol.19 , pp. 101-108
    • Avdic, V.1    Zhang, P.2    Lanouette, S.3    Groulx, A.4    Tremblay, V.5    Brunzelle, J.6
  • 35
    • 84893139184 scopus 로고    scopus 로고
    • Histone H3K27 trimethylation inhibits H3 binding and function of SET1-like H3K4 methyltransferase complexes
    • D.H. Kim, Z. Tang, M. Shimada, B. Fierz, B. Houck-Loomis, and M. Bar-Dagen Histone H3K27 trimethylation inhibits H3 binding and function of SET1-like H3K4 methyltransferase complexes Mol Cell Biol 33 2013 4936 4946 10.1128/MCB.00601-13
    • (2013) Mol Cell Biol , vol.33 , pp. 4936-4946
    • Kim, D.H.1    Tang, Z.2    Shimada, M.3    Fierz, B.4    Houck-Loomis, B.5    Bar-Dagen, M.6
  • 36
    • 29244438472 scopus 로고    scopus 로고
    • CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex
    • J.H. Lee, and D.G. Skalnik CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex J Biol Chem 280 2005 41725 41731 10.1074/jbc.M508312200
    • (2005) J Biol Chem , vol.280 , pp. 41725-41731
    • Lee, J.H.1    Skalnik, D.G.2
  • 37
    • 36849046285 scopus 로고    scopus 로고
    • Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS
    • J.S. Lee, A. Shukla, J. Schneider, S.K. Swanson, M.P. Washburn, and L. Florens Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS Cell 131 2007 1084 1096 10.1016/j.cell.2007.09.046
    • (2007) Cell , vol.131 , pp. 1084-1096
    • Lee, J.S.1    Shukla, A.2    Schneider, J.3    Swanson, S.K.4    Washburn, M.P.5    Florens, L.6
  • 38
    • 34250352746 scopus 로고    scopus 로고
    • Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex
    • J.H. Lee, C.M. Tate, J.S. You, and D.G. Skalnik Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex J Biol Chem 282 2007 13419 13428 10.1074/jbc.M609809200
    • (2007) J Biol Chem , vol.282 , pp. 13419-13428
    • Lee, J.H.1    Tate, C.M.2    You, J.S.3    Skalnik, D.G.4
  • 39
    • 37849008702 scopus 로고    scopus 로고
    • Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes
    • J.H. Lee, and D.G. Skalnik Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes Mol Cell Biol 28 2008 609 618 10.1128/MCB.01356-07
    • (2008) Mol Cell Biol , vol.28 , pp. 609-618
    • Lee, J.H.1    Skalnik, D.G.2
  • 40
    • 57349124451 scopus 로고    scopus 로고
    • Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS
    • M. Wu, P.F. Wang, J.S. Lee, S. Martin-Brown, L. Florens, and M. Washburn Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS Mol Cell Biol 28 2008 7337 7344 10.1128/MCB.00976-08
    • (2008) Mol Cell Biol , vol.28 , pp. 7337-7344
    • Wu, M.1    Wang, P.F.2    Lee, J.S.3    Martin-Brown, S.4    Florens, L.5    Washburn, M.6
  • 42
    • 0037126594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4
    • A. Roguev, D. Schaft, A. Shevchenko, W.W. Pijnappel, M. Wilm, and R. Aasland The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4 EMBO J 20 2001 7137 7148 10.1093/emboj/20.24.7137
    • (2001) EMBO J , vol.20 , pp. 7137-7148
    • Roguev, A.1    Schaft, D.2    Shevchenko, A.3    Pijnappel, W.W.4    Wilm, M.5    Aasland, R.6
  • 43
    • 79953291321 scopus 로고    scopus 로고
    • WDR82, a key epigenetics-related factor, plays a crucial role in normal early embryonic development in mice
    • Y. Bi, Z. Lv, Y. Wang, T. Hai, R. Huo, and Z. Zhou WDR82, a key epigenetics-related factor, plays a crucial role in normal early embryonic development in mice Biol Reprod 84 2011 756 764 10.1095/biolreprod.110.084343
