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Volumn 37, Issue 9, 2009, Pages 2818-2829

Distinctive sequence patterns in metazoan and yeast nucleosomes: Implications for linker histone binding to AT-rich and methylated DNA

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; DNA; HISTONE; LINKER HISTONE; THYMINE; UNCLASSIFIED DRUG;

EID: 66249136850     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp113     Document Type: Article
Times cited : (52)

References (72)
  • 1
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures 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 superstructures 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
  • 2
    • 33744831161 scopus 로고    scopus 로고
    • Structure of the '30 nm' chromatin fibre: A key role for the linker histone
    • Robinson, P.J. and Rhodes, D. (2006) Structure of the '30 nm' chromatin fibre: A key role for the linker histone. Curr. Opin. Struct. Biol. 16, 336-343.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 336-343
    • Robinson, P.J.1    Rhodes, D.2
  • 3
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • Woodcock, C.L., Skoultchi, A.I. and Fan, Y. (2006) Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res., 14, 17-25.
    • (2006) Chromosome Res , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoultchi, A.I.2    Fan, Y.3
  • 4
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones
    • Simpson, R.T. (1978) Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry 17, 5524-5531.
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 5
    • 84984424074 scopus 로고
    • Complexes of histone F1 with DNA in 0.15M NaCl
    • Sponar, J. and Sormova, Z. (1972) Complexes of histone F1 with DNA in 0.15M NaCl. Eur. J. Biochem., 29, 99-103.
    • (1972) Eur. J. Biochem , vol.29 , pp. 99-103
    • Sponar, J.1    Sormova, Z.2
  • 6
    • 0024820573 scopus 로고
    • Specific inhibition of DNA binding to nuclear scaffolds and histone H1 by distamycin
    • Kas, E., Izaurralde, E. and Laemmli, U.K. (1989) Specific inhibition of DNA binding to nuclear scaffolds and histone H1 by distamycin. J. Mol. Biol., 210, 587-599.
    • (1989) J. Mol. Biol , vol.210 , pp. 587-599
    • Kas, E.1    Izaurralde, E.2    Laemmli, U.K.3
  • 7
    • 0029680555 scopus 로고    scopus 로고
    • The linker histones and chromatin structure: New twists
    • Zlatanova, J. and van Holde, K. (1996) The linker histones and chromatin structure: New twists. Prog. Nucleic Acid Res. Mol. Biol., 52 217-259.
    • (1996) Prog. Nucleic Acid Res. Mol. Biol , vol.52 , pp. 217-259
    • Zlatanova, J.1    van Holde, K.2
  • 10
    • 34047111213 scopus 로고    scopus 로고
    • Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome
    • Albert, I., Mavrich, T.N., Tomsho, L.P., Qi, J., Zanton, S.J., Schuster, S.C. and Pugh, B.F. (2007) Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome. Nature, 446, 572-576.
    • (2007) Nature , vol.446 , pp. 572-576
    • Albert, I.1    Mavrich, T.N.2    Tomsho, L.P.3    Qi, J.4    Zanton, S.J.5    Schuster, S.C.6    Pugh, B.F.7
  • 12
    • 0023001414 scopus 로고
    • Sequence periodicities in chicken nucleosome core DNA
    • Satchwell, S.C., Drew, H.R. and Travers, A.A. (1986) Sequence periodicities in chicken nucleosome core DNA. J. Mol. Biol., 191, 659-675.
    • (1986) J. Mol. Biol , vol.191 , pp. 659-675
    • Satchwell, S.C.1    Drew, H.R.2    Travers, A.A.3
  • 13
    • 0001415964 scopus 로고
    • The pitch of chromatin DNA is reflected in its nucleotide sequence
    • Trifonov, E.N. and Sussman, J.L. (1980) The pitch of chromatin DNA is reflected in its nucleotide sequence. Proc. Natl Acad. Sci. USA, 77, 3816-3820.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 3816-3820
    • Trifonov, E.N.1    Sussman, J.L.2
  • 14
    • 0003903126 scopus 로고
    • Springer, New York, NY, pp
    • van Holde, K. (1988) Chromatin. Springer, New York, NY, pp. 289-354.
    • (1988) Chromatin , pp. 289-354
    • van Holde, K.1
  • 15
    • 0019888694 scopus 로고
    • Histone H1 and H5: One or two molecules per nucleosome?
