메뉴 건너뛰기




Volumn 25, Issue 7, 2005, Pages 2525-2538

Relationship between histone H3 lysine 9 methylation, transcription repression, and heterochromatin protein 1 recruitment

Author keywords

[No Author keywords available]

Indexed keywords

HETEROCHROMATIN 1; HISTONE H3; LYSINE; METHYLTRANSFERASE; NUCLEAR PROTEIN; UNCLASSIFIED DRUG;

EID: 15044350409     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.7.2525-2538.2005     Document Type: Article
Times cited : (296)

References (64)
  • 1
    • 0033118322 scopus 로고    scopus 로고
    • Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
    • Aagaard, L., G. Laible, P. Selenko, M. Schmid, R. Dorn, G. Schotta, S. Kuhfittig, A. Wolf, A. Lebersorger, P. B. Singh, G. Reuter, and T. Jenuwein. 1999. Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 18:1923-1938.
    • (1999) EMBO J. , vol.18 , pp. 1923-1938
    • Aagaard, L.1    Laible, G.2    Selenko, P.3    Schmid, M.4    Dorn, R.5    Schotta, G.6    Kuhfittig, S.7    Wolf, A.8    Lebersorger, A.9    Singh, P.B.10    Reuter, G.11    Jenuwein, T.12
  • 2
    • 0027385167 scopus 로고
    • Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo
    • Almouzni, G., and A. P. Wolffe. 1993. Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo. Genes Dev. 7:2033-2047.
    • (1993) Genes Dev. , vol.7 , pp. 2033-2047
    • Almouzni, G.1    Wolffe, A.P.2
  • 3
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A. J., and T. Kouzarides. 1996. The CBP co-activator is a histone acetyltransferase. Nature 384:641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 8
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin, C., J. E. Carlson, L. Zeng, C. He, A. K. Aggarwal, and M. M. Zhou. 1999. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399:491-496.
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.M.6
  • 9
    • 1642369447 scopus 로고    scopus 로고
    • The N-terminus of Drosophila SU(VAR)3-9 mediates dimerization and regulates its methyltransferase activity
    • Eskeland, R., B. Czermin, J. Boeke, T. Bonaldi, J. T. Regula, and A. Imhof. 2004. The N-terminus of Drosophila SU(VAR)3-9 mediates dimerization and regulates its methyltransferase activity. Biochemistry 43:3740-3749.
    • (2004) Biochemistry , vol.43 , pp. 3740-3749
    • Eskeland, R.1    Czermin, B.2    Boeke, J.3    Bonaldi, T.4    Regula, J.T.5    Imhof, A.6
  • 10
    • 0034122096 scopus 로고    scopus 로고
    • Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9
    • Firestein, R., X. Cui, P. Huie, and M. L. Cleary. 2000. Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9. Mol. Cell. Biol. 20:4900-4909.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4900-4909
    • Firestein, R.1    Cui, X.2    Huie, P.3    Cleary, M.L.4
  • 11
    • 0035949598 scopus 로고    scopus 로고
    • Transcriptional repression of euchromatic genes by Drosophila heterochromatin protein 1 and histone modifiers
    • Hwang, K. K., J. C. Eissenberg, and H. J. Worman. 2001. Transcriptional repression of euchromatic genes by Drosophila heterochromatin protein 1 and histone modifiers. Proc. Natl. Acad. Sci. USA 98:11423-11427.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11423-11427
    • Hwang, K.K.1    Eissenberg, J.C.2    Worman, H.J.3
  • 12
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs, S. A., and S. Khorasanizadeh. 2002. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295:2080-2083.
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 14
    • 0024445456 scopus 로고
    • Distribution patterns of HP1, a heterochromatin-associated nonhistone chromosomal protein of Drosophila
    • James, T. C., J. C. Eissenberg, C. Craig, V. Dietrich, A. Hobson, and S. C. Elgin. 1989. Distribution patterns of HP1, a heterochromatin-associated nonhistone chromosomal protein of Drosophila. Eur. J. Cell Biol. 50:170-180.