    • (2011) Biol Reprod , vol.84 , pp. 756-764
    • Bi, Y.1    Lv, Z.2    Wang, Y.3    Hai, T.4    Huo, R.5    Zhou, Z.6
  • 44
    • 1642309579 scopus 로고    scopus 로고
    • The essential WD repeat protein Swd2 has dual functions in RNA polymerase II transcription termination and lysine 4 methylation of histone H3
    • H. Cheng, X. He, and C. Moore The essential WD repeat protein Swd2 has dual functions in RNA polymerase II transcription termination and lysine 4 methylation of histone H3 Mol Cell Biol 24 2004 2932 2943
    • (2004) Mol Cell Biol , vol.24 , pp. 2932-2943
    • Cheng, H.1    He, X.2    Moore, C.3
  • 46
    • 78751662908 scopus 로고    scopus 로고
    • The Polycomb complex PRC2 and its mark in life
    • R. Margueron, and D. Reinberg The Polycomb complex PRC2 and its mark in life Nature 469 2011 343 349 10.1038/nature09784
    • (2011) Nature , vol.469 , pp. 343-349
    • Margueron, R.1    Reinberg, D.2
  • 47
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • R. Cao, L. Wang, H. Wang, L. Xia, H. Erdjument-Bromage, and P. Tempst Role of histone H3 lysine 27 methylation in Polycomb-group silencing Science 298 2002 1039 1043 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
  • 48
    • 18644383738 scopus 로고    scopus 로고
    • Histone methyltransferase activity of a Drosophila Polycomb group repressor complex
    • J. Muller, C.M. Hart, N.J. Francis, M.L. Vargas, A. Sengupta, and B. Wild Histone methyltransferase activity of a Drosophila Polycomb group repressor complex Cell 111 2002 197 208
    • (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
  • 49
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • B. Czermin, R. Melfi, D. McCabe, V. Seitz, A. Imhof, and V. Pirrotta Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites Cell 111 2002 185 196
    • (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
  • 50
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • A. Kuzmichev, K. Nishioka, H. Erdjument-Bromage, P. Tempst, and D. Reinberg Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein Genes Dev 16 2002 2893 2905
    • (2002) Genes Dev , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 51
    • 3042801308 scopus 로고    scopus 로고
    • SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex
    • R. Cao, and Y. Zhang SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex Mol Cell 15 2004 57 67 10.1016/j.molcel.2004.06.020
    • (2004) Mol Cell , vol.15 , pp. 57-67
    • Cao, R.1    Zhang, Y.2
  • 52
    • 0019369234 scopus 로고
    • A gene product required for correct initiation of segmental determination in Drosophila
    • G. Struhl A gene product required for correct initiation of segmental determination in Drosophila Nature 293 1981 36 41
    • (1981) Nature , vol.293 , pp. 36-41
    • Struhl, G.1
  • 53
    • 0031843056 scopus 로고    scopus 로고
    • Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: Indication for separate Pc-G complexes
    • M. van Lohuizen, M. Tijms, J.W. Voncken, A. Schumacher, T. Magnuson, and E. Wientjens Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexes Mol Cell Biol 18 1998 3572 3579
    • (1998) Mol Cell Biol , vol.18 , pp. 3572-3579
    • Van Lohuizen, M.1    Tijms, M.2    Voncken, J.W.3    Schumacher, A.4    Magnuson, T.5    Wientjens, E.6
  • 54
    • 0031842310 scopus 로고    scopus 로고
    • Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes
