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Volumn 15, Issue 7, 1996, Pages 1705-1714

A preference of histone H1 for methylated DNA

Author keywords

Cooperativity; DNA methylation; H1 variants; H1 DNA complexes; Histone H1

Indexed keywords

DNA; HISTONE H1; RESTRICTION ENDONUCLEASE;

EID: 0029964505     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00516.x     Document Type: Article
Times cited : (63)

References (37)
  • 1
    • 0021029105 scopus 로고
    • 5-methylcytosine is localised in nucleosomes that contain histone H1
    • Ball, D J., Gross, D.S. and Garrard, W.T. (1983) 5-methylcytosine is localised in nucleosomes that contain histone H1. Proc. Natl Acad. Sci. USA, 80, 5490-5494.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 5490-5494
    • Ball, D.J.1    Gross, D.S.2    Garrard, W.T.3
  • 2
    • 0019628147 scopus 로고
    • Stability of the higher-order structure of chicken erythrocyte chromatin in solution
    • Bates, D.L., Butler, P.J.G., Pearson, E.C. and Thomas, J.O. (1981) Stability of the higher-order structure of chicken erythrocyte chromatin in solution Eur. J. Biochem., 119, 469-476.
    • (1981) Eur. J. Biochem. , vol.119 , pp. 469-476
    • Bates, D.L.1    Butler, P.J.G.2    Pearson, E.C.3    Thomas, J.O.4
  • 3
    • 0022540321 scopus 로고
    • CpG-rich islands and the function of DNA methylation
    • Bird, A.P. (1986) CpG-rich islands and the function of DNA methylation. Nature, 321, 209-213.
    • (1986) Nature , vol.321 , pp. 209-213
    • Bird, A.P.1
  • 4
    • 0018289345 scopus 로고
    • Methylated and unmethylated DNA compartments in the sea urchin genome
    • Bird, A.P., Taggart, M.H. and Smith, B.A. (1979) Methylated and unmethylated DNA compartments in the sea urchin genome. Cell, 17, 889-901.
    • (1979) Cell , vol.17 , pp. 889-901
    • Bird, A.P.1    Taggart, M.H.2    Smith, B.A.3
  • 5
    • 0344630574 scopus 로고
    • Chromatin structure is required to block transcription of the methylated herpes simplex virus thymidine kinase gene
    • Buschhausen, G, Wittig, B., Graessmann, M. and Graessmann, A. (1987) Chromatin structure is required to block transcription of the methylated herpes simplex virus thymidine kinase gene. Proc. Natl Acad. Sci. USA, 84, 1177-1181.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1177-1181
    • Buschhausen, G.1    Wittig, B.2    Graessmann, M.3    Graessmann, A.4
  • 6
    • 0024281345 scopus 로고
    • DNA methylation and gene activity
    • Cedar, H. (1988) DNA methylation and gene activity. Cell, 53, 3-4.
    • (1988) Cell , vol.53 , pp. 3-4
    • Cedar, H.1
  • 7
    • 0028068811 scopus 로고
    • Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Full assignment, tertiary structure, and comparison with the globular domain of H5
    • Cerf, C., Lippens, G., Ramakrishnan, V., Muyldermans, S., Segers, A., Wyns, L., Wodak, S.J. and Hallenga, K. (1994) Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of H5. Biochemistry, 33, 11079-11086.
    • (1994) Biochemistry , vol.33 , pp. 11079-11086
    • Cerf, C.1    Lippens, G.2    Ramakrishnan, V.3    Muyldermans, S.4    Segers, A.5    Wyns, L.6    Wodak, S.J.7    Hallenga, K.8
  • 8
    • 0022470051 scopus 로고
    • Salt-dependent co-operative interaction of histone H1 with linear DNA
    • Clark, D.J. and Thomas, J.O. (1986) Salt-dependent co-operative interaction of histone H1 with linear DNA. J. Mol. Biol., 187, 569-580
    • (1986) J. Mol. Biol. , vol.187 , pp. 569-580
    • Clark, D.J.1    Thomas, J.O.2
  • 9
    • 0024264685 scopus 로고
