메뉴 건너뛰기




Volumn 14, Issue 2, 2004, Pages 183-193

Different Ezh2-containing complexes target methylation of histone H1 or nucleosomal histone H3

Author keywords

[No Author keywords available]

Indexed keywords

EMBRYONIC ECTODERM DEVELOPMENT PROTEIN; ENZYME; HISTONE H1; HISTONE H3; HISTONE LYSINE METHYLTRANSFERASE; HUMAN ENHANCER OF ZESTE HOMOLOG; ISOPROTEIN; LYSINE; MESSENGER RNA; METHYLTRANSFERASE; POLYCOMB REPRESSIVE COMPLEX; PROTEIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 1942502862     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00185-6     Document Type: Article
Times cited : (380)

References (37)
  • 1
    • 0034935019 scopus 로고    scopus 로고
    • Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling
    • Bhattacharjee R.N., Banks G.C., Trotter K.W., Lee H.L., Archer T.K. Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling. Mol. Cell. Biol. 21:2001;5417-5425.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5417-5425
    • Bhattacharjee, R.N.1    Banks, G.C.2    Trotter, K.W.3    Lee, H.L.4    Archer, T.K.5
  • 2
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury E.M. Reversible histone modifications and the chromosome cell cycle. Bioessays. 14:1992;9-16.
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 4
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • 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.
    • (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
  • 5
    • 0030855478 scopus 로고    scopus 로고
    • The product of the murine homolog of the Drosophila extra sex combs gene displays transcriptional repressor activity
    • Denisenko O.N., Bomsztyk K. The product of the murine homolog of the Drosophila extra sex combs gene displays transcriptional repressor activity. Mol. Cell. Biol. 17:1997;4707-4717.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4707-4717
    • Denisenko, O.N.1    Bomsztyk, K.2
  • 6
    • 0024977387 scopus 로고
    • The ultrastructure of upstream and downstream regions of an active Balbiani ring gene
    • Ericsson C., Mehlin H., Bjorkroth B., Lamb M.M., Daneholt B. The ultrastructure of upstream and downstream regions of an active Balbiani ring gene. Cell. 56:1989;631-639.
    • (1989) Cell , vol.56 , pp. 631-639
    • Ericsson, C.1    Mehlin, H.2    Bjorkroth, B.3    Lamb, M.M.4    Daneholt, B.5
  • 7
  • 8
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • a
    • Fischle W., Wang Y., Allis C.D. Binary switches and modification cassettes in histone biology and beyond. Nature. 425:2003;475-479. a.
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 9
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains
    • b
    • 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. b.
    • (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
  • 10
    • 0032537558 scopus 로고    scopus 로고
    • Asymmetric linker histone association directs the asymmetric rearrangement of core histone interactions in a positioned nucleosome containing a thyroid hormone response element
    • Guschin D., Chandler S., Wolffe A.P. Asymmetric linker histone association directs the asymmetric rearrangement of core histone interactions in a positioned nucleosome containing a thyroid hormone response element. Biochemistry. 37:1998;8629-8636.
    • (1998) Biochemistry , vol.37 , pp. 8629-8636
    • Guschin, D.1    Chandler, S.2    Wolffe, A.P.3
  • 11
    • 0035861875 scopus 로고    scopus 로고
    • Methylation of histone H3 at Lys-9 is an early mark on the X chromosome during X inactivation
    • Heard E., Rougeulle C., Arnaud D., Avner P., Allis C.D., Spector D.L. Methylation of histone H3 at Lys-9 is an early mark on the X chromosome during X inactivation. Cell. 107:2001;727-738.
    • (2001) Cell , vol.107 , pp. 727-738
    • Heard, E.1    Rougeulle, C.2    Arnaud, D.3    Avner, P.4    Allis, C.D.5    Spector, D.L.6
  • 12
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science. 293:2001;1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 13
    • 0035854055 scopus 로고    scopus 로고
    • Histone H1 diversity: Bridging regulatory signals to linker histone function
    • Khochbin S. Histone H1 diversity. bridging regulatory signals to linker histone function Gene. 271:2001;1-12.
    • (2001) Gene , vol.271 , pp. 1-12
    • Khochbin, S.1
  • 14
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • a
    • 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.
    • (2002) Genes Dev. , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 15
    • 0036143859 scopus 로고    scopus 로고
    • Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)
    • b
    • Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D. Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1). Mol. Cell. Biol. 22:2002;835-848. b.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 835-848
    • Kuzmichev, A.1    Zhang, Y.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 16
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner M., Jenuwein T. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14:2002;286-298.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 17
    • 0032473501 scopus 로고    scopus 로고
    • Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter