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 170-180
    • James, T.C.1    Eissenberg, J.C.2    Craig, C.3    Dietrich, V.4    Hobson, A.5    Elgin, S.C.6
  • 15
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T., and C. D. Allis. 2001. Translating the histone code. Science 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 16
    • 0028217604 scopus 로고
    • Micrococcal nuclease digestion of nuclei reveals extended nucleosome ladders having anomalous DNA lengths for chromatin assembled on non-replicating plasmids in transfected cells
    • Jeong, S., and A. Stein. 1994. Micrococcal nuclease digestion of nuclei reveals extended nucleosome ladders having anomalous DNA lengths for chromatin assembled on non-replicating plasmids in transfected cells. Nucleic Acids Res. 22:370-375.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 370-375
    • Jeong, S.1    Stein, A.2
  • 17
    • 0037135602 scopus 로고    scopus 로고
    • Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptionai activators
    • Koh, S. S., H. Li, Y. H. Lee, R. B. Widelitz, C. M. Chuong, and M. R. Stallcup. 2002. Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptionai activators. J. Biol. Chem. 277:26031-26035.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26031-26035
    • Koh, S.S.1    Li, H.2    Lee, Y.H.3    Widelitz, R.B.4    Chuong, C.M.5    Stallcup, M.R.6
  • 18
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides, T. 2002. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12:198-209.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 20
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner, M., D. O'Carroll, S. Rea, K. Mechtler, and T. Jenuwein. 2001. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 21
    • 0037087573 scopus 로고    scopus 로고
    • Specific targeting and constitutive association of histone deacetylase complexes during transcriptional repression
    • Li, J., Q. Lin, W. Wang, P. Wade, and J. Wong. 2002. Specific targeting and constitutive association of histone deacetylase complexes during transcriptional repression. Genes Dev. 16:687-692.
    • (2002) Genes Dev. , vol.16 , pp. 687-692
    • Li, J.1    Lin, Q.2    Wang, W.3    Wade, P.4    Wong, J.5
  • 22
    • 0036311564 scopus 로고    scopus 로고
    • Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor
    • Li, J., Q. Lin, H. G. Yoon, Z. Q. Huang, B. D. Strahl, C. D. Allis, and J. Wong. 2002. Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor. Mol. Cell. Biol. 22:5688-5697.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5688-5697
    • Li, J.1    Lin, Q.2    Yoon, H.G.3    Huang, Z.Q.4    Strahl, B.D.5    Allis, C.D.6    Wong, J.7
  • 23
    • 0037059081 scopus 로고    scopus 로고
    • Does heterochromatin protein 1 always follow code?
    • Li, Y., D. A. Kirschmann, and L. L. Wallrath. 2002. Does heterochromatin protein 1 always follow code? Proc. Natl. Acad. Sci. USA 99(Suppl. 4):16462-16469.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.4 SUPPL. , pp. 16462-16469
    • Li, Y.1    Kirschmann, D.A.2    Wallrath, L.L.3
  • 24
    • 0023815070 scopus 로고
    • Dosage-dependent modifiers of position effect variegation in Drosophila and a mass action model that explains their effect
    • Locke, J., M. A. Kotarski, and K. D. Tartof. 1988. Dosage-dependent modifiers of position effect variegation in Drosophila and a mass action model that explains their effect. Genetics 120:181-198.
    • (1988) Genetics , vol.120 , pp. 181-198
    • Locke, J.1    Kotarski, M.A.2    Tartof, K.D.3
  • 25
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison, C., D. Bailly, A. H. Peters, J. P. Quivy, D. Roche, A. Taddei, M. Lachner, T. Jenuwein, and G. Almouzni. 2002. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat. Genet. 30:329-334.