    • R.G. Sewalt, J. van der Vlag, M.J. Gunster, K.M. Hamer, J.L. den Blaauwen, and D.P. Satijn Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes Mol Cell Biol 18 1998 3586 3595
    • (1998) Mol Cell Biol , vol.18 , pp. 3586-3595
    • Sewalt, R.G.1    Van Der Vlag, J.2    Gunster, M.J.3    Hamer, K.M.4    Den Blaauwen, J.L.5    Satijn, D.P.6
  • 55
    • 35148822835 scopus 로고    scopus 로고
    • Structural basis of EZH2 recognition by EED
    • Z. Han, X. Xing, M. Hu, Y. Zhang, P. Liu, and J. Chai Structural basis of EZH2 recognition by EED Structure 15 2007 1306 1315 10.1016/j.str.2007.08.007
    • (2007) Structure , vol.15 , pp. 1306-1315
    • Han, Z.1    Xing, X.2    Hu, M.3    Zhang, Y.4    Liu, P.5    Chai, J.6
  • 57
    • 78650613168 scopus 로고    scopus 로고
    • Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2)
    • C. Xu, C. Bian, W. Yang, M. Galka, H. Ouyang, and C. Chen Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2) Proc Natl Acad Sci U S A 107 2010 19266 19271 10.1073/pnas.1008937107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19266-19271
    • Xu, C.1    Bian, C.2    Yang, W.3    Galka, M.4    Ouyang, H.5    Chen, C.6
  • 58
    • 70349952171 scopus 로고    scopus 로고
    • Role of the polycomb protein EED in the propagation of repressive histone marks
    • R. Margueron, N. Justin, K. Ohno, M.L. Sharpe, J. Son, and W.J. Drury Role of the polycomb protein EED in the propagation of repressive histone marks Nature 461 2009 762 767 10.1038/nature08398
    • (2009) Nature , vol.461 , pp. 762-767
    • Margueron, R.1    Justin, N.2    Ohno, K.3    Sharpe, M.L.4    Son, J.5    Drury, W.J.6
  • 59
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • M. Lachner, D. O'Carroll, S. Rea, K. Mechtler, and T. Jenuwein Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins Nature 410 2001 116 120 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
  • 60
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • A.J. Bannister, P. Zegerman, J.F. Partridge, E.A. Miska, J.O. Thomas, and R.C. Allshire Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain Nature 410 2001 120 124 10.1038/35065138
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1    Zegerman, P.2    Partridge, J.F.3    Miska, E.A.4    Thomas, J.O.5    Allshire, R.C.6
  • 62
    • 1942502862 scopus 로고    scopus 로고
    • Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3
    • A. Kuzmichev, T. Jenuwein, P. Tempst, and D. Reinberg Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3 Mol Cell 14 2004 183 193
    • (2004) Mol Cell , vol.14 , pp. 183-193
    • Kuzmichev, A.1    Jenuwein, T.2    Tempst, P.3    Reinberg, D.4
  • 63
    • 33646848438 scopus 로고    scopus 로고
    • Substrate preferences of the EZH2 histone methyltransferase complex
    • C. Martin, R. Cao, and Y. Zhang Substrate preferences of the EZH2 histone methyltransferase complex J Biol Chem 281 2006 8365 8370 10.1074/jbc.M513425200
    • (2006) J Biol Chem , vol.281 , pp. 8365-8370
    • Martin, C.1    Cao, R.2    Zhang, Y.3
  • 64
    • 0027320814 scopus 로고
    • A retinoblastoma-binding protein related to a negative regulator of Ras in yeast
    • Y.W. Qian, Y.C. Wang, R.E. Hollingsworth, D. Jones, N. Ling, and E.Y. Lee A retinoblastoma-binding protein related to a negative regulator of Ras in yeast Nature 364 1993 648 652
    • (1993) Nature , vol.364 , pp. 648-652
