메뉴 건너뛰기




Volumn 44, Issue 14, 2005, Pages 5357-5372

Histone release during transcription: Displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress

Author keywords

[No Author keywords available]

Indexed keywords

ACETONE; BIOCHEMISTRY; DNA; ENZYMES; RNA;

EID: 16844366808     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047786o     Document Type: Article
Times cited : (56)

References (91)
  • 1
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents, G., Burlingame, R. W., Wang, B., Love, W. E., and Moudrianakis, E. N. (1991) The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix, Proc. Natl. Acad. Sci. U.S.A. 88, 10148-10152.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.3    Love, W.E.4    Moudrianakis, E.N.5
  • 2
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K. Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution, Nature 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
  • 4
    • 0001074488 scopus 로고
    • Determination of the number of superhelical turns in simian virus 40 DNA by gel electrophoresis
    • Keller, W. (1975) Determination of the number of superhelical turns in simian virus 40 DNA by gel electrophoresis, Proc. Natl. Acad. Sci. U.S.A. 72, 4876-4880.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 4876-4880
    • Keller, W.1
  • 6
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker, P. B., and Horz, W. (2002) ATP-dependent nucleosome remodeling, Annu. Rev. Biochem. 71, 247-274.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 247-274
    • Becker, P.B.1    Horz, W.2
  • 7
    • 0022393483 scopus 로고
    • Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells
    • Jackson, V., and Chalkley, R. (1985) Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells, Biochemistry 24, 6921-6930.
    • (1985) Biochemistry , vol.24 , pp. 6921-6930
    • Jackson, V.1    Chalkley, R.2
  • 8
    • 0025134076 scopus 로고
    • In vivo studies on the dynamics of histone-DNA interaction: Evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both
    • Jackson, V. (1990) In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both. Biochemistry 29, 719-731.
    • (1990) Biochemistry , vol.29 , pp. 719-731
    • Jackson, V.1
  • 9
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura, H., and Cook, P. R. (2001) Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B, J. Cell Biol. 153, 1341-1353.
    • (2001) J. Cell Biol. , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 10
    • 0019001211 scopus 로고
    • Reversible association of calf thymus histones to form the symmetrical octamer (H2AH2BH3H4)2: A case of a mixed-associating system
    • Godfrey, J. E., Eickbush, T. H., and Moudrianakis, E. N. (1980) Reversible association of calf thymus histones to form the symmetrical octamer (H2AH2BH3H4)2: a case of a mixed-associating system, Biochemistry 19, 1339-1346.
    • (1980) Biochemistry , vol.19 , pp. 1339-1346
    • Godfrey, J.E.1    Eickbush, T.H.2    Moudrianakis, E.N.3
  • 11
    • 0025836653 scopus 로고
    • Nucleosome positioning is determined by the (H3-H4)2 tetramer
    • Dong, F., and van Holde, K. E. (1991) Nucleosome positioning is determined by the (H3-H4)2 tetramer, Proc. Natl. Acad. Sci. U.S.A. 88, 10596-10600.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10596-10600
    • Dong, F.1    Van Holde, K.E.2
  • 12
    • 0026010309 scopus 로고
    • Histone contributions to the structure of DNA in the nucleosome
    • Hayes, J. J., Clark, D. J., and Wolffe, A. P. (1991) Histone contributions to the structure of DNA in the nucleosome, Proc. Natl. Acad. Sci. U.S.A. 88, 6829-6833.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 6829-6833
    • Hayes, J.J.1    Clark, D.J.2    Wolffe, A.P.3
  • 13
    • 0028284413 scopus 로고
    • The rapid transfer and selective association of histones H2A and H2B onto negatively coiled DNA at physiological ionic strength
    • Brooks, W., and Jackson, V. (1994) The rapid transfer and selective association of histones H2A and H2B onto negatively coiled DNA at physiological ionic strength, J. Biol. Chem. 269, 18155-18166.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18155-18166