    • Differences in the binding of H1 variants to DNA: Cooperativity and linker-length related distribution
    • Clark, D.J. and Thomas, J.O. (1988) Differences in the binding of H1 variants to DNA: cooperativity and linker-length related distribution. Eur. J. Biochem., 178, 225-233.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 225-233
    • Clark, D.J.1    Thomas, J.O.2
  • 10
    • 0023711642 scopus 로고
    • α-Helix in the carboxy-terminal domains of histones H1 and H5
    • Clark, D J., Hill, C.S., Martin, S.R. and Thomas, J.O. (1988) α-Helix in the carboxy-terminal domains of histones H1 and H5. EMBO J, 7, 69-75.
    • (1988) EMBO J , vol.7 , pp. 69-75
    • Clark, D.J.1    Hill, C.S.2    Martin, S.R.3    Thomas, J.O.4
  • 11
    • 0026663825 scopus 로고
    • Co-operative binding of the globular domain of histone H5 to DNA
    • Draves, P.H., Lowary, P.T. and Widom, J. (1992) Co-operative binding of the globular domain of histone H5 to DNA. J. Mol Biol, 225, 1105-1121.
    • (1992) J. Mol Biol , vol.225 , pp. 1105-1121
    • Draves, P.H.1    Lowary, P.T.2    Widom, J.3
  • 12
    • 0028031310 scopus 로고
    • Contacts of the globular domain of histone H5 and core histones with DNA in a 'chromatosome'
    • Hayes, J.J., Pruss, D. and Wolffe, A.P. (1994) Contacts of the globular domain of histone H5 and core histones with DNA in a 'chromatosome' Proc. Natl Acad. Sci. USA, 91, 7817-7821.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7817-7821
    • Hayes, J.J.1    Pruss, D.2    Wolffe, A.P.3
  • 13
    • 0025744289 scopus 로고
    • The combination of DNA methylation and H1 histone binding inhibits the action of a restriction nuclease on plasmid DNA
    • Higurashi, M. and Cole, R.D. (1991) The combination of DNA methylation and H1 histone binding inhibits the action of a restriction nuclease on plasmid DNA. J. Biol. Chem., 266, 8619-8625.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8619-8625
    • Higurashi, M.1    Cole, R.D.2
  • 14
    • 0025764058 scopus 로고
    • Histone-DNA interactions and their modulation by phosphorylation of Ser-Pro-X-Lys/Arg- Motifs
    • Hill, C.S., Rimmer, J.M., Green, B.N., Finch, J.T. and Thomas, J.O. (1991) Histone-DNA interactions and their modulation by phosphorylation of Ser-Pro-X-Lys/Arg- motifs. EMBO J., 10, 1939-1948.
    • (1991) EMBO J. , vol.10 , pp. 1939-1948
    • Hill, C.S.1    Rimmer, J.M.2    Green, B.N.3    Finch, J.T.4    Thomas, J.O.5
  • 15
    • 0028954415 scopus 로고
    • The effect of histone H1 and DNA methylation on transcription
    • Johnson, C.A., Goddard, J.P. and Adams, R.L.P. (1995) The effect of histone H1 and DNA methylation on transcription. Biochem. J., 305, 791-798.
    • (1995) Biochem. J. , vol.305 , pp. 791-798
    • Johnson, C.A.1    Goddard, J.P.2    Adams, R.L.P.3
  • 16
    • 0026668770 scopus 로고
    • The repressor MDBP-2 is a member of the histone H1 family that binds preferentially in vitro and in vivo to methylated nonspecific DNA sequences
    • Jost, J.-P. and Hofsteenge, J. (1992) The repressor MDBP-2 is a member of the histone H1 family that binds preferentially in vitro and in vivo to methylated nonspecific DNA sequences. Proc. Natl Acad. Sci. USA, 89, 9499-9503.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9499-9503
    • Jost, J.-P.1    Hofsteenge, J.2
  • 17
    • 0025081555 scopus 로고
    • Chromatin structure of transcriptionally competent and repressed genes
    • Kamakaka, R.T. and Thomas, J.O. (1990) Chromatin structure of transcriptionally competent and repressed genes- EMBO J., 9, 3997-4006.