    • Qian, Y.W.1    Wang, Y.C.2    Hollingsworth, R.E.3    Jones, D.4    Ling, N.5    Lee, E.Y.6
  • 65
    • 0025735647 scopus 로고
    • A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product
    • S. Huang, W.H. Lee, and E.Y. Lee A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product Nature 350 1991 160 162
    • (1991) Nature , vol.350 , pp. 160-162
    • Huang, S.1    Lee, W.H.2    Lee, E.Y.3
  • 66
    • 0033180082 scopus 로고    scopus 로고
    • Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
    • Y. Zhang, H.H. Ng, H. Erdjument-Bromage, P. Tempst, A. Bird, and D. Reinberg Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation Genes Dev 13 1999 1924 1935
    • (1999) Genes Dev , vol.13 , pp. 1924-1935
    • Zhang, Y.1    Ng, H.H.2    Erdjument-Bromage, H.3    Tempst, P.4    Bird, A.5    Reinberg, D.6
  • 67
    • 0029562736 scopus 로고
    • Purification and properties of an ATP-dependent nucleosome remodeling factor
    • T. Tsukiyama, and C. Wu Purification and properties of an ATP-dependent nucleosome remodeling factor Cell 83 1995 1011 1020
    • (1995) Cell , vol.83 , pp. 1011-1020
    • Tsukiyama, T.1    Wu, C.2
  • 69
    • 0035141264 scopus 로고    scopus 로고
    • The Drosophila Polycomb group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3
    • F. Tie, T. Furuyama, J. Prasad-Sinha, E. Jane, and P.J. Harte The Drosophila Polycomb group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3 Development 128 2001 275 286
    • (2001) Development , vol.128 , pp. 275-286
    • Tie, F.1    Furuyama, T.2    Prasad-Sinha, J.3    Jane, E.4    Harte, P.J.5
  • 70
    • 44149101970 scopus 로고    scopus 로고
    • Diverse functions of WD40 repeat proteins in histone recognition
    • T. Suganuma, S.G. Pattenden, and J.L. Workman Diverse functions of WD40 repeat proteins in histone recognition Genes Dev 22 2008 1265 1268 10.1101/gad.1676208
    • (2008) Genes Dev , vol.22 , pp. 1265-1268
    • Suganuma, T.1    Pattenden, S.G.2    Workman, J.L.3
  • 71
    • 33646589676 scopus 로고    scopus 로고
    • Chaperone-mediated assembly of centromeric chromatin in vitro
    • T. Furuyama, Y. Dalal, and S. Henikoff Chaperone-mediated assembly of centromeric chromatin in vitro Proc Natl Acad Sci U S A 103 2006 6172 6177 10.1073/pnas.0601686103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6172-6177
    • Furuyama, T.1    Dalal, Y.2    Henikoff, S.3
  • 72
    • 44149123117 scopus 로고    scopus 로고
    • Structural basis of histone H4 recognition by p55
    • J.J. Song, J.D. Garlick, and R.E. Kingston Structural basis of histone H4 recognition by p55 Genes Dev 22 2008 1313 1318 10.1101/gad.1653308
    • (2008) Genes Dev , vol.22 , pp. 1313-1318
    • Song, J.J.1    Garlick, J.D.2    Kingston, R.E.3
  • 73
    • 46049093174 scopus 로고    scopus 로고
    • Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46
    • N.V. Murzina, X.Y. Pei, W. Zhang, M. Sparkes, J. Vicente-Garcia, and J.V. Pratap Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46 Structure 16 2008 1077 1085 10.1016/j.str.2008.05.006
    • (2008) Structure , vol.16 , pp. 1077-1085
    • Murzina, N.V.1    Pei, X.Y.2    Zhang, W.3    Sparkes, M.4    Vicente-Garcia, J.5    Pratap, J.V.6
  • 74
    • 79959537973 scopus 로고    scopus 로고
    • Chromatin-modifying complex component Nurf55/p55 associates with histones H3 and H4 and polycomb repressive complex 2 subunit Su(z)12 through partially overlapping binding sites
