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Volumn 10, Issue 2, 2000, Pages 224-228

Dynamics of DNA methylation pattern

Author keywords

[No Author keywords available]

Indexed keywords

METHYLTRANSFERASE;

EID: 0034109336     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(00)00064-2     Document Type: Review
Times cited : (83)

References (35)
  • 1
    • 0019318994 scopus 로고
    • DNA methylation and gene regulation
    • Razin A., Riggs A.D. DNA methylation and gene regulation. Science. 210:1980;604-610.
    • (1980) Science , vol.210 , pp. 604-610
    • Razin, A.1    Riggs, A.D.2
  • 2
    • 0023119242 scopus 로고
    • Temporal and regional changes in DNA methylation in the embryonic, extraembryonic and germ cell lineages during mouse embryo development
    • Monk M., Boubelik M., Lehnert S. Temporal and regional changes in DNA methylation in the embryonic, extraembryonic and germ cell lineages during mouse embryo development. Development. 99:1987;371-382.
    • (1987) Development , vol.99 , pp. 371-382
    • Monk, M.1    Boubelik, M.2    Lehnert, S.3
  • 3
    • 0030840954 scopus 로고    scopus 로고
    • Cytosine methylation and the ecology of intragenomic parasites
    • Yoder J.A., Walsh C.P., Bestor T.H. Cytosine methylation and the ecology of intragenomic parasites. Trends Genet. 13:1997;335-340.
    • (1997) Trends Genet , vol.13 , pp. 335-340
    • Yoder, J.A.1    Walsh, C.P.2    Bestor, T.H.3
  • 4
    • 0025637814 scopus 로고
    • Dynamics of demethylation and activation of the α-actin gene in myoblasts
    • Paroush Z., Keshet I., Yisraeli J., Cedar H. Dynamics of demethylation and activation of the α-actin gene in myoblasts. Cell. 63:1990;1229-1237.
    • (1990) Cell , vol.63 , pp. 1229-1237
    • Paroush, Z.1    Keshet, I.2    Yisraeli, J.3    Cedar, H.4
  • 6
    • 0344002662 scopus 로고
    • B cell-specific demethylation: A novel role for the intronic κ chain enhancer sequences
    • Lichtenstein M., Keini G., Cedar H., Bergman Y. B cell-specific demethylation: a novel role for the intronic κ chain enhancer sequences. Cell. 22:1994;817-823.
    • (1994) Cell , vol.22 , pp. 817-823
    • Lichtenstein, M.1    Keini, G.2    Cedar, H.3    Bergman, Y.4
  • 7
    • 0030572637 scopus 로고    scopus 로고
    • DNA demethylation in vitro: Involvement of RNA
    • Weiss A., Keshet I., Razin A., Cedar H. DNA demethylation in vitro: involvement of RNA. Cell. 86:1996;709-718.
    • (1996) Cell , vol.86 , pp. 709-718
    • Weiss, A.1    Keshet, I.2    Razin, A.3    Cedar, H.4
  • 8
    • 0033580326 scopus 로고    scopus 로고
    • A mammalian protein with specific demethylase activity for mCpG DNA
    • These authors claimed that a demethylase can be eluted at ~4.8-5.0 M NaCl from several successive weak anion exchange columns. This demethylase is identical to a previously reported methyl-CpG binding protein 2B, and it purportedly converts 5-methylcytosine to cytosine without requiring ATP (but see [25,26]).
    • Bhattacharya S.K., Ramchandani S., Cervoni N., Szyf M. A mammalian protein with specific demethylase activity for mCpG DNA. Nature. 397:1999;579-583. These authors claimed that a demethylase can be eluted at ~4.8-5.0 M NaCl from several successive weak anion exchange columns. This demethylase is identical to a previously reported methyl-CpG binding protein 2B, and it purportedly converts 5-methylcytosine to cytosine without requiring ATP (but see [25,26]).
