메뉴 건너뛰기




Volumn 19, Issue 7, 2005, Pages 815-826

Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9

Author keywords

G9a; GLP; Histone; Methylation

Indexed keywords

HISTONE H3; HISTONE METHYLTRANSFERASE G9A; METHYLTRANSFERASE; PROTEIN GLP; UNCLASSIFIED DRUG;

EID: 20144388930     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1284005     Document Type: Article
Times cited : (672)

References (40)
  • 1
    • 0033118322 scopus 로고    scopus 로고
    • Functional mammalian homologs of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
    • Aagaard, L., Laible, G., Selenko, P., Schmid, M., Dorn, R., Schotta, G., Kuhfittig, S., Wolf, A., Lebersorger, A., Singh, P.E., et al. 1999. Functional mammalian homologs 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.E.10
  • 3
    • 1942503942 scopus 로고    scopus 로고
    • The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3
    • Cao, R. and Zhang, Y. 2004a. The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3. Curr. Opin. Genet. Dev. 14: 155-164.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 155-164
    • Cao, R.1    Zhang, Y.2
  • 4
    • 3042801308 scopus 로고    scopus 로고
    • SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex
    • -. 2004b. SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol. Cell 15: 57-67.
    • (2004) Mol. Cell , vol.15 , pp. 57-67
  • 6
    • 1542314243 scopus 로고    scopus 로고
    • Histone H3-K9 methyltransferase ESET is essential for early development
    • Dodge, J.E., Kang, Y.K., Beppu, H., Lei, H., and Li, E. 2004. Histone H3-K9 methyltransferase ESET is essential for early development. Mol. Cell. Biol. 24: 2478-2486.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2478-2486
    • Dodge, J.E.1    Kang, Y.K.2    Beppu, H.3    Lei, H.4    Li, E.5
  • 7
    • 0034026194 scopus 로고    scopus 로고
    • The HP1 protein family: Getting a grip on chromatin
    • Eissenberg, J.C. and Elgin, S.C. 2000. The HP1 protein family: Getting a grip on chromatin. Curr. Opin. Genet. Dev. 10: 204-210.
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 204-210
    • Eissenberg, J.C.1    Elgin, S.C.2
  • 8
    • 1642369447 scopus 로고    scopus 로고
    • The N-terminus of Drosophila SU(VAR)3-9 mediates dimerization and regulates its methyltransferase activity
    • Eskeland, R., Czermin, B., Boeke, J., Bonaldi, T., Regula, J.T., and Imhof, A. 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
  • 11
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysinc marks in histone H3 by Polycomb and HP1 chromodomains
    • Fischle, W., Wang, Y., Jacobs, S.A., Kim, Y., Allis, C.D., and Khorasanizadeh, S. 2003. Molecular basis for the discrimination of repressive methyl-lysinc marks in histone H3 by Polycomb and HP1 chromodomains. Genes & Dev. 17: 1870-1881.
    • (2003) Genes & Dev. , vol.17 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 12
    • 1542347557 scopus 로고    scopus 로고
    • PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing
    • Gyory, L, Wu, J., Fejer, G., Seto, E., and Wright, K.L. 2004. PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing. Nat. Immunol. 5: 299-308.
    • (2004) Nat. Immunol. , vol.5 , pp. 299-308
    • Gyory, L.1    Wu, J.2    Fejer, G.3    Seto, E.4    Wright, K.L.5
  • 13
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. and Allis, C.D. 2001. Translating the histone code. Science 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 14
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M. and Jenuwein, T. 2002. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14: 286-298.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 15
    • 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., and Jenuwein, T. 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
  • 16
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner, M., O'Sullivan, R.J., and Jenuwein, T. 2003. An epigenetic road map for histone lysine methylation. J. Cell Sci. 116: 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., and Richmond, T.J. 1997. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389: 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
    • 3843147151 scopus 로고    scopus 로고
    • CCAAT displacement protein/cut homolog recruits G9a histone lysine methyltransferase to repress transcription
    • Nishio, H. and Walsh, M.J. 2004. CCAAT displacement protein/cut homolog recruits G9a histone lysine methyltransferase to repress transcription. Proc. Natl. Acad. Sci. 101: 11257-11262.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 11257-11262
    • Nishio, H.1    Walsh, M.J.2
  • 22
    • 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., and Nakatani, Y. 2002. A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. Science 296: 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
  • 28
    • 2942631126 scopus 로고    scopus 로고
    • Localized domains of g9a-mediated histone methylation are required for silencing of neuronal genes
    • Roopra, A., Qazi, R., Schoenike, B., Daley, T.J., and Morrison, J.F. 2004. Localized domains of g9a-mediated histone methylation are required for silencing of neuronal genes. Mol. Cell 14: 727-738.
    • (2004) Mol. Cell , vol.14 , pp. 727-738
    • Roopra, A.1    Qazi, R.2    Schoenike, B.3    Daley, T.J.4    Morrison, J.F.5
  • 29
    • 4344685735 scopus 로고    scopus 로고
    • Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly
    • Sarraf, S.A. and Stancheva, I. 2004. Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly. Mol. Cell 15: 595-605.
    • (2004) Mol. Cell , vol.15 , pp. 595-605
    • Sarraf, S.A.1    Stancheva, I.2
  • 31
    • 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., Ayyanathan, K., Negorev, D., Maul, G.G., and Rauscher III, F.J. 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
  • 33
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D. and Allis, C.D. 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
  • 34
    • 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., and Shinkai, Y. 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
  • 35
    • 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., et al. 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
  • 37
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner, B.M. 2000. Histone acetylation and an epigenetic code. Bioessays 22: 836-845.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 38
    • 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., An, W., Cao, R., Xia, L., Erdjument-Bromage, H., Chatton, B., Tempst, P., Roeder, R.G., and Zhang, Y. 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
  • 40
    • 0037012042 scopus 로고    scopus 로고
    • Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor
    • Yang, L., Xia, L., Wu, D.Y., Wang, H., Chansky, H.A., Schubach, W.H., Hiekstein, D.D., and Zhang, Y. 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    Hiekstein, D.D.7    Zhang, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.