    • A.J. Nowak, C. Alfieri, C.U. Stirnimann, V. Rybin, F. Baudin, and N. Ly-Hartig Chromatin-modifying complex component Nurf55/p55 associates with histones H3 and H4 and polycomb repressive complex 2 subunit Su(z)12 through partially overlapping binding sites J Biol Chem 286 2011 23388 23396 10.1074/jbc.M110.207407
    • (2011) J Biol Chem , vol.286 , pp. 23388-23396
    • Nowak, A.J.1    Alfieri, C.2    Stirnimann, C.U.3    Rybin, V.4    Baudin, F.5    Ly-Hartig, N.6
  • 75
    • 0037154963 scopus 로고    scopus 로고
    • Cooperation between complexes that regulate chromatin structure and transcription
    • G.J. Narlikar, H.Y. Fan, and R.E. Kingston Cooperation between complexes that regulate chromatin structure and transcription Cell 108 2002 475 487
    • (2002) Cell , vol.108 , pp. 475-487
    • Narlikar, G.J.1    Fan, H.Y.2    Kingston, R.E.3
  • 76
    • 23344450547 scopus 로고    scopus 로고
    • Subunit contributions to histone methyltransferase activities of fly and worm polycomb group complexes
    • C.S. Ketel, E.F. Andersen, M.L. Vargas, J. Suh, S. Strome, and J.A. Simon Subunit contributions to histone methyltransferase activities of fly and worm polycomb group complexes Mol Cell Biol 25 2005 6857 6868 10.1128/MCB.25.16.6857-6868.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 6857-6868
    • Ketel, C.S.1    Andersen, E.F.2    Vargas, M.L.3    Suh, J.4    Strome, S.5    Simon, J.A.6
  • 77
    • 17644410781 scopus 로고    scopus 로고
    • Nucleosome binding and histone methyltransferase activity of Drosophila PRC2
    • M. Nekrasov, B. Wild, and J. Muller Nucleosome binding and histone methyltransferase activity of Drosophila PRC2 EMBO Rep 6 2005 348 353 10.1038/sj.embor.7400376
    • (2005) EMBO Rep , vol.6 , pp. 348-353
    • Nekrasov, M.1    Wild, B.2    Muller, J.3
  • 79
    • 76549105779 scopus 로고    scopus 로고
    • MLL-AF9-induced leukemogenesis requires coexpression of the wild-type Mll allele
    • A.T. Thiel, P. Blessington, T. Zou, D. Feather, X. Wu, and J. Yan MLL-AF9-induced leukemogenesis requires coexpression of the wild-type Mll allele Cancer Cell 17 2010 148 159 10.1016/j.ccr.2009.12.034
    • (2010) Cancer Cell , vol.17 , pp. 148-159
    • Thiel, A.T.1    Blessington, P.2    Zou, T.3    Feather, D.4    Wu, X.5    Yan, J.6
  • 80
    • 0037309997 scopus 로고    scopus 로고
    • Structure of SET domain proteins: A new twist on histone methylation
    • R. Marmorstein Structure of SET domain proteins: a new twist on histone methylation Trends Biochem Sci 28 2003 59 62 10.1016/S0968-0004(03)00007-0
    • (2003) Trends Biochem Sci , vol.28 , pp. 59-62
    • Marmorstein, R.1
  • 81
    • 80455125845 scopus 로고    scopus 로고
    • Structural chemistry of human SET domain protein methyltransferases
    • M. Schapira Structural chemistry of human SET domain protein methyltransferases Curr Chem Genomics 5 2011 85 94 10.2174/1875397301005010085
    • (2011) Curr Chem Genomics , vol.5 , pp. 85-94
    • Schapira, M.1
  • 82
    • 84872531591 scopus 로고    scopus 로고
    • High-affinity, small-molecule peptidomimetic inhibitors of MLL1/WDR5 protein-protein interaction
    • H. Karatas, E.C. Townsend, F. Cao, Y. Chen, D. Bernard, and L. Liu High-affinity, small-molecule peptidomimetic inhibitors of MLL1/WDR5 protein-protein interaction J Am Chem Soc 135 2013 669 682 10.1021/ja306028q
    • (2013) J Am Chem Soc , vol.135 , pp. 669-682