    • Lee H.L., Archer T.K. Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter. EMBO J. 17:1998;1454-1466.
    • (1998) EMBO J. , vol.17 , pp. 1454-1466
    • Lee, H.L.1    Archer, T.K.2
  • 18
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 a resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature. 389:1997;251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 19
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • Luger K., Rechsteiner T.J., Richmond T.J. Preparation of nucleosome core particle from recombinant histones. Methods Enzymol. 304:1999;3-19.
    • (1999) Methods Enzymol. , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 20
    • 0037172659 scopus 로고    scopus 로고
    • Mitotically stable association of polycomb group proteins eed and enx1 with the inactive x chromosome in trophoblast stem cells
    • Mak W., Baxter J., Silva J., Newall A.E., Otte A.P., Brockdorff N. Mitotically stable association of polycomb group proteins eed and enx1 with the inactive x chromosome in trophoblast stem cells. Curr. Biol. 12:2002;1016-1020.
    • (2002) Curr. Biol. , vol.12 , pp. 1016-1020
    • Mak, W.1    Baxter, J.2    Silva, J.3    Newall, A.E.4    Otte, A.P.5    Brockdorff, N.6
  • 21
    • 0041624288 scopus 로고    scopus 로고
    • Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
    • 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.
    • (2003) Genes Dev. , vol.17 , pp. 1823-1828
    • Min, J.1    Zhang, Y.2    Xu, R.M.3
  • 23
    • 0033999219 scopus 로고    scopus 로고
    • A Drosophila ESC-E(Z) protein complex is distinct from other polycomb group complexes and contains covalently modified ESC
    • Ng J., Hart C.M., Morgan K., Simon J.A. A Drosophila ESC-E(Z) protein complex is distinct from other polycomb group complexes and contains covalently modified ESC. Mol. Cell. Biol. 20:2000;3069-3078.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3069-3078
    • Ng, J.1    Hart, C.M.2    Morgan, K.3    Simon, J.A.4
  • 24
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 16:2002;1518-1527.
    • (2002) Genes Dev. , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 25
    • 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., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D., Tempst P., Reinberg D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16:2002;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
  • 26
    • 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
  • 28
    • 0027538330 scopus 로고
    • Related chromosome binding sites for zeste, suppressors of zeste and Polycomb group proteins in Drosophila and their dependence on Enhancer of zeste function
    • Rastelli L., Chan C.S., Pirrotta V. Related chromosome binding sites for zeste, suppressors of zeste and Polycomb group proteins in Drosophila and their dependence on Enhancer of zeste function. EMBO J. 12:1993;1513-1522.
    • (1993) EMBO J. , vol.12 , pp. 1513-1522
    • Rastelli, L.1    Chan, C.S.2    Pirrotta, V.3
  • 30
    • 0032538433 scopus 로고    scopus 로고
    • The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins
    • Rietzler M., Bittner M., Kolanus W., Schuster A., Holzmann B. The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins. J. Biol. Chem. 273:1998;27459-27466.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27459-27466
    • Rietzler, M.1    Bittner, M.2    Kolanus, W.3    Schuster, A.4    Holzmann, B.5
  • 31
    • 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
    • Sewalt R.G., van der Vlag J., Gunster M.J., Hamer K.M., den Blaauwen J.L., Satijn D.P., Hendrix T., van Driel R., Otte A.P. 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    Hendrix, T.7    Van Driel, R.8    Otte, A.P.9
  • 33
    • 0003903126 scopus 로고
    • New York: Springer-Verlag
    • van Holde K. Chromatin. 1988;Springer-Verlag, New York.
    • (1988) Chromatin
    • Van Holde, K.1
  • 34
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F., Gafken P.R., Gottschling D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell. 109:2002;745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 35
    • 0033926403 scopus 로고    scopus 로고
    • Review: Chromatin structural features and targets that regulate transcription
    • Wolffe A.P., Guschin D. Review. chromatin structural features and targets that regulate transcription J. Struct. Biol. 129:2000;102-122.
    • (2000) J. Struct. Biol. , vol.129 , pp. 102-122
    • Wolffe, A.P.1    Guschin, D.2
  • 36
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang Y., Reinberg D. Transcription regulation by histone methylation. interplay between different covalent modifications of the core histone tails Genes Dev. 15:2001;2343-2360.
    • (2001) Genes Dev. , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 37
    • 0032563864 scopus 로고    scopus 로고
    • Position and orientation of the globular domain of linker histone H5 on the nucleosome
    • Zhou Y.B., Gerchman S.E., Ramakrishnan V., Travers A., Muyldermans S. Position and orientation of the globular domain of linker histone H5 on the nucleosome. Nature. 395:1998;402-405.
    • (1998) Nature , vol.395 , pp. 402-405
    • Zhou, Y.B.1    Gerchman, S.E.2    Ramakrishnan, V.3    Travers, A.4    Muyldermans, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.