    • Brooks, W.1    Jackson, V.2
  • 14
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983) Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei, Nucleic Acids Res. 11, 1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 15
    • 0026713778 scopus 로고
    • What happens to nucleosomes during transcription?
    • van Holde, K. E., Lohr, D. E., and Robert, C. (1992) What happens to nucleosomes during transcription?, J. Biol. Chem. 267, 2837-2840.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2837-2840
    • Van Holde, K.E.1    Lohr, D.E.2    Robert, C.3
  • 16
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • Liu, L. F., and Wang, J. C. (1987) Supercoiling of the DNA template during transcription, Proc. Natl. Acad. Sci. U.S.A. 84, 7024-7027.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 17
    • 0024279845 scopus 로고
    • Transcription generates positively and negatively supercoiled domains in the template
    • Wu, H. Y., Shyy, S., Wang, J. C., and Liu, L. F. (1988) Transcription generates positively and negatively supercoiled domains in the template, Cell 53, 433-440.
    • (1988) Cell , vol.53 , pp. 433-440
    • Wu, H.Y.1    Shyy, S.2    Wang, J.C.3    Liu, L.F.4
  • 18
    • 0024299511 scopus 로고
    • Transcription-dependent DNA supercoiling in Yeast DNA topoisomerase mutants
    • Brill, S. J., and Sternglanz, R. (1988) Transcription-dependent DNA supercoiling in Yeast DNA topoisomerase mutants, Cell 54, 403-411.
    • (1988) Cell , vol.54 , pp. 403-411
    • Brill, S.J.1    Sternglanz, R.2
  • 19
    • 0023790970 scopus 로고
    • Supercoiling of intracellular DNA can occur in eukaryotic cells
    • Giaever, G. N., and Wang, J. C. (1988) Supercoiling of intracellular DNA can occur in eukaryotic cells, Cell 55, 849-856.
    • (1988) Cell , vol.55 , pp. 849-856
    • Giaever, G.N.1    Wang, J.C.2
  • 20
    • 0024968110 scopus 로고
    • Transcription-driven supercoiling of DNA: Direct biochemical evidence from in ultra studies
    • Tsao, Y. P., Wu, H. Y., and Liu, L. F. (1989) Transcription-driven supercoiling of DNA: Direct biochemical evidence from in ultra studies Cell 56, 111-118.
    • (1989) Cell , vol.56 , pp. 111-118
    • Tsao, Y.P.1    Wu, H.Y.2    Liu, L.F.3
  • 21
    • 0024563782 scopus 로고
    • Formation of supercoiling domains in plasmid pBR322
    • Lodge, J. K., Kazic, T., and Berg, D. E. (1989) Formation of supercoiling domains in plasmid pBR322, J. Bacteriol. 171, 2181-2187.
    • (1989) J. Bacteriol. , vol.171 , pp. 2181-2187
    • Lodge, J.K.1    Kazic, T.2    Berg, D.E.3
  • 22
    • 0026502006 scopus 로고
    • Direct evidence for the effect of transcription on local DNA supercoiling in vivo
    • Rahmouni, A. R., and Wells, R. D. (1992) Direct evidence for the effect of transcription on local DNA supercoiling in vivo, J. Mol. Biol. 223, 131-144.
    • (1992) J. Mol. Biol. , vol.223 , pp. 131-144
    • Rahmouni, A.R.1    Wells, R.D.2
  • 23
    • 0026442269 scopus 로고
    • Dynamics of DNA supercoiling by transcription in Escherichia coli
    • Cook, D. N., Ma, D., Pon, N. G., and Hearst, J. E. (1992) Dynamics of DNA supercoiling by transcription in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 89, 10603-10607.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10603-10607
    • Cook, D.N.1    Ma, D.2    Pon, N.G.3    Hearst, J.E.4
  • 24
    • 0027530935 scopus 로고
    • Transcription-driven site-specific DNA recombination in vitro
    • Droge, P. (1993) Transcription-driven site-specific DNA recombination in vitro, Proc. Natl. Acad. Sci. U.S.A. 90, 2759-2763.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2759-2763
    • Droge, P.1
  • 25
    • 0030901608 scopus 로고    scopus 로고
    • Measurement of unrestrained negative supercoiling and topological domain size in living human cells
    • Kramer, P. R., and Sinden, R. R. (1997) Measurement of unrestrained negative supercoiling and topological domain size in living human cells, Biochemistry 36, 3151-3158.