    • (2002) Nat. Genet. , vol.30 , pp. 329-334
    • Maison, C.1    Bailly, D.2    Peters, A.H.3    Quivy, J.P.4    Roche, D.5    Taddei, A.6    Lachner, M.7    Jenuwein, T.8    Almouzni, G.9
  • 26
    • 0038613861 scopus 로고    scopus 로고
    • HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain
    • Meehan, R. R., C. F. Kao, and S. Pennings. 2003. HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain. EMBO J. 22:3164-3174.
    • (2003) EMBO J. , vol.22 , pp. 3164-3174
    • Meehan, R.R.1    Kao, C.F.2    Pennings, S.3
  • 27
    • 0034056777 scopus 로고    scopus 로고
    • Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression
    • Melcher, M., M. Schmid, L. Aagaard, P. Selenko, G. Laible, and T. Jenuwein. 2000. Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression. Mol. Cell. Biol. 20:3728-3741.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3728-3741
    • Melcher, M.1    Schmid, M.2    Aagaard, L.3    Selenko, P.4    Laible, G.5    Jenuwein, T.6
  • 28
    • 0036775704 scopus 로고    scopus 로고
    • Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1α
    • Muchardt, C., M. Guilleme, J. S. Seeler, D. Trouche, A. Dejean, and M. Yaniv. 2002. Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1α. EMBO Rep. 3:975-981.
    • (2002) EMBO Rep. , vol.3 , pp. 975-981
    • Muchardt, C.1    Guilleme, M.2    Seeler, J.S.3    Trouche, D.4    Dejean, A.5    Yaniv, M.6
  • 29
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • Nakayama, J., J. C. Rice, B. D. Strahl, C. D. Allis, and S. I. Grewal. 2001. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292:110-113.
    • (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
  • 30
    • 0037452770 scopus 로고    scopus 로고
    • Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: A potential mechanism for position-effect variegation
    • Ng, H. H., D. N. Ciccone, K. B. Morshead, M. A. Oettinger, and K. Struhl. 2003. Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation. Proc. Natl. Acad. Sci. USA 100:1820-1825.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1820-1825
    • Ng, H.H.1    Ciccone, D.N.2    Morshead, K.B.3    Oettinger, M.A.4    Struhl, K.5
  • 31
    • 0033571206 scopus 로고    scopus 로고
    • Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family
    • Nielsen, A. L., J. A. Ortiz, J. You, M. Oulad-Abdelghani, R. Khechumian, A. Gansmuller, P. Chambon, and R. Losson. 1999. Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. EMBO J. 18:6385-6395.
    • (1999) EMBO J. , vol.18 , pp. 6385-6395
    • Nielsen, A.L.1    Ortiz, J.A.2    You, J.3    Oulad-Abdelghani, M.4    Khechumian, R.5    Gansmuller, A.6    Chambon, P.7    Losson, R.8
  • 34
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka, K., S. Chuikov, K. Sarma, H. Erdjument-Bromage, C. D. Allis, P. Tempst, and D. Reinberg. 2002. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16:479-489.
    • (2002) Genes Dev. , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7
  • 35
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V. V., R. L. Schiltz, V. Russanova, B. H. Howard, and Y. Nakatani. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 36
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p
    • Owen, D. J., P. Ornaghi, J. C. Yang, N. Lowe, P. R. Evans, P. Ballario, D. Neuhaus, P. Filetici, and A. A. Travers. 2000. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p. EMBO J. 19:6141-6149.
    • (2000) EMBO J. , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.C.3    Lowe, N.4    Evans, P.R.5    Ballario, P.6    Neuhaus, D.7    Filetici, P.8    Travers, A.A.9
  • 37
    • 0942279615 scopus 로고    scopus 로고
    • Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery
    • Pal-Bhadra, M., B. A. Leibovitch, S. G. Gandhi, M. Rao, U. Bhadra, J. A. Birchler, and S. C. Elgin. 2004. Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery. Science 303:669-672.