    • (1999) Nature , vol.397 , pp. 579-583
    • Bhattacharya, S.K.1    Ramchandani, S.2    Cervoni, N.3    Szyf, M.4
  • 9
    • 0031964577 scopus 로고    scopus 로고
    • A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast
    • Yoder J.A., Bestor T.H. A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast. Hum Mol Genet. 7:1998;279-284.
    • (1998) Hum Mol Genet , vol.7 , pp. 279-284
    • Yoder, J.A.1    Bestor, T.H.2
  • 10
    • 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. Nat Genet. 19:1998;219-220.
    • (1998) Nat Genet , vol.19 , pp. 219-220
    • Okano, M.1    Xie, S.2    Li, E.3
  • 11
    • 0032102949 scopus 로고    scopus 로고
    • Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells
    • Okano M., Xie S., Li E. Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells. Nucleic Acids Res. 26:1998;2536-2540.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2536-2540
    • Okano, M.1    Xie, S.2    Li, E.3
  • 12
    • 0033499867 scopus 로고    scopus 로고
    • In vivo activity of murine de novo methyltransferases, Dnmt3a and Dnmat3b
    • This paper provides the first evidence that Dnmt3a and Dnmt3b have de novo methyltransferase activity in human cells. The pattern of methylation generated by these two proteins on the stable episome is nonrandom. This study provides evidence that Dnmt3a and Dnmt3b may have preferred targets that are different from DNMT1. Furthermore, Dnmt3a methylates the same sequence on the episome and in the chromosome.
    • Hsieh C-L. In vivo activity of murine de novo methyltransferases, Dnmt3a and Dnmat3b. Mol Cell Biol. 19:1999;8211-8218. This paper provides the first evidence that Dnmt3a and Dnmt3b have de novo methyltransferase activity in human cells. The pattern of methylation generated by these two proteins on the stable episome is nonrandom. This study provides evidence that Dnmt3a and Dnmt3b may have preferred targets that are different from DNMT1. Furthermore, Dnmt3a methylates the same sequence on the episome and in the chromosome.
    • (1999) Mol Cell Biol , vol.19 , pp. 8211-8218
    • Hsieh, C.-L.1
  • 13
    • 0032697888 scopus 로고    scopus 로고
    • Mammalian (cytosine-5) methyltransferases cause genomic DNA methylation and lethality in Drosophila
    • Dnmt3a functions as a de novo methyltransferase whereas no such activity is detected for Dnmt1 in vivo in a Drosophila system. However, Dnmt1 has a higher methylation activity in vitro in the same system. Expression of Dnmt3a can cause developmental defects in Drosophila.
    • Lyko F., Ramsahoye B.H., Kashevsky H., Tudor M., Mastrangelo M-A., Orr-Weaver T.L., Jaenish R. Mammalian (cytosine-5) methyltransferases cause genomic DNA methylation and lethality in Drosophila. Nat Genet. 23:1999;363-366. Dnmt3a functions as a de novo methyltransferase whereas no such activity is detected for Dnmt1 in vivo in a Drosophila system. However, Dnmt1 has a higher methylation activity in vitro in the same system. Expression of Dnmt3a can cause developmental defects in Drosophila.
    • (1999) Nat Genet , vol.23 , pp. 363-366
    • Lyko, F.1    Ramsahoye, B.H.2    Kashevsky, H.3    Tudor, M.4    Mastrangelo, M.-A.5    Orr-Weaver, T.L.6    Jaenish, R.7
  • 14
    • 0033615717 scopus 로고    scopus 로고
    • DNA methylationtransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development
    • Inactivation of Dnmt3a and Dnmt3b in ES cells results in hypomethylation of the satellite sequences, IAP repeats and C-type retroviral DNA. Although disruption of Dnmt3a and Dnmt3b does not influence methylation within region 2 of the Igf2 receptor gene and the 5′ upstream region of the H19 gene, the DMR2 region in the Igf2 gene and the 5′ region of the Xist gene becomes demethylated in undifferentiated double knockout ES cells.