    • Bates, D.L. and Thomas, J.O. (1981) Histone H1 and H5: One or two molecules per nucleosome? Nucleic Acids Res., 9, 5883-5894.
    • (1981) Nucleic Acids Res , vol.9 , pp. 5883-5894
    • Bates, D.L.1    Thomas, J.O.2
  • 16
    • 0035477211 scopus 로고    scopus 로고
    • Specific distribution of the Saccharomyces cerevisiae linker histone homolog HHO1p in the chromatin
    • Freidkin, I. and Katcoff, D.J. (2001) Specific distribution of the Saccharomyces cerevisiae linker histone homolog HHO1p in the chromatin. Nucleic Acids Res., 9, 4043-4051.
    • (2001) Nucleic Acids Res , vol.9 , pp. 4043-4051
    • Freidkin, I.1    Katcoff, D.J.2
  • 17
    • 0037490067 scopus 로고    scopus 로고
    • Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone
    • Downs, J.A., Kosmidou, E., Morgan, A. and Jackson, S.P. (2003) Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone. Mol. Cell, 11, 1685-1692.
    • (2003) Mol. Cell , vol.11 , pp. 1685-1692
    • Downs, J.A.1    Kosmidou, E.2    Morgan, A.3    Jackson, S.P.4
  • 19
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9Å resolution
    • Davey, C.A., Sargent, D.F., Luger, K., Maeder, A.W. and Richmond, T.J. (2002) Solvent mediated interactions in the structure of the nucleosome core particle at 1.9Å resolution. J. Mol. Biol., 319, 1097-1113.
    • (2002) J. Mol. Biol , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 20
    • 0027402969 scopus 로고
    • Crystal structure of 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 globular domain of histone H5 and its implications for nucleosome binding. Nature, 362, 219-224.
    • (1993) Nature , vol.362 , pp. 219-224
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 21
    • 0025800219 scopus 로고
    • Static and statistical bending of DNA evaluated by Monte Carlo simulations
    • Zhurkin, V.B., Ulyanov, N.B., Gorin, A.A. and Jernigan, R.L. (1991) Static and statistical bending of DNA evaluated by Monte Carlo simulations. Proc. Natl Acad. Sci. USA, 88, 7046-7050.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7046-7050
    • Zhurkin, V.B.1    Ulyanov, N.B.2    Gorin, A.A.3    Jernigan, R.L.4
  • 22
    • 0028931709 scopus 로고
    • B-DNA twisting correlates with base-pair morphology
    • Gorin, A.A., Zhurkin, V.B. and Olson, W.K. (1995) B-DNA twisting correlates with base-pair morphology. J. Mol. Biol., 247, 34-48.
    • (1995) J. Mol. Biol , vol.247 , pp. 34-48
    • Gorin, A.A.1    Zhurkin, V.B.2    Olson, W.K.3
  • 23
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1Å
    • Pavletich, N.P. and Pabo, C.O. (1991) Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1Å. Science, 252, 809-817.
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2
  • 24
    • 21444444520 scopus 로고    scopus 로고
    • How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: A view from high-resolution crystal structures
    • Court, R., Chapman, L., Fairall, L. and Rhodes, D. (2005) How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: A view from high-resolution crystal structures. EMBO Rep., 6, 39-45.
    • (2005) EMBO Rep , vol.6 , pp. 39-45
    • Court, R.1    Chapman, L.2    Fairall, L.3    Rhodes, D.4
  • 25
    • 0022527052 scopus 로고
    • Sequence-directed curvature of DNA
    • Hagerman, P.J. (1986) Sequence-directed curvature of DNA. Nature, 321, 449-450.
    • (1986) Nature , vol.321 , pp. 449-450
    • Hagerman, P.J.1
  • 26
    • 0023846051 scopus 로고
    • Structural details of an adenine tract that does not cause DNA to bend
    • Burkhoff, A.M. and Tullius, T.D. (1988) Structural details of an adenine tract that does not cause DNA to bend. Nature, 331, 455-457.
    • (1988) Nature , vol.331 , pp. 455-457
    • Burkhoff, A.M.1    Tullius, T.D.2
  • 27
  • 28
    • 0019888118 scopus 로고
    • Sequence specific cleavage of DNA by micrococcal nuclease
    • Horz, W. and Altenburger, W. (1981) Sequence specific cleavage of DNA by micrococcal nuclease. Nucleic Acids Res., 9, 2643-2658.
