메뉴 건너뛰기




Volumn 22, Issue 1, 1999, Pages 98-101

Acetylated histones are associated with FMR1 in normal but not fragile X-syndrome cells

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE;

EID: 0032905253     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/8807     Document Type: Article
Times cited : (280)

References (30)
  • 2
    • 0025905795 scopus 로고
    • Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting a length variation in fragile X syndrome
    • Verkerk, A.J. et al. Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting a length variation in fragile X syndrome. Cell 65, 905-914 (1991).
    • (1991) Cell , vol.65 , pp. 905-914
    • Verkerk, A.J.1
  • 3
    • 0025952727 scopus 로고
    • Direct diagnosis of fragile X syndrome of mental retardation
    • Rousseau, F. et al. Direct diagnosis of fragile X syndrome of mental retardation. N. Engl. J. Med. 325, 1673-1681 (1991).
    • (1991) N. Engl. J. Med. , vol.325 , pp. 1673-1681
    • Rousseau, F.1
  • 4
    • 0026347628 scopus 로고
    • Fragile X genotype characterized by an unstable repeat region of DNA
    • Yu, S. et al. Fragile X genotype characterized by an unstable repeat region of DNA. Science 252, 1179-1181 (1991).
    • (1991) Science , vol.252 , pp. 1179-1181
    • Yu, S.1
  • 5
    • 0026922707 scopus 로고
    • DNA methylation represses FMR1 transcription in fragile X syndrome
    • Sutcliffe, J.S. et al. DNA methylation represses FMR1 transcription in fragile X syndrome. Hum. Mol. Genet. 1, 397-400 (1992).
    • (1992) Hum. Mol. Genet. , vol.1 , pp. 397-400
    • Sutcliffe, J.S.1
  • 6
    • 0025833298 scopus 로고
    • Absence of expression of the FMR1 gene in fragile X syndrome
    • Pieretti, M. et al. Absence of expression of the FMR1 gene in fragile X syndrome. Cell 66, 817-822 (1991).
    • (1991) Cell , vol.66 , pp. 817-822
    • Pieretti, M.1
  • 7
    • 0019318994 scopus 로고
    • DNA methylation and gene function
    • Razin, A. & Riggs, A.D. DNA methylation and gene function. Science 210, 604-610 (1980).
    • (1980) Science , vol.210 , pp. 604-610
    • Razin, A.1    Riggs, A.D.2
  • 8
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V.G., Faulkner, R. & Mirsky, A.E. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl Acad. Sci. USA 51, 786-794 (1964).
    • (1964) Proc. Natl Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 9
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner, B.M. Decoding the nucleosome. Cell 75, 5-8 (1993).
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 10
    • 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
  • 11
    • 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
  • 12
    • 0032168678 scopus 로고    scopus 로고
    • CpG methylation, chromatin structure and gene silencing - A three way connection
    • Razin, A. CpG methylation, chromatin structure and gene silencing - a three way connection. EMBO J. 17, 4905-4908 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4905-4908
    • Razin, A.1
  • 13
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nucleosome acetylation
    • Braunstein, M., Rose, A.B., Holmes, S.G., Allis, C.D. & Broach, J.R. Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev. 7, 592-604 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 592-604
    • Braunstein, M.1    Rose, A.B.2    Holmes, S.G.3    Allis, C.D.4    Broach, J.R.5
  • 14
    • 0025790419 scopus 로고
    • Sequence of human glucose-6-phosphate dehydrogenase cloned in plasmids and a yeast artificial chromosome
    • Chen, E.Y. et al. Sequence of human glucose-6-phosphate dehydrogenase cloned in plasmids and a yeast artificial chromosome. Genomics 10, 792-780 (1991).
    • (1991) Genomics , vol.10 , pp. 792-1780
    • Chen, E.Y.1
  • 15
    • 0026706866 scopus 로고
    • Hemimethylation and hypersensitivity are early events in transcriptional reactivation of human inactive X-linked genes in a hamster X human somatic cell hybrid
    • Sasaki, T., Hansen, R.S. & Gartler, S.M. Hemimethylation and hypersensitivity are early events in transcriptional reactivation of human inactive X-linked genes in a hamster X human somatic cell hybrid. Mol. Cell. Biol. 12, 3819-3826 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3819-3826
    • Sasaki, T.1    Hansen, R.S.2    Gartler, S.M.3
  • 16
    • 0032403946 scopus 로고    scopus 로고
    • Repression of the mouse M-lysozyme gene involves both hindrance of enhancer factor binding to the methylated enhancer and histone deacetylation
    • Ammerpohl, O., Schmitz, A., Steinmuller, L. & Renkawitz, R. Repression of the mouse M-lysozyme gene involves both hindrance of enhancer factor binding to the methylated enhancer and histone deacetylation. Nucleic. Acids Res. 26, 5256-5260 (1998).