    • (2004) Science , vol.303 , pp. 669-672
    • Pal-Bhadra, M.1    Leibovitch, B.A.2    Gandhi, S.G.3    Rao, M.4    Bhadra, U.5    Birchler, J.A.6    Elgin, S.C.7
  • 42
    • 0033013868 scopus 로고    scopus 로고
    • KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: A potential role for Kruppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing
    • Ryan, R. F., D. C. Schultz, K. Ayyanathan, P. B. Singh, J. R. Friedman, W. J. Fredericks, and F. J. Rauscher III. 1999. KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Kruppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing. Mol. Cell. Biol. 19:4366-4378.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4366-4378
    • Ryan, R.F.1    Schultz, D.C.2    Ayyanathan, K.3    Singh, P.B.4    Friedman, J.R.5    Fredericks, W.J.6    Rauscher III, F.J.7
  • 43
    • 0036499971 scopus 로고    scopus 로고
    • Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing
    • Schotta, G., A. Ebert, V. Krauss, A. Fischer, J. Hoffmann, S. Rea, T. Jenuwein, R. Dorn, and G. Reuter. 2002. Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing. EMBO J. 21:1121-1131.
    • (2002) EMBO J. , vol.21 , pp. 1121-1131
    • Schotta, G.1    Ebert, A.2    Krauss, V.3    Fischer, A.4    Hoffmann, J.5    Rea, S.6    Jenuwein, T.7    Dorn, R.8    Reuter, G.9
  • 44
    • 0037089626 scopus 로고    scopus 로고
    • SETDB1: A novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins
    • Schultz, D. C., K. Ayyanathan, D. Negorev, G. G. Maul, and F. J. Rauscher III. 2002. SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 16:919-932.
    • (2002) Genes Dev. , vol.16 , pp. 919-932
    • Schultz, D.C.1    Ayyanathan, K.2    Negorev, D.3    Maul, G.G.4    Rauscher III, F.J.5
  • 45
    • 0037164741 scopus 로고    scopus 로고
    • Gene-specific targeting of H3K9 methylation is sufficient for initiating repression in vivo
    • Snowden, A. W., P. D. Gregory, C. C. Case, and C. O. Pabo. 2002. Gene-specific targeting of H3K9 methylation is sufficient for initiating repression in vivo. Curr. Biol. 12:2159-2166.
    • (2002) Curr. Biol. , vol.12 , pp. 2159-2166
    • Snowden, A.W.1    Gregory, P.D.2    Case, C.C.3    Pabo, C.O.4
  • 47
    • 85047686621 scopus 로고    scopus 로고
    • Interferon-tau (IFNτ) regulation of IFN-stimulated gene expression in cell lines lacking specific IFN-signaling components
    • Stewart, M. D., G. A. Johnson, F. W. Bazer, and T. E. Spencer. 2001. Interferon-tau (IFNτ) regulation of IFN-stimulated gene expression in cell lines lacking specific IFN-signaling components. Endocrinology 142:1786-1794.
    • (2001) Endocrinology , vol.142 , pp. 1786-1794
    • Stewart, M.D.1    Johnson, G.A.2    Bazer, F.W.3    Spencer, T.E.4
  • 48
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D., and C. D. Allis. 2000. The language of covalent histone modifications. Nature 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 49
    • 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., K. Sugimoto, T. Fukushima, and Y. Shinkai. 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. 276:25309-25317.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 50
    • 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., K. Sugimoto, M. Nozaki, J. Ueda, T. Ohta, M. Ohki, M. Fukuda, N. Takeda, H. Niida, H. Kato, and Y. Shinkai. 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.
    • (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
  • 52
    • 0028110864 scopus 로고
    • The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes
    • Tschiersch, B., A. Hofmann, V. Krauss, R. Dorn, G. Korge, and G. Reuter. 1994. The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes. EMBO J. 13:3822-3831.
    • (1994) EMBO J. , vol.13 , pp. 3822-3831
    • Tschiersch, B.1    Hofmann, A.2    Krauss, V.3    Dorn, R.4    Korge, G.5    Reuter, G.6
  • 53
    • 0037079677 scopus 로고    scopus 로고
    • Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases
    • Vaute, O., E. Nicolas, L. Vandel, and D. Trouche. 2002. Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases. Nucleic Acids Res. 30:475-481.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 475-481
    • Vaute, O.1    Nicolas, E.2    Vandel, L.3    Trouche, D.4
  • 54
    • 0037072661 scopus 로고    scopus 로고
    • Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi
    • Volpe, T. A., C. Kidner, I. M. Hall, G. Teng, S. I. Grewal, and R. A. Martienssen. 2002. Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi. Science 297:1833-1837.
