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Volumn 24, Issue 1, 2000, Pages 88-91

DNA methyltransferase Dnmt1 associates with histone deacetylase activity

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA METHYLTRANSFERASE; HISTONE DEACETYLASE;

EID: 0033988813     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/71750     Document Type: Article
Times cited : (852)

References (29)
  • 1
    • 0026708177 scopus 로고
    • Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
    • Li, E., Bestor, T.H. & Jaenisch, R. Targeted mutation of the DNA methyltransferase gene results in embryonic lethality. Cell 69, 915-926 (1992).
    • (1992) Cell , vol.69 , pp. 915-926
    • Li, E.1    Bestor, T.H.2    Jaenisch, R.3
  • 2
    • 0027535235 scopus 로고
    • Effects of DNA methylation on DNA-binding proteins and gene expression
    • Tate, P.H. & Bird, A.P. Effects of DNA methylation on DNA-binding proteins and gene expression. Curr. Opin. Genet. Dev. 3, 226-231 (1993).
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 226-231
    • Tate, P.H.1    Bird, A.P.2
  • 3
    • 0033119780 scopus 로고    scopus 로고
    • DNA methylation and chromatin modification
    • Ng, H.-H. & Bird, A. DNA methylation and chromatin modification. Curr. Opin. Genet. Dev. 9, 158-163 (1999).
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 158-163
    • Ng, H.-H.1    Bird, A.2
  • 4
    • 0032992224 scopus 로고    scopus 로고
    • DNA methylation represses transcription in vivo
    • Siegfried, Z. et al. DNA methylation represses transcription in vivo. Nature Genet. 22, 203-206 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 203-206
    • Siegfried, Z.1
  • 5
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan, X. et al. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393, 386-389 (1998).
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1
  • 6
    • 0031837109 scopus 로고    scopus 로고
    • Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription
    • Jones, P.L. et al. Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription. Nature Genet. 19, 187-191 (1998).
    • (1998) Nature Genet. , vol.19 , pp. 187-191
    • Jones, P.L.1
  • 7
    • 0027225233 scopus 로고
    • Analysis of the murine All-1 gene reveals conserved domains with human ALL-1 and identifies a motif shared with DNA methyltransferases
    • Ma, Q. et al. Analysis of the murine All-1 gene reveals conserved domains with human ALL-1 and identifies a motif shared with DNA methyltransferases. Proc. Natl Acad. Sci. USA 90, 6350-6354 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6350-6354
    • Ma, Q.1
  • 8
    • 0030977310 scopus 로고    scopus 로고
    • A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins
    • Cross, S.H., Meehan, R.R., Nan, X. & Bird, A. A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins Nature Genet. 16, 256-259 (1997).
    • (1997) Nature Genet. , vol.16 , pp. 256-259
    • Cross, S.H.1    Meehan, R.R.2    Nan, X.3    Bird, A.4
  • 9
    • 0029616201 scopus 로고
    • Domains with transcriptional regulatory activity within the ALL1 and AF4 proteins involved in acute leukemia
    • Prasad, R. et al. Domains with transcriptional regulatory activity within the ALL1 and AF4 proteins involved in acute leukemia. Proc. Natl Acad. Sci. USA 92, 12160-12164 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12160-12164
    • Prasad, R.1
  • 10
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl, K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 12, 599-606 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 599-606
    • Struhl, K.1
  • 11
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides, T. Histone acetylases and deacetylases in cell proliferation. Curr. Opin. Genet. Dev. 9, 40-48 (1999).
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 12
    • 0029294663 scopus 로고
    • Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
    • Yoshida, M., Horinouchi, S. & Beppu, T. Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays 17, 423-430 (1995).
    • (1995) Bioessays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 13
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor
    • Miska, E.A. et al. HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 18, 5099-5107 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5099-5107
    • Miska, E.A.1
  • 14
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • Brehm, A. et al. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 391, 597-601 (1998).