    • (1981) Nucleic Acids Res , vol.9 , pp. 2643-2658
    • Horz, W.1    Altenburger, W.2
  • 29
    • 57149119464 scopus 로고    scopus 로고
    • Field, Y., Kaplan, N., Fondufe-Mittendorf, Y., Moore, I.K., Sharon, E., Lubling, Y., Widom, J. and Segal, E. (2008) Distinct modes of regulation by chromatin encoded through nucleosome positioning signals. PLoS Comput. Biol., 4, e1000216. doi:10.1371/journal.pcbi.1000216.
    • Field, Y., Kaplan, N., Fondufe-Mittendorf, Y., Moore, I.K., Sharon, E., Lubling, Y., Widom, J. and Segal, E. (2008) Distinct modes of regulation by chromatin encoded through nucleosome positioning signals. PLoS Comput. Biol., 4, e1000216. doi:10.1371/journal.pcbi.1000216.
  • 30
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R.K., Clarkson, M.J., Tremethick, D.J. and Luger, K. (2000) Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol., 7, 1121-1124.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 32
    • 0030219940 scopus 로고    scopus 로고
    • Histone H1 in Saccharomyces cerevisiae: A double mystery solved?
    • Landsman, D. (1996) Histone H1 in Saccharomyces cerevisiae: A double mystery solved? Trends Biochem. Sci., 21, 287-288.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 287-288
    • Landsman, D.1
  • 34
    • 33845298285 scopus 로고    scopus 로고
    • Flexibility and constraint in the nucleosome core landscape of Caenorhabditis elegans chromatin
    • Johnson, S.M., Tan, F.J., McCullough, H.L., Riordan, D.P. and Fire, A.Z. (2006) Flexibility and constraint in the nucleosome core landscape of Caenorhabditis elegans chromatin. Genome Res., 16, 1505-1516.
    • (2006) Genome Res , vol.16 , pp. 1505-1516
    • Johnson, S.M.1    Tan, F.J.2    McCullough, H.L.3    Riordan, D.P.4    Fire, A.Z.5
  • 35
    • 0019887286 scopus 로고
    • Periodicity in DNA primary structure is defined by secondary structure of the coded protein
    • Zhurkin, V.B. (1981) Periodicity in DNA primary structure is defined by secondary structure of the coded protein. Nucleic Acids Res., 9 1963-1971.
    • (1981) Nucleic Acids Res , vol.9 , pp. 1963-1971
    • Zhurkin, V.B.1
  • 36
    • 0034522793 scopus 로고    scopus 로고
    • Asymmetries in the nucleosome core particle at 2.5 Ångstrom resolution
    • Harp, J.M., Hanson, B.L., Timm, D.E. and Bunick, G.J. (2000) Asymmetries in the nucleosome core particle at 2.5 Ångstrom resolution. Acta Crystallogr., D56, 1513-1534.
    • (2000) Acta Crystallogr , vol.D56 , pp. 1513-1534
    • Harp, J.M.1    Hanson, B.L.2    Timm, D.E.3    Bunick, G.J.4
  • 37
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White, C.L., Suto, R.K. and Luger, K. (2001) Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J., 20, 5207-5218.
    • (2001) EMBO J , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 38
    • 40549121635 scopus 로고    scopus 로고
    • Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer
    • Clapier, C.R., Chakravarthy, S., Petosa, C., Fernandez-Tornero, C., Luger, K. and Muller, C.W. (2008) Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. Proteins, 71, 1-7.
    • (2008) Proteins , vol.71 , pp. 1-7
    • Clapier, C.R.1    Chakravarthy, S.2    Petosa, C.3    Fernandez-Tornero, C.4    Luger, K.5    Muller, C.W.6
  • 39
    • 0025321717 scopus 로고
    • Structure of nucleosomes and organization of internucleosomal DNA in chromatin
    • Bavykin, S.G., Usachenko, S.I., Zalensky, A.O. and Mirzabekov, A.D. (1990) Structure of nucleosomes and organization of internucleosomal DNA in chromatin. J. Mol. Biol., 212, 495-511.