    • Okano M., Bell D.W., Haber D.A., Li E. DNA methylationtransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development. Cell. 99:1999;247-257. Inactivation of Dnmt3a and Dnmt3b in ES cells results in hypomethylation of the satellite sequences, IAP repeats and C-type retroviral DNA. Although disruption of Dnmt3a and Dnmt3b does not influence methylation within region 2 of the Igf2 receptor gene and the 5′ upstream region of the H19 gene, the DMR2 region in the Igf2 gene and the 5′ region of the Xist gene becomes demethylated in undifferentiated double knockout ES cells.
    • (1999) Cell , vol.99 , pp. 247-257
    • Okano, M.1    Bell, D.W.2    Haber, D.A.3    Li, E.4
  • 15
    • 0033547330 scopus 로고    scopus 로고
    • Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene
    • This paper shows that the constitutive abnormality of the genomic methylation pattern in ICF syndrome is the consequence of DNMT3B mutations. This reveals one of the specific targets of DNTM3B and indicates that DNMT3A cannot fully complement the function of DNMT3B.
    • Xu G-L., Bestor T.H., Bourc'his D., Hsieh C-L., Tommerup N., Hulten M., Ou A., Russo J.J., Viegas-Pequignot E. Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene. Nature. 402:1999;187-191. This paper shows that the constitutive abnormality of the genomic methylation pattern in ICF syndrome is the consequence of DNMT3B mutations. This reveals one of the specific targets of DNTM3B and indicates that DNMT3A cannot fully complement the function of DNMT3B.
    • (1999) Nature , vol.402 , pp. 187-191
    • Xu, G.-L.1    Bestor, T.H.2    Bourc'his, D.3    Hsieh, C.-L.4    Tommerup, N.5    Hulten, M.6    Ou, A.7    Russo, J.J.8    Viegas-Pequignot, E.9
  • 17
    • 0033588291 scopus 로고    scopus 로고
    • Factors affecting de novo methylation of foreign DNA in mouse embryonic stem cells
    • Hertz J.M., Schell G., Doerfler W. Factors affecting de novo methylation of foreign DNA in mouse embryonic stem cells. J Biol Chem. 274:1999;24232-24240.
    • (1999) J Biol Chem , vol.274 , pp. 24232-24240
    • Hertz, J.M.1    Schell, G.2    Doerfler, W.3
  • 18
    • 0027342250 scopus 로고
    • Patterns of de novo DNA methylation and promoter inhibition: Studies on the adenovirus and the human genomes
    • J.P. Jost, & H.P. Saluz. Switzerland: Birkhauser Verlag Basel
    • Doerfler W. Patterns of de novo DNA methylation and promoter inhibition: studies on the adenovirus and the human genomes. Jost J.P., Saluz H.P. DNA Methylation: Molecular Biology and Biological Significance. 1993;262-299 Birkhauser Verlag Basel, Switzerland.
    • (1993) DNA Methylation: Molecular Biology and Biological Significance , pp. 262-299
    • Doerfler, W.1
  • 19
    • 0028014280 scopus 로고
    • Enhancement of reporter gene de novo methylation by DNA fragments from the α-fetoprotein control region
    • Hasse A., Schulz W.A. Enhancement of reporter gene de novo methylation by DNA fragments from the α-fetoprotein control region. J Biol Chem. 269:1994;1821-1826.
    • (1994) J Biol Chem , vol.269 , pp. 1821-1826
    • Hasse, A.1    Schulz, W.A.2
  • 20
    • 0030793717 scopus 로고    scopus 로고
    • Stability of patch methylation and its impact in regions of transcriptional initiation and elongation
    • Hsieh C-L. Stability of patch methylation and its impact in regions of transcriptional initiation and elongation. Mol Cell Biol. 17:1997;5897-5904.
    • (1997) Mol Cell Biol , vol.17 , pp. 5897-5904
    • Hsieh, C.-L.1
  • 21
    • 0033153303 scopus 로고    scopus 로고
    • The human DNA methyltransferases (DNMTs) 1, 3a and 3b: Coordinate mRNA expression in normal tissues and overexpression in tumors
    • Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J., Gonzales F.A., Jones P.A. The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. Nucleic Acids Res. 27:1999;2291-2298.