    • (1997) Biochemistry , vol.36 , pp. 3151-3158
    • Kramer, P.R.1    Sinden, R.R.2
  • 26
    • 0035804245 scopus 로고    scopus 로고
    • Direct observation of DNA rotation during transcription by Escherichia coli RNA polymerase
    • Harada, Y., Ohara, O., Takatsuki, A., Itoh, H., Shimamoto, N., and Kinosita, K. (2001) Direct observation of DNA rotation during transcription by Escherichia coli RNA polymerase, Nature 409, 113-115.
    • (2001) Nature , vol.409 , pp. 113-115
    • Harada, Y.1    Ohara, O.2    Takatsuki, A.3    Itoh, H.4    Shimamoto, N.5    Kinosita, K.6
  • 27
    • 7544242666 scopus 로고    scopus 로고
    • The dynamic response of upstream DNA to transcription-generated torsional stress
    • Kouzine, F., Liu, J., Sanford, S., Chung, H., and Levens, D. (2004) The dynamic response of upstream DNA to transcription-generated torsional stress, Nat. Struct. Biol. 11, 1092-1100.
    • (2004) Nat. Struct. Biol. , vol.11 , pp. 1092-1100
    • Kouzine, F.1    Liu, J.2    Sanford, S.3    Chung, H.4    Levens, D.5
  • 28
    • 0025075435 scopus 로고
    • Studies on rates of nucleosome formation with DNA under stress
    • Pfaffle, P., and Jackson, V. (1990) Studies on rates of nucleosome formation with DNA under stress. J. Biol. Chem. 265, 16821-16829.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16821-16829
    • Pfaffle, P.1    Jackson, V.2
  • 29
    • 0025939524 scopus 로고
    • Positive DNA supercoiling generates a chromatin conformation characteristic of highly active genes
    • Lee, M.-S., and Garrard, W. T. (1991) Positive DNA supercoiling generates a chromatin conformation characteristic of highly active genes, Proc. Natl. Acad. Sci. U.S.A. 88, 9675-9679.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9675-9679
    • Lee, M.-S.1    Garrard, W.T.2
  • 30
    • 0015222656 scopus 로고
    • Interaction between DNA and an Escherichia coli protein ω
    • Wang, J. C. (1971) Interaction between DNA and an Escherichia coli protein ω, J. Mol. Biol. 55, 523-533.
    • (1971) J. Mol. Biol. , vol.55 , pp. 523-533
    • Wang, J.C.1
  • 31
    • 0021930945 scopus 로고
    • Bacterial DNA topoisomerase I can relax positively supercoiled DNA containing a single-stranded loop
    • Kirkegaard, K., and Wang, J. C. (1985) Bacterial DNA topoisomerase I can relax positively supercoiled DNA containing a single-stranded loop, J. Mol. Biol. 185, 625-637.
    • (1985) J. Mol. Biol. , vol.185 , pp. 625-637
    • Kirkegaard, K.1    Wang, J.C.2
  • 32
    • 0039765281 scopus 로고    scopus 로고
    • In vitro studies on the maintenance of transcription-induced stress by histones and polyamines
    • Peng, H. F., and Jackson, V. (2000) In vitro studies on the maintenance of transcription-induced stress by histones and polyamines, J. Biol. Chem. 275, 657-668.
    • (2000) J. Biol. Chem. , vol.275 , pp. 657-668
    • Peng, H.F.1    Jackson, V.2
  • 33
    • 1542267778 scopus 로고    scopus 로고
    • Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome
    • Levchenko, V., and Jackson, V. (2004) Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome, Biochemistry 43, 2359-2372.
    • (2004) Biochemistry , vol.43 , pp. 2359-2372
    • Levchenko, V.1    Jackson, V.2
  • 34
    • 0018435056 scopus 로고
    • A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite
    • Simon, R. H., and Felsenfeld, G. (1979) A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite, Nucleic Acids Res. 6, 689-696.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 689-696
    • Simon, R.H.1    Felsenfeld, G.2
  • 35
    • 0017795309 scopus 로고
    • Resolution of histones by polyacrylamide gel electrophoresis in the presence of nonionic detergents
    • Zweidler, A. (1978) Resolution of histones by polyacrylamide gel electrophoresis in the presence of nonionic detergents, Methods Cell Biol. 17, 223-233.
    • (1978) Methods Cell Biol. , vol.17 , pp. 223-233
    • Zweidler, A.1
  • 36
    • 0018676876 scopus 로고
    • Isolation and characterization of the histone variants in chicken erythrocytes