    • (1998) Nature , vol.391 , pp. 597-601
    • Brehm, A.1
  • 15
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo, R.X., Postigo, A.A. & Dean, D.C. Rb interacts with histone deacetylase to repress transcription. Cell 32, 463-473 (1998).
    • (1998) Cell , vol.32 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 16
    • 0032484904 scopus 로고    scopus 로고
    • Retinoblastoma protein represses transcription by recruiting a histone deacetytase
    • Magnaghi-Jaulin, L. et al. Retinoblastoma protein represses transcription by recruiting a histone deacetytase. Nature 391, 601-605 (1998).
    • (1998) Nature , vol.391 , pp. 601-605
    • Magnaghi-Jaulin, L.1
  • 18
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron, E.E., Bachman, K.E., Myohanen, S., Herman, J.G. & Baylin, S.B. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nature Genet. 21, 103-107 (1999).
    • (1999) Nature Genet. , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 19
    • 0033180082 scopus 로고    scopus 로고
    • Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
    • Zhang, Y. et al. Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. Genes Dev. 13, 1924-1935 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1924-1935
    • Zhang, Y.1
  • 20
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • Zhang, Y., LeRoy, G., Seelig, H.P., Lane, W.S. & Reinberg, D. The dermatomyositis specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 95, 279-289 (1998).
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 21
    • 0032482974 scopus 로고    scopus 로고
    • Trichostatin A causes selective loss of DNA methylation in Neurospora
    • Selker, E.U. Trichostatin A causes selective loss of DNA methylation in Neurospora. Proc. Natl Acad. Sci. USA 95, 9430-9435 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9430-9435
    • Selker, E.U.1
  • 22
    • 0032907728 scopus 로고    scopus 로고
    • Maintenance of genomic methylation requires a SWI2/SNF2-like protein
    • Jeddeloh, J.A., Stokes, T.L. & Richards, E.J. Maintenance of genomic methylation requires a SWI2/SNF2-like protein Nature Genet. 22, 94-97 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 94-97
    • Jeddeloh, J.A.1    Stokes, T.L.2    Richards, E.J.3
  • 23
    • 0031860739 scopus 로고    scopus 로고
    • Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases
    • Okano, M., Xie, S. & Li, E. Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases. Nature Genet. 19, 219-220 (1998).
    • (1998) Nature Genet. , vol.19 , pp. 219-220
    • Okano, M.1    Xie, S.2    Li, E.3
  • 24
    • 0027520469 scopus 로고
    • The retinoblastoma protein binds E2F residues required for activation in vivo and TBP binding in vitro
    • Hagemeier, C., Cook, A. & Kouzarides, T. The retinoblastoma protein binds E2F residues required for activation in vivo and TBP binding in vitro. Nucleic Acids Res. 21, 4998-5004 (1993).
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4998-5004
    • Hagemeier, C.1    Cook, A.2    Kouzarides, T.3
  • 27
    • 0026752598 scopus 로고
    • The human cytomegalovirus 80-kilodalton but not the 72-kilodalton immediate-early protein transactivates heterologous promoters in a TATA box-dependent mechanism and interacts directly with TFIID
    • Hagemeier, C., Walker, S., Caswell, R., Kouzarides, T. & Sinclair, J. The human cytomegalovirus 80-kilodalton but not the 72-kilodalton immediate-early protein transactivates heterologous promoters in a TATA box-dependent mechanism and interacts directly with TFIID. J. Virol. 66, 4452-4456 (1992).
    • (1992) J. Virol. , vol.66 , pp. 4452-4456
    • Hagemeier, C.1    Walker, S.2    Caswell, R.3    Kouzarides, T.4    Sinclair, J.5
  • 28
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C.A. & Schreiber, S.L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272, 408-411 (1996).
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 29
    • 0031025621 scopus 로고    scopus 로고
    • Inhibition of tumorigenesis by a cytosine-DNA, methyltransferase, antisense oligodeoxynucleotide
    • Ramchandani, S., MacLeod, A.R., Pinard, M., von Hofe, E. & Szyf, M. Inhibition of tumorigenesis by a cytosine-DNA, methyltransferase, antisense oligodeoxynucleotide. Proc. Natl Acad. Sci. USA 94, 684-689 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 684-689
    • Ramchandani, S.1    MacLeod, A.R.2    Pinard, M.3    Von Hofe, E.4    Szyf, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.