    • (1990) EMBO J. , vol.9 , pp. 3997-4006
    • Kamakaka, R.T.1    Thomas, J.O.2
  • 18
    • 0022545498 scopus 로고
    • DNA methylation affects the formation of active chromatin
    • Keshet, I., Lieman-Hurwitz, J. and Cedar, H. (1986) DNA methylation affects the formation of active chromatin. Cell, 44, 535-543.
    • (1986) Cell , vol.44 , pp. 535-543
    • Keshet, I.1    Lieman-Hurwitz, J.2    Cedar, H.3
  • 19
    • 0024814234 scopus 로고
    • Bending of DNA by gene-regulatory proteins - Construction and use of a DNA bending vector
    • Kim, J., Zweib, C., Wu, C. and Adhya, S. (1989) Bending of DNA by gene-regulatory proteins - construction and use of a DNA bending vector. Gene, 85, 15-23.
    • (1989) Gene , vol.85 , pp. 15-23
    • Kim, J.1    Zweib, C.2    Wu, C.3    Adhya, S.4
  • 20
    • 0027486811 scopus 로고
    • Histone H1-mediated inhibition of transcription initiation of methylated templates in vitro
    • Levine, A., Yeivin, A., Ben-Asher, E., Aloni, Y. and Razin, A. (1993) Histone H1-mediated inhibition of transcription initiation of methylated templates in vitro. J. Biol. Chem., 268, 21754-21759.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21754-21759
    • Levine, A.1    Yeivin, A.2    Ben-Asher, E.3    Aloni, Y.4    Razin, A.5
  • 21
    • 0026747761 scopus 로고
    • Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA
    • Lewis, J.D., Meehan, R.R., Henzel, W.J., Maurer-Fogy, I., Jeppesen, P., Klein, F. and Bird, A. (1992) Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA. Cell, 69, 905-914
    • (1992) Cell , vol.69 , pp. 905-914
    • Lewis, J.D.1    Meehan, R.R.2    Henzel, W.J.3    Maurer-Fogy, I.4    Jeppesen, P.5    Klein, F.6    Bird, A.7
  • 22
    • 0024342686 scopus 로고
    • Identification of a mammalian protein that binds specifically to DNA containing methylated CpGs
    • Meehan, R.R., Lewis, J.D, McKay, S., Kleiner, E.L. and Bird, A.P. (1989) Identification of a mammalian protein that binds specifically to DNA containing methylated CpGs. Cell, 58, 499-507.
    • (1989) Cell , vol.58 , pp. 499-507
    • Meehan, R.R.1    Lewis, J.D.2    McKay, S.3    Kleiner, E.L.4    Bird, A.P.5
  • 23
    • 0026658662 scopus 로고
    • Characterization of MeCP2, a vertebrate DNA binding protein with affinity for methylated DNA
    • Meehan, R.R., Lewis, J.D. and Bird, A.P. (1992) Characterization of MeCP2, a vertebrate DNA binding protein with affinity for methylated DNA. Nucleic Acids Res., 20, 5085-5092.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5085-5092
    • Meehan, R.R.1    Lewis, J.D.2    Bird, A.P.3
  • 24
    • 0010007475 scopus 로고
    • Use of a protein-blotting procedure to identify nuclear proteins that recognize the promoter regions of the transferrin receptor gene
    • Miskimins, W.K., Roberts, M.P., McClelland, A. and Ruddle, F.H. (1985) Use of a protein-blotting procedure to identify nuclear proteins that recognize the promoter regions of the transferrin receptor gene. Proc. Natl Acad. Sci USA, 82, 6741-6744.
    • (1985) Proc. Natl Acad. Sci USA , vol.82 , pp. 6741-6744
    • Miskimins, W.K.1    Roberts, M.P.2    McClelland, A.3    Ruddle, F.H.4
  • 25
    • 0028954144 scopus 로고
    • Methylation at CpG sequences does not influence histone H1 binding to a nucleosome including Xenopus borealis SS rRNA gene
    • Nightingale, K. and Wolffe, A P. (1995) Methylation at CpG sequences does not influence histone H1 binding to a nucleosome including Xenopus borealis SS rRNA gene. J. Biol. Chem., 270, 4197-4200.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4197-4200