    • Urban, M. K., Franklin, S. G., and Zweidler, A. (1979) Isolation and characterization of the histone variants in chicken erythrocytes, Biochemistry 18, 3952-3960.
    • (1979) Biochemistry , vol.18 , pp. 3952-3960
    • Urban, M.K.1    Franklin, S.G.2    Zweidler, A.3
  • 37
    • 0001498255 scopus 로고
    • Eukaryotic DNA topoisomerases: Two forms of type I DNA topoisomerases from HeLa cell nuclei
    • Liu, L., and Miller, K. G. (1981) Eukaryotic DNA topoisomerases: two forms of type I DNA topoisomerases from HeLa cell nuclei, Proc. Natl. Acad. Sci. U.S.A. 78, 3487-3491.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 3487-3491
    • Liu, L.1    Miller, K.G.2
  • 38
    • 0024814206 scopus 로고
    • Peptide sequencing and site-directed mutagenesis identify tyrosine-319 as the active site tyrosine of Escherichia coli DNA topoisomerase I
    • Lynn, R. M., and Wang, J. C. (1989) Peptide sequencing and site-directed mutagenesis identify tyrosine-319 as the active site tyrosine of Escherichia coli DNA topoisomerase I, Proteins: Struct., Funct., Genet. 6, 231-239.
    • (1989) Proteins: Struct., Funct., Genet. , vol.6 , pp. 231-239
    • Lynn, R.M.1    Wang, J.C.2
  • 39
    • 0025091721 scopus 로고
    • In vitro evidence that transcription-induced stress causes nucleosome dissolution and regeneration
    • Pfaffle, P., Gerlach, V., Bunzel, L., and Jackson, V. (1990) In vitro evidence that transcription-induced stress causes nucleosome dissolution and regeneration, J. Biol. Chem. 265, 16830-16840.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16830-16840
    • Pfaffle, P.1    Gerlach, V.2    Bunzel, L.3    Jackson, V.4
  • 40
    • 0022493193 scopus 로고
    • Transcription by T7 RNA polymerase is not zinc-dependent and is abolished on amidomethylation of cysteine-347
    • King, G. C., Martin, C. T., Pham, T. T., and Coleman, J. E. (1986) Transcription by T7 RNA polymerase is not zinc-dependent and is abolished on amidomethylation of cysteine-347, Biochemistry 25, 36-40.
    • (1986) Biochemistry , vol.25 , pp. 36-40
    • King, G.C.1    Martin, C.T.2    Pham, T.T.3    Coleman, J.E.4
  • 41
    • 0026656374 scopus 로고
    • Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity
    • Fujii-Nakata, T., Ishimi, Y., Okuda, A., and Kikuchi, A. (1992) Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity, J. Biol. Chem. 267, 20980-20986.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20980-20986
    • Fujii-Nakata, T.1    Ishimi, Y.2    Okuda, A.3    Kikuchi, A.4
  • 42
    • 0000744136 scopus 로고
    • Conformational fluctuations of DNA helix
    • Depew, R. E., and Wang, J. C. (1975) Conformational fluctuations of DNA helix, Proc. Natl. Acad. Sci. U.S.A. 72, 4275-4279.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 4275-4279
    • Depew, R.E.1    Wang, J.C.2
  • 43
    • 0017835311 scopus 로고
    • Supercoiling in closed circular DNA: Dependence upon ion type and concentration
    • Anderson, P., and Bauer, W. (1978) Supercoiling in closed circular DNA: dependence upon ion type and concentration, Biochemistry 17, 594-601.
    • (1978) Biochemistry , vol.17 , pp. 594-601
    • Anderson, P.1    Bauer, W.2
  • 44
    • 0029162295 scopus 로고
    • Preferential binding of histones H3 and H4 to highly positively coiled DNA
    • Jackson, V. (1995) Preferential binding of histones H3 and H4 to highly positively coiled DNA, Biochemistry 34, 10607-10619.
    • (1995) Biochemistry , vol.34 , pp. 10607-10619
    • Jackson, V.1
  • 45
    • 0027319432 scopus 로고
    • Histone octamer dissociation is not required for transcript elongation through arrays of nucleosome cores by phage T7 RNA polymerase in vitro
    • O'Neill, T. E., Smith, J. G., and Bradbury, E. M. (1993) Histone octamer dissociation is not required for transcript elongation through arrays of nucleosome cores by phage T7 RNA polymerase in vitro, Proc. Natl. Acad. Sci. U.S.A. 90, 6203-6207.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6203-6207
    • O'Neill, T.E.1    Smith, J.G.2    Bradbury, E.M.3
  