    • Karatas, H.1    Townsend, E.C.2    Cao, F.3    Chen, Y.4    Bernard, D.5    Liu, L.6
  • 83
    • 84892841527 scopus 로고    scopus 로고
    • Targeting MLL1 H3K4 methyltransferase activity in mixed-lineage leukemia
    • F. Cao, E.C. Townsend, H. Karatas, J. Xu, L. Li, and S. Lee Targeting MLL1 H3K4 methyltransferase activity in mixed-lineage leukemia Mol Cell 53 2014 247 261 10.1016/j.molcel.2013.12.001
    • (2014) Mol Cell , vol.53 , pp. 247-261
    • Cao, F.1    Townsend, E.C.2    Karatas, H.3    Xu, J.4    Li, L.5    Lee, S.6
  • 84
    • 84877815031 scopus 로고    scopus 로고
    • EZH2 is required for germinal center formation and somatic EZH2 mutations promote lymphoid transformation
    • W. Beguelin, R. Popovic, M. Teater, Y. Jiang, K.L. Bunting, and M. Rosen EZH2 is required for germinal center formation and somatic EZH2 mutations promote lymphoid transformation Cancer Cell 23 2013 677 692 10.1016/j.ccr.2013.04.011
    • (2013) Cancer Cell , vol.23 , pp. 677-692
    • Beguelin, W.1    Popovic, R.2    Teater, M.3    Jiang, Y.4    Bunting, K.L.5    Rosen, M.6
  • 85
    • 84870573126 scopus 로고    scopus 로고
    • EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations
    • M.T. McCabe, H.M. Ott, G. Ganji, S. Korenchuk, C. Thompson, and G.S. Van Aller EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations Nature 492 2012 108 112 10.1038/nature11606
    • (2012) Nature , vol.492 , pp. 108-112
    • McCabe, M.T.1    Ott, H.M.2    Ganji, G.3    Korenchuk, S.4    Thompson, C.5    Van Aller, G.S.6
  • 86
    • 84888303259 scopus 로고    scopus 로고
    • Identification of EZH2 and EZH1 small molecule inhibitors with selective impact on diffuse large B cell lymphoma cell growth
    • S. Garapaty-Rao, C. Nasveschuk, A. Gagnon, E.Y. Chan, P. Sandy, and J. Busby Identification of EZH2 and EZH1 small molecule inhibitors with selective impact on diffuse large B cell lymphoma cell growth Chem Biol 20 2013 1329 1339 10.1016/j.chembiol.2013.09.013
    • (2013) Chem Biol , vol.20 , pp. 1329-1339
    • Garapaty-Rao, S.1    Nasveschuk, C.2    Gagnon, A.3    Chan, E.Y.4    Sandy, P.5    Busby, J.6
  • 87
    • 84884532954 scopus 로고    scopus 로고
    • Targeted disruption of the EZH2-EED complex inhibits EZH2-dependent cancer
    • W. Kim, G.H. Bird, T. Neff, G. Guo, M.A. Kerenyi, and L.D. Walensky Targeted disruption of the EZH2-EED complex inhibits EZH2-dependent cancer Nat Chem Biol 9 2013 643 650 10.1038/nchembio.1331
    • (2013) Nat Chem Biol , vol.9 , pp. 643-650
    • Kim, W.1    Bird, G.H.2    Neff, T.3    Guo, G.4    Kerenyi, M.A.5    Walensky, L.D.6
  • 88
    • 4444291734 scopus 로고    scopus 로고
    • Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix
    • L.D. Walensky, A.L. Kung, I. Escher, T.J. Malia, S. Barbuto, and R.D. Wright Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix Science 305 2004 1466 1470 10.1126/science.1099191
    • (2004) Science , vol.305 , pp. 1466-1470
    • Walensky, L.D.1    Kung, A.L.2    Escher, I.3    Malia, T.J.4    Barbuto, S.5    Wright, R.D.6
  • 89
    • 84855584802 scopus 로고    scopus 로고
    • Stapled peptides for intracellular drug targets
    • G.L. Verdine, and G.J. Hilinski Stapled peptides for intracellular drug targets Methods Enzymol 503 2012 3 33 10.1016/B978-0-12-396962-0.00001-X
    • (2012) Methods Enzymol , vol.503 , pp. 3-33
    • Verdine, G.L.1    Hilinski, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.