    • Nightingale, K.1    Wolffe, A.P.2
  • 26
    • 0016734866 scopus 로고
    • Preparation of native chromatin and damage caused by shearing
    • Noll, M., Thomas, J.O. and Kornberg, R.D. (1975) Preparation of native chromatin and damage caused by shearing, Science, 187, 1203-1206.
    • (1975) Science , vol.187 , pp. 1203-1206
    • Noll, M.1    Thomas, J.O.2    Kornberg, R.D.3
  • 27
    • 0027402969 scopus 로고
    • Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J.T., Graziano, V., Lee, P.L. and Sweet, R.M. (1993) Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding. Nature, 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 28
    • 0016629558 scopus 로고
    • Preferential and cooperative binding of histone 1 to chromosomal mammalian DNA
    • Renz, M. (1975) Preferential and cooperative binding of histone 1 to chromosomal mammalian DNA. Proc. Natl Acad. Sci. USA, 72, 733-736.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 733-736
    • Renz, M.1
  • 31
    • 0025266610 scopus 로고
    • Alternative chromatin structure at CpG islands
    • Tazi, J. and Bird, A. (1990) Alternative chromatin structure at CpG islands. Cell, 60, 909-920.
    • (1990) Cell , vol.60 , pp. 909-920
    • Tazi, J.1    Bird, A.2
  • 32
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructure of chromatin
    • Thoma, F., Koller, T. and Klug, A. (1979) Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructure of chromatin. J. Cell Biol., 83, 403-427.
    • (1979) J. Cell Biol. , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 33
    • 0017903377 scopus 로고
    • A study of histone-histone associations by chemical cross-linking
    • Thomas, J.O. and Kornberg, R.D. (1978) A study of histone-histone associations by chemical cross-linking. Methods Cell Biol., 18, 429-440.
    • (1978) Methods Cell Biol. , vol.18 , pp. 429-440
    • Thomas, J.O.1    Kornberg, R.D.2
  • 34
    • 0022541447 scopus 로고
    • Salt-induced folding of sea urchin sperm chromatin
    • Thomas, J.O., Rees, C. and Butler, P.J.G. (1986) Salt-induced folding of sea urchin sperm chromatin. Eur. J. Biochem., 154, 343-348.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 343-348
    • Thomas, J.O.1    Rees, C.2    Butler, P.J.G.3
  • 35
    • 0026597552 scopus 로고
    • Cooperative binding of the globular domains of histones H1 and H5 to DNA
    • Thomas, J.O., Rees, C. and Finch, J.T. (1992) Cooperative binding of the globular domains of histones H1 and H5 to DNA Nucleic Acids Res., 20, 187-194.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 187-194
    • Thomas, J.O.1    Rees, C.2    Finch, J.T.3
  • 36
    • 0024046344 scopus 로고
    • In situ detection of sequence-specific DNA binding activity specified by a recombinant bacteriophage
    • Vinson, C.R., LaMarco, K.L., Johnson, P.F., Landschulz, W.H. and McKnight, S.L. (1988) In situ detection of sequence-specific DNA binding activity specified by a recombinant bacteriophage. Genes Dev., 2, 801-806.
    • (1988) Genes Dev. , vol.2 , pp. 801-806
    • Vinson, C.R.1    LaMarco, K.L.2    Johnson, P.F.3    Landschulz, W.H.4    McKnight, S.L.5
  • 37
    • 0018171799 scopus 로고
    • MspI an isoschizomer of HpaII which cleaves both nonmethylated and methylated HpaII sites
    • Waalwijk, C. and Flavell, R.A. (1978) MspI an isoschizomer of HpaII which cleaves both nonmethylated and methylated HpaII sites. Nucleic Acids Res., 5, 3231-3236.
    • (1978) Nucleic Acids Res. , vol.5 , pp. 3231-3236
    • Waalwijk, C.1    Flavell, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.