    • (1990) J. Mol. Biol , vol.212 , pp. 495-511
    • Bavykin, S.G.1    Usachenko, S.I.2    Zalensky, A.O.3    Mirzabekov, A.D.4
  • 41
    • 0034680588 scopus 로고    scopus 로고
    • Two DNA-binding sites on the globular domain of histone H5 are required for binding to both bulk and 5S reconstituted nucleosomes
    • Duggan, M.M. and Thomas, J.O. (2000) Two DNA-binding sites on the globular domain of histone H5 are required for binding to both bulk and 5S reconstituted nucleosomes. J. Mol. Biol., 304, 21-33.
    • (2000) J. Mol. Biol , vol.304 , pp. 21-33
    • Duggan, M.M.1    Thomas, J.O.2
  • 42
    • 33644800314 scopus 로고    scopus 로고
    • Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo
    • Brown, D.T., Izard, T. and Misteli, T. (2006) Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo. Nat. Struct. Mol. Biol., 13, 250-255.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 250-255
    • Brown, D.T.1    Izard, T.2    Misteli, T.3
  • 43
    • 0032563864 scopus 로고    scopus 로고
    • Position and orientation of the globular domain of linker histone H5 on the nucleosome
    • Zhou, Y.B., Gerchman, S.E., Ramakrishana, V., Travers, A. and Muyldermans, S. (1998) Position and orientation of the globular domain of linker histone H5 on the nucleosome. Nature, 395, 402-405.
    • (1998) Nature , vol.395 , pp. 402-405
    • Zhou, Y.B.1    Gerchman, S.E.2    Ramakrishana, V.3    Travers, A.4    Muyldermans, S.5
  • 44
    • 0242285999 scopus 로고    scopus 로고
    • Molecular modeling of the chromatosome particle
    • Bharath, M.M.S., Chandra, N.R. and Rao, M.R.S. (2003) Molecular modeling of the chromatosome particle. Nucleic Acids Res., 31, 4264-4274.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4264-4274
    • Bharath, M.M.S.1    Chandra, N.R.2    Rao, M.R.S.3
  • 45
    • 1842474282 scopus 로고    scopus 로고
    • Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p
    • Ali, T., Coles, P., Stevens, T.J., Stott, K. and Thomas, J.O. (2004) Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. J. Mol. Biol., 338, 139-148.
    • (2004) J. Mol. Biol , vol.338 , pp. 139-148
    • Ali, T.1    Coles, P.2    Stevens, T.J.3    Stott, K.4    Thomas, J.O.5
  • 46
    • 19444366667 scopus 로고    scopus 로고
    • Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p
    • Sanderson, A., Stott, K., Stevens, T.J. and Thomas, J.O. (2005) Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. J. Mol. Biol., 349, 608-620.
    • (2005) J. Mol. Biol , vol.349 , pp. 608-620
    • Sanderson, A.1    Stott, K.2    Stevens, T.J.3    Thomas, J.O.4
  • 47
    • 0347519278 scopus 로고    scopus 로고
    • The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy
    • Ono, K., Kusano, O., Shimotakahara, S., Shimizu, M., Yamazaki, T. and Shindo, H. (2003) The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. Nucleic Acids Res., 31, 7199-7207.
    • (2003) Nucleic Acids Res , vol.31 , pp. 7199-7207
    • Ono, K.1    Kusano, O.2    Shimotakahara, S.3    Shimizu, M.4    Yamazaki, T.5    Shindo, H.6
  • 48
    • 0028241531 scopus 로고
    • Distinctive DNA conformation with enlarged major groove is found in Zn-finger-DNA and other protein-DNA complexes
    • Nekludova, L. and Pabo, C.O. (1994) Distinctive DNA conformation with enlarged major groove is found in Zn-finger-DNA and other protein-DNA complexes. Proc. Natl Acad. Sci. USA, 91, 6948-6952.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6948-6952
    • Nekludova, L.1    Pabo, C.O.2
  • 49
    • 0028315988 scopus 로고
    • Determinants of repressor/ operator recognition from the structure of the trp operator binding site
    • Shakked, Z., Guzikevich-Guerstein, G., Frolow, F., Rabinovich, D., Joachimiak, A. and Sigler, P.B. (1994) Determinants of repressor/ operator recognition from the structure of the trp operator binding site. Nature, 368, 469-473.