    • (2002) Science , vol.297 , pp. 1833-1837
    • Volpe, T.A.1    Kidner, C.2    Hall, I.M.3    Teng, G.4    Grewal, S.I.5    Martienssen, R.A.6
  • 55
    • 0141992115 scopus 로고    scopus 로고
    • mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression
    • Wang, H., W. An, R. Cao, L. Xia, H. Erdjument-Bromage, B. Chatton, P. Tempst, R. G. Roeder, and Y. Zhang. 2003. mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol. Cell 12:475-487.
    • (2003) Mol. Cell , vol.12 , pp. 475-487
    • Wang, H.1    An, W.2    Cao, R.3    Xia, L.4    Erdjument-Bromage, H.5    Chatton, B.6    Tempst, P.7    Roeder, R.G.8    Zhang, Y.9
  • 56
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • Wang, H., R. Cao, L. Xia, H. Erdjument-Bromage, C. Borchers, P. Tempst, and Y. Zhang. 2001. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 8:1207-1217.
    • (2001) Mol. Cell , vol.8 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 57
    • 0032518799 scopus 로고    scopus 로고
    • Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase
    • Wong, J., D. Patterton, A. Imhof, D. Guschin, Y. B. Shi, and A. P. Wolffe. 1998. Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. EMBO J. 17:520-534.
    • (1998) EMBO J. , vol.17 , pp. 520-534
    • Wong, J.1    Patterton, D.2    Imhof, A.3    Guschin, D.4    Shi, Y.B.5    Wolffe, A.P.6
  • 58
    • 0028860925 scopus 로고
    • A role for nucleosome assembly in both silencing and activation of the Xenopus TR beta A gene by the thyroid hormone receptor
    • Wong, J., Y. B. Shi, and A. P. Wolffe. 1995. A role for nucleosome assembly in both silencing and activation of the Xenopus TR beta A gene by the thyroid hormone receptor. Genes Dev. 9:2696-2711.
    • (1995) Genes Dev. , vol.9 , pp. 2696-2711
    • Wong, J.1    Shi, Y.B.2    Wolffe, A.P.3
  • 59
    • 0024320630 scopus 로고
    • The genetics of position-effect variegation modifying loci in Drosophila melanogaster
    • Wustmann, G., J. Szidonya, H. Taubert, and G. Reuter. 1989. The genetics of position-effect variegation modifying loci in Drosophila melanogaster. Mol. Gen. Genet. 217:520-527.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 520-527
    • Wustmann, G.1    Szidonya, J.2    Taubert, H.3    Reuter, G.4
  • 61
    • 0037423688 scopus 로고    scopus 로고
    • Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1
    • Yamamoto, K., and M. Sonoda. 2003. Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1. Biochem. Biophys. Res. Commun. 301:287-292.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 287-292
    • Yamamoto, K.1    Sonoda, M.2
  • 62
    • 0037012042 scopus 로고    scopus 로고
    • Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor
    • Yang, L., L. Xia, D. Y. Wu, H. Wang, H. A. Chansky, W. H. Schubach, D. D. Hickstein, and Y. Zhang. 2002. Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor. Oncogene 21:148-152.
    • (2002) Oncogene , vol.21 , pp. 148-152
    • Yang, L.1    Xia, L.2    Wu, D.Y.3    Wang, H.4    Chansky, H.A.5    Schubach, W.H.6    Hickstein, D.D.7    Zhang, Y.8
  • 63
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X. J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 64
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
    • Zegerman, P., B. Canas, D. Pappin, and T. Kouzarides. 2002. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J. Biol. Chem. 277:11621-11624.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.