    • (1998) Nucleic. Acids Res. , vol.26 , pp. 5256-5260
    • Ammerpohl, O.1    Schmitz, A.2    Steinmuller, L.3    Renkawitz, R.4
  • 18
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • Van Lint, C., Emiliani, S. & Verdin, E. The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr. 5, 245-253 (1996).
    • (1996) Gene Expr. , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 19
    • 0029092238 scopus 로고
    • Stimulation of tissue-type plasminogen activator gene expression by sodium butyrate and trichostatin A in human endothelial cells involves histone acetylation
    • Arts, J., Lansink, M., Grimbergen, J., Toet, K.H. & Kooistra, T. Stimulation of tissue-type plasminogen activator gene expression by sodium butyrate and trichostatin A in human endothelial cells involves histone acetylation. Biochem. J. 310, 171-176 (1995).
    • (1995) Biochem. J. , vol.310 , pp. 171-176
    • Arts, J.1    Lansink, M.2    Grimbergen, J.3    Toet, K.H.4    Kooistra, T.5
  • 20
    • 0029919356 scopus 로고    scopus 로고
    • Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation
    • Van Lint, C., Emiliani, S., Ott, M. & Verdin E. Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation. EMBO J. 15, 1112-1120 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1112-1120
    • Van Lint, C.1    Emiliani, S.2    Ott, M.3    Verdin, E.4
  • 21
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • Rundlett, S.E. et al. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc. Natl Acad. Sci. USA 93, 14503-14058 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14503-114058
    • Rundlett, S.E.1
  • 22
    • 0030440796 scopus 로고    scopus 로고
    • Nuclease sensitivity of permeabilized cells confirms altered chromatin conformation at the fragile X locus
    • Eberhart, D.E. & Warren, S.T. Nuclease sensitivity of permeabilized cells confirms altered chromatin conformation at the fragile X locus. Somat. Cell Mol. Genet. 22, 435-441 (1996).
    • (1996) Somat. Cell Mol. Genet. , vol.22 , pp. 435-441
    • Eberhart, D.E.1    Warren, S.T.2
  • 23
    • 0030668366 scopus 로고    scopus 로고
    • Structural and functional characterization of the human FMR1 promoter reveals similarities with the hnRNP-A2 promoter region
    • Drouin, R. et al. Structural and functional characterization of the human FMR1 promoter reveals similarities with the hnRNP-A2 promoter region. Hum. Mol. Genet. 6, 2051-2060 (1997)
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 2051-2060
    • Drouin, R.1
  • 24
    • 16944362592 scopus 로고    scopus 로고
    • Characterization of FMR1 promoter elements by in vivo-footprinting analysis
    • Schwemmle, S. et. al. Characterization of FMR1 promoter elements by in vivo-footprinting analysis. Am. J. Hum. Genet. 60, 1354-1362 (1997).
    • (1997) Am. J. Hum. Genet. , vol.60 , pp. 1354-1362
    • Schwemmle, S.1
  • 25
    • 0031792775 scopus 로고    scopus 로고
    • The immunoglobulin heavy chain locus control region increases histone acetylation along linked c-myc genes
    • Madisen, L., Krumm, A., Hebbes, T. S Groudine, M. The immunoglobulin heavy chain locus control region increases histone acetylation along linked c-myc genes. Mol. Cell. Biol. 18, 6281-6292 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6281-6292
    • Madisen, L.1    Krumm, A.2    Hebbes, T.S.3    Groudine, M.4
  • 26
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo, R., Postigo, A. & Dean, D. Rb interacts with histone deacetylase to repress transcription. Cell 92, 463-473 (1998).
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.1    Postigo, A.2    Dean, D.3
  • 27
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron, E. et al. 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.1
  • 28
    • 0028989063 scopus 로고
    • Translational suppression by trinucleotide repeat expansion at FMR1
    • Feng, Y. et al. Translational suppression by trinucleotide repeat expansion at FMR1. Science 268, 731-734 (1995).
    • (1995) Science , vol.268 , pp. 731-734
    • Feng, Y.1
  • 29
    • 0024544492 scopus 로고
    • Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
    • Lin, R., Leone, J., Cook, R. & Allis, C.D. Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena. J. Cell. Biol. 108, 1577-1588 (1989).
    • (1989) J. Cell. Biol. , vol.108 , pp. 1577-1588
    • Lin, R.1    Leone, J.2    Cook, R.3    Allis, C.D.4
  • 30
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • Hendzel, M. et al. Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106, 348-360 (1997).
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.