    • (1994) Nature , vol.368 , pp. 469-473
    • Shakked, Z.1    Guzikevich-Guerstein, G.2    Frolow, F.3    Rabinovich, D.4    Joachimiak, A.5    Sigler, P.B.6
  • 50
    • 0024380891 scopus 로고
    • Thymine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin
    • Pehrson, J.R. (1989) Thymine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin. Proc. Natl Acad. Sci. USA, 86, 9149-9153.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9149-9153
    • Pehrson, J.R.1
  • 51
  • 52
    • 0034882165 scopus 로고    scopus 로고
    • Higher-order folding of heterochromatin: Protein bridges span the nucleosome arrays
    • Grigoryev, S.A. (2001) Higher-order folding of heterochromatin: Protein bridges span the nucleosome arrays. Biochem. Cell. Biol., 79 227-241.
    • (2001) Biochem. Cell. Biol , vol.79 , pp. 227-241
    • Grigoryev, S.A.1
  • 54
    • 0024787643 scopus 로고
    • Highly preferential nucleation of histone H1 assembly on scaffold-associated regions
    • Izaurralde, E., Kas, E. and Laemmli, U.K. (1989) Highly preferential nucleation of histone H1 assembly on scaffold-associated regions. J. Mol. Biol., 210, 573-585.
    • (1989) J. Mol. Biol , vol.210 , pp. 573-585
    • Izaurralde, E.1    Kas, E.2    Laemmli, U.K.3
  • 55
    • 0021670305 scopus 로고
    • The transcriptional regulation of Xenopus 5S RNA genes in chromatin: The roles of active stable transcription complexes and histone H1
    • Schlissel, M.S. and Brown, D.D. (1984) The transcriptional regulation of Xenopus 5S RNA genes in chromatin: The roles of active stable transcription complexes and histone H1. Cell, 37, 903-913.
    • (1984) Cell , vol.37 , pp. 903-913
    • Schlissel, M.S.1    Brown, D.D.2
  • 56
    • 0025336095 scopus 로고
    • Flanking sequences of Xenopus 5S RNA genes determine differential inhibition of transcription by H1 histone in vitro
    • Jerzmanowski, A. and Cole, R.D. (1990) Flanking sequences of Xenopus 5S RNA genes determine differential inhibition of transcription by H1 histone in vitro. J. Biol. Chem., 265, 10726-10732.
    • (1990) J. Biol. Chem , vol.265 , pp. 10726-10732
    • Jerzmanowski, A.1    Cole, R.D.2
  • 57
    • 0030791395 scopus 로고    scopus 로고
    • The AT-rich flanks of the oocyte-type 5S RNA gene of Xenopus laevis act as a strong local signal for histone H1-mediated chromatin reorganization in vitro
    • Tomaszewski, R. and Jerzmanowski, A. (1997) The AT-rich flanks of the oocyte-type 5S RNA gene of Xenopus laevis act as a strong local signal for histone H1-mediated chromatin reorganization in vitro. Nucleic Acids Res., 25, 458-465.
    • (1997) Nucleic Acids Res , vol.25 , pp. 458-465
    • Tomaszewski, R.1    Jerzmanowski, A.2
  • 58
    • 0032534222 scopus 로고    scopus 로고
    • Both the 5S rRNA gene and the AT-rich flanks of Xenopus laevis oocyte-type 5S rDNA repeat are required for histone H1-dependent repression of transcription of pol III-type genes in in vitro reconstituted chromatin
    • Tomaszewski, R., Mogielnicka, E. and Jerzmanowski, A. (1998) Both the 5S rRNA gene and the AT-rich flanks of Xenopus laevis oocyte-type 5S rDNA repeat are required for histone H1-dependent repression of transcription of pol III-type genes in in vitro reconstituted chromatin. Nucleic Acids Res., 26, 5596-5601.
    • (1998) Nucleic Acids Res , vol.26 , pp. 5596-5601
    • Tomaszewski, R.1    Mogielnicka, E.2    Jerzmanowski, A.3
  • 59
    • 0013959237 scopus 로고
    • The preferential interactions of polylysine and polyarginine with specific base sequences in DNA
    • Leng, M. and Felsenfeld, G. (1966) The preferential interactions of polylysine and polyarginine with specific base sequences in DNA. Proc. Natl Acad. Sci. USA, 56, 1325-1332.