    • (1999) Nucleic Acids Res , vol.27 , pp. 2291-2298
    • Robertson, K.D.1    Uzvolgyi, E.2    Liang, G.3    Talmadge, C.4    Sumegi, J.5    Gonzales, F.A.6    Jones, P.A.7
  • 22
    • 0027310491 scopus 로고
    • Nuclear extracts of chicken embryos promote an active demethylation of DNA by excision repair of 5-methyldeoxycytidine
    • Jost J.P. Nuclear extracts of chicken embryos promote an active demethylation of DNA by excision repair of 5-methyldeoxycytidine. Proc Natl Acad Sci USA. 90:1993;4684-4688.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4684-4688
    • Jost, J.P.1
  • 23
    • 1842289276 scopus 로고    scopus 로고
    • The RNA moiety of chick embryo 5-methylcytosine-DNA glycosylase targets DNA demethylation
    • Jost J.P., Frémont M., Siegmann M., Hofsteenge J. The RNA moiety of chick embryo 5-methylcytosine-DNA glycosylase targets DNA demethylation. Nucleic Acids Res. 25:1997;4545-4550.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4545-4550
    • Jost, J.P.1    Frémont, M.2    Siegmann, M.3    Hofsteenge, J.4
  • 24
    • 0032534635 scopus 로고    scopus 로고
    • Analysis of putative Rnase sensitivity and protease insensitivity of demethylation activity in extracts from rat myoblasts
    • This study ruled out that a demethylase activity previously reported to be a ribozyme (see [7]) involves an RNA cofactor or a ribozyme component. The importance of this paper is to clarify that the demethylase is most likely a protein.
    • Swisher J.F., Rand E., Cedar H., Marie Pyle A. Analysis of putative Rnase sensitivity and protease insensitivity of demethylation activity in extracts from rat myoblasts. Nucleic Acids Res. 26:1998;5573-5580. This study ruled out that a demethylase activity previously reported to be a ribozyme (see [7]) involves an RNA cofactor or a ribozyme component. The importance of this paper is to clarify that the demethylase is most likely a protein.
    • (1998) Nucleic Acids Res , vol.26 , pp. 5573-5580
    • Swisher, J.F.1    Rand, E.2    Cedar, H.3    Marie Pyle, A.4
  • 25
    • 0031792779 scopus 로고    scopus 로고
    • Identification and characterization of a family of mammalian methyl-CpG binding protein
    • Hendrich B., Bird A. Identification and characterization of a family of mammalian methyl-CpG binding protein. Mol Cell Biol. 18:1998;6538-6547.
    • (1998) Mol Cell Biol , vol.18 , pp. 6538-6547
    • Hendrich, B.1    Bird, A.2
  • 26
    • 0033605556 scopus 로고    scopus 로고
    • DNA demethylase is a processive enzyme
    • Cervoni N., Bhattacharya S., Szyf M. DNA demethylase is a processive enzyme. J Biol Chem. 274:1999;8363-8366.
    • (1999) J Biol Chem , vol.274 , pp. 8363-8366
    • Cervoni, N.1    Bhattacharya, S.2    Szyf, M.3
  • 29
    • 0032845039 scopus 로고    scopus 로고
    • Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation
    • Mi-2 from Xenopus is part of a histone deacetylase complex that contains three subunits. One of the subunits, p35, has similarity to mammalian MBD3 and MBD2. The Mi-2 complex is found to have no demethylase activity.
    • Wade P.A., Gegonne A., Jones P.L., Ballestar E., Aubry F., Wolffe A.P. Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation. Nat Genet. 23:1999;62-66. Mi-2 from Xenopus is part of a histone deacetylase complex that contains three subunits. One of the subunits, p35, has similarity to mammalian MBD3 and MBD2. The Mi-2 complex is found to have no demethylase activity.
    • (1999) Nat Genet , vol.23 , pp. 62-66
    • Wade, P.A.1    Gegonne, A.2    Jones, P.L.3    Ballestar, E.4    Aubry, F.5    Wolffe, A.P.6
  • 30
    • 0032473428 scopus 로고    scopus 로고
    • An embryonic demethylation mechanism involving binding of transcription factors to replicating DNA
    • Matsuo K., Silke J., Georgiev O., Marti P., Giovannini N., Rungger D. An embryonic demethylation mechanism involving binding of transcription factors to replicating DNA. EMBO J. 17:1998;1446-1453.
