메뉴 건너뛰기




Volumn 12, Issue 6, 2003, Pages 1577-1589

Partitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ANTIBODY; HISTONE H3; LYSINE; METHYLTRANSFERASE;

EID: 9144268924     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00477-5     Document Type: Article
Times cited : (939)

References (51)
  • 2
    • 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
  • 3
    • 0015919688 scopus 로고
    • Histone 3. 3. Sequence studies on the cyanogen bromide peptides; Complete amino acid sequence of calf thymus histone 3
    • DeLange R.J., Hooper J.A., Smith E.L. Histone 3. 3. Sequence studies on the cyanogen bromide peptides; complete amino acid sequence of calf thymus histone 3. J. Biol. Chem. 248:1973;3261-3274.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3261-3274
    • Delange, R.J.1    Hooper, J.A.2    Smith, E.L.3
  • 6
    • 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
  • 7
    • 0141929385 scopus 로고    scopus 로고
    • Extending the histone code: Modification cassettes and switches
    • c
    • Fischle W., Wang Y., Allis C.D. Extending the histone code. modification cassettes and switches Nature. 425:2003;475-479. c.
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 9
    • 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
  • 11
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides T. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12:2002;198-209.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 12
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • 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.
    • (2002) Genes Dev. , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 13
    • 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
  • 14
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature. 410:2001;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
  • 15
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner M., O'Sullivan R.J., Jenuwein T. An epigenetic road map for histone lysine methylation. J. Cell Sci. 116:2003;2117-2124.
    • (2003) J. Cell Sci. , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'sullivan, R.J.2    Jenuwein, T.3
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0036208002 scopus 로고    scopus 로고
    • Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes
    • Martens J.H., Verlaan M., Kalkhoven E., Dorsman J.C., Zantema A. Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes. Mol. Cell. Biol. 22:2002;2598-2608.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2598-2608
    • Martens, J.H.1    Verlaan, M.2    Kalkhoven, E.3    Dorsman, J.C.4    Zantema, A.5
  • 21
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence
    • Narita M., Nunez S., Heard E., Lin A.W., Hearn S.A., Spector D.L., Hannon G.J., Lowe S.W. Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. Cell. 113:2003;703-716.
    • (2003) Cell , vol.113 , pp. 703-716
    • Narita, M.1    Nunez, S.2    Heard, E.3    Lin, A.W.4    Hearn, S.A.5    Spector, D.L.6    Hannon, G.J.7    Lowe, S.W.8
  • 22
    • 0037371661 scopus 로고    scopus 로고
    • Balance between acetylation and methylation of histone H3 lysine 9 on the E2F-responsive dihydrofolate reductase promoter
    • Nicolas E., Roumillac C., Trouche D. Balance between acetylation and methylation of histone H3 lysine 9 on the E2F-responsive dihydrofolate reductase promoter. Mol. Cell. Biol. 23:2003;1614-1622.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1614-1622
    • Nicolas, E.1    Roumillac, C.2    Trouche, D.3
  • 25
    • 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
  • 26
    • 0015215623 scopus 로고
    • Protein methylation
    • Paik W.K., Kim S. Protein methylation. Science. 174:1971;114-119.
    • (1971) Science , vol.174 , pp. 114-119
    • Paik, W.K.1    Kim, S.2
  • 31
    • 0035370439 scopus 로고    scopus 로고
    • Histone methylation versus histone acetylation: New insights into epigenetic regulation
    • Rice J.C., Allis C.D. Histone methylation versus histone acetylation. new insights into epigenetic regulation Curr. Opin. Cell Biol. 13:2001;263-273.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 263-273
    • Rice, J.C.1    Allis, C.D.2
  • 32
    • 0347955358 scopus 로고    scopus 로고
    • Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains
    • , this issue
    • Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J., Hunt D.F., Shinkai Y., Allis C.D. Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains. Mol. Cell. 12:2003;1591-1598. , this issue.
    • (2003) Mol. Cell , vol.12 , pp. 1591-1598
    • Rice, J.C.1    Briggs, S.D.2    Ueberheide, B.3    Barber, C.M.4    Shabanowitz, J.5    Hunt, D.F.6    Shinkai, Y.7    Allis, C.D.8
  • 35
    • 1042265479 scopus 로고    scopus 로고
    • Tips in analyzing antibodies directed against specific histone tail modifications
    • Sarma K., Nishioka K., Reinberg D. Tips in analyzing antibodies directed against specific histone tail modifications. Methods Enzymol. in press:2003.
    • (2003) Methods Enzymol.
    • Sarma, K.1    Nishioka, K.2    Reinberg, D.3
  • 36
    • 85030933337 scopus 로고    scopus 로고
    • Schotta, G., Lachner, M., Peters, A.H.F.M., and Jenuwein, T. (2003). The indexing potential of histone lysine methylation. Reversible Acetylation of Histone and Non-Histone Proteins, Novartis Symposium, in press.
    • Schotta, G., Lachner, M., Peters, A.H.F.M., and Jenuwein, T. (2003). The indexing potential of histone lysine methylation. Reversible Acetylation of Histone and Non-Histone Proteins, Novartis Symposium, in press.
  • 37
    • 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
  • 38
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:1996;850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 40
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature. 403:2000;41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 41
    • 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
  • 42
    • 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
  • 44
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner B.M. Histone acetylation and an epigenetic code. Bioessays. 22:2000;836-845.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 45
    • 85030921833 scopus 로고    scopus 로고
    • van Holde, K.E. (1988). Chromatin (New York: Springer Verlag).
    • van Holde, K.E. (1988). Chromatin (New York: Springer Verlag).
  • 48
    • 0038003140 scopus 로고    scopus 로고
    • Role of histone methyltransferase G9a in CpG methylation of the Prader-Willi syndrome imprinting center
    • Xin Z., Tachibana M., Guggiari M., Heard E., Shinkai Y., Wagstaff J. Role of histone methyltransferase G9a in CpG methylation of the Prader-Willi syndrome imprinting center. J. Biol. Chem. 278:2003;14996-15000.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14996-15000
    • Xin, Z.1    Tachibana, M.2    Guggiari, M.3    Heard, E.4    Shinkai, Y.5    Wagstaff, J.6
  • 49
    • 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
  • 50
    • 0037099664 scopus 로고    scopus 로고
    • Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization- postsource decay, and nanoelectrospray ionization tandem mass spectrometry
    • Zhang K., Tang H., Huang L., Blankenship J.W., Jones P.R., Xiang F., Yau P.M., Burlingame A.L. Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization-postsource decay, and nanoelectrospray ionization tandem mass spectrometry. Anal. Biochem. 306:2002;259-269.
    • (2002) Anal. Biochem. , vol.306 , pp. 259-269
    • Zhang, K.1    Tang, H.2    Huang, L.3    Blankenship, J.W.4    Jones, P.R.5    Xiang, F.6    Yau, P.M.7    Burlingame, A.L.8
  • 51
    • 0042164227 scopus 로고    scopus 로고
    • Structural basis for the product specificity of histone lysine methyltransferases
    • Zhang X., Yang Z., Khan S.I., Horton J.R., Tamaru H., Selker E.U., Cheng X. Structural basis for the product specificity of histone lysine methyltransferases. Mol. Cell. 12:2003;177-185.
    • (2003) Mol. Cell , vol.12 , pp. 177-185
    • Zhang, X.1    Yang, Z.2    Khan, S.I.3    Horton, J.R.4    Tamaru, H.5    Selker, E.U.6    Cheng, X.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.