    • (1966) Proc. Natl Acad. Sci. USA , vol.56 , pp. 1325-1332
    • Leng, M.1    Felsenfeld, G.2
  • 60
    • 0018255280 scopus 로고
    • Studies on the preferential binding of histone H1 to AT-rich DNA
    • Marekov, L.N., Angelov, G. and Beltchev, B. (1978) Studies on the preferential binding of histone H1 to AT-rich DNA. Biochimie, 60, 1347-1349.
    • (1978) Biochimie , vol.60 , pp. 1347-1349
    • Marekov, L.N.1    Angelov, G.2    Beltchev, B.3
  • 61
    • 0024465335 scopus 로고
    • SPKK, a new nucleic acid-binding unit of protein found in histone
    • Suzuki, M. (1989) SPKK, a new nucleic acid-binding unit of protein found in histone. EMBO J., 8, 797-804.
    • (1989) EMBO J , vol.8 , pp. 797-804
    • Suzuki, M.1
  • 62
    • 0024841735 scopus 로고
    • SPKK' motifs prefer to bind to DNA at A/T-rich sites
    • Churchill, M.E.A. and Suzuki, M. (1989) 'SPKK' motifs prefer to bind to DNA at A/T-rich sites. EMBO J., 8, 4189-4195.
    • (1989) EMBO J , vol.8 , pp. 4189-4195
    • Churchill, M.E.A.1    Suzuki, M.2
  • 63
    • 0022446807 scopus 로고
    • Roles of H1 domains in determining higher order chromatin structure and H1 location
    • Allan, J., Mitchell, T., Harborne, N., Bohm, L. and Crane-Robinson, C. (1986) Roles of H1 domains in determining higher order chromatin structure and H1 location. J. Mol. Biol., 187, 591-601.
    • (1986) J. Mol. Biol , vol.187 , pp. 591-601
    • Allan, J.1    Mitchell, T.2    Harborne, N.3    Bohm, L.4    Crane-Robinson, C.5
  • 65
    • 0029589679 scopus 로고
    • 0, H5 and H1M are descendants of invertebrate "orphon" histone H1 genes
    • 0, H5 and H1M are descendants of invertebrate "orphon" histone H1 genes. J. Mol. Evol., 41, 833-840.
    • (1995) J. Mol. Evol , vol.41 , pp. 833-840
    • Schulze, E.1    Schulze, B.2
  • 66
    • 0023429583 scopus 로고
    • Microheterogeneity in H1 histones and its consequences
    • Cole, R.D. (1987) Microheterogeneity in H1 histones and its consequences. Int. J. Peptide Protein Res., 30, 433-449.
    • (1987) Int. J. Peptide Protein Res , vol.30 , pp. 433-449
    • Cole, R.D.1
  • 67
    • 0028696279 scopus 로고
    • 0: A major player in cell differentiation?
    • 0: A major player in cell differentiation? FASEB J., 8, 1260-1268.
    • (1994) FASEB J , vol.8 , pp. 1260-1268
    • Zlatanova, J.1    Doenecke, D.2
  • 68
    • 0021029105 scopus 로고
    • 5-Methylcytosine is localized in nucleosomes that contain histone H1
    • Ball, D.J., Gross, D.S. and Garrard, W.T. (1983) 5-Methylcytosine is localized 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
  • 69
    • 0029964505 scopus 로고    scopus 로고
    • A preference of histone H1 for methylated DNA
    • McArthur, M. and Thomas, J.O. (1996) A preference of histone H1 for methylated DNA. EMBO J., 15, 1705-1714.
    • (1996) EMBO J , vol.15 , pp. 1705-1714
    • McArthur, M.1    Thomas, J.O.2
  • 70
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • Lowary, P.T. and Widom, J. (1998) New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J. Mol. Biol., 276, 19-42.
    • (1998) J. Mol. Biol , vol.276 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 71
    • 0032584136 scopus 로고    scopus 로고
    • Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner
    • An, W., Leuba, S.H., van Holde, K. and Zlatanova, J. (1998) Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner. Proc. Natl Acad. Sci. USA, 95, 3396-3401.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3396-3401
    • An, W.1    Leuba, S.H.2    van Holde, K.3    Zlatanova, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.