    • (1998) EMBO J , vol.17 , pp. 1446-1453
    • Matsuo, K.1    Silke, J.2    Georgiev, O.3    Marti, P.4    Giovannini, N.5    Rungger, D.6
  • 31
    • 0032937871 scopus 로고    scopus 로고
    • Evidence that protein binding specifies sites of DNA demethylation
    • Demethylation sites within the oriP region are specified by EBNA-1 binding. Demethylation of the first strand involves a replication-dependent pathway, and the second strand demethylation appears to involve an active demethylase.
    • Hsieh C-L. Evidence that protein binding specifies sites of DNA demethylation. Mol Cell Biol. 19:1999;46-56. Demethylation sites within the oriP region are specified by EBNA-1 binding. Demethylation of the first strand involves a replication-dependent pathway, and the second strand demethylation appears to involve an active demethylase.
    • (1999) Mol Cell Biol , vol.19 , pp. 46-56
    • Hsieh, C.-L.1
  • 32
    • 0034017955 scopus 로고    scopus 로고
    • Modulation of DNA binding protein affinity directly affects target site demethylation
    • in press. This paper further supports the hypothesis that demethylation in human cells is initiated by specific DNA-binding proteins. The possibility of transcriptional effects is also ruled out. By titrating the binding protein in the system, this study showed for the first time that demethylation at DNA sites can be determined by the protein binding site occupancy.
    • Lin I.P., Tomzynski T.J., Ou Q., Hsieh C-L. Modulation of DNA binding protein affinity directly affects target site demethylation. Mol Cell Biol. 2000;. in press. This paper further supports the hypothesis that demethylation in human cells is initiated by specific DNA-binding proteins. The possibility of transcriptional effects is also ruled out. By titrating the binding protein in the system, this study showed for the first time that demethylation at DNA sites can be determined by the protein binding site occupancy.
    • (2000) Mol Cell Biol
    • Lin, I.P.1    Tomzynski, T.J.2    Ou, Q.3    Hsieh, C.-L.4
  • 34
    • 0034598784 scopus 로고    scopus 로고
    • Demethylation of the zygotic paternal genome
    • Maternal and paternal chromosomes are compartmentalized during early embryogenesis and demethylation of these two sets of chromosomes occurs at different times via different mechanisms. The concept of how the methylation pattern is established in the preimplantation stage may be changed if the findings in this study are confirmed.
    • Mayer W., Niveleau A., Walter J., Fundele R., Haaf T. Demethylation of the zygotic paternal genome. Nature. 403:2000;501-502. Maternal and paternal chromosomes are compartmentalized during early embryogenesis and demethylation of these two sets of chromosomes occurs at different times via different mechanisms. The concept of how the methylation pattern is established in the preimplantation stage may be changed if the findings in this study are confirmed.
    • (2000) Nature , vol.403 , pp. 501-502
    • Mayer, W.1    Niveleau, A.2    Walter, J.3    Fundele, R.4    Haaf, T.5
  • 35
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
    • The methyl-CpG binding domain of MBD4 preferentially binds to the deaminated product of methyl-CpG. MBD4 can remove thymine or uracil from a CpG site with mismatches generated either by cytosine deamination or by methyl-cytosine deamination in vitro. It is suggested that MBD4 may be responsible for eliminating mutations at methyl-CpG sites.
    • Hendrich B., Hardeland U., Ng H-H., Jiricny J., Bird A. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature. 401:1999;301-304. The methyl-CpG binding domain of MBD4 preferentially binds to the deaminated product of methyl-CpG. MBD4 can remove thymine or uracil from a CpG site with mismatches generated either by cytosine deamination or by methyl-cytosine deamination in vitro. It is suggested that MBD4 may be responsible for eliminating mutations at methyl-CpG sites.
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.-H.3    Jiricny, J.4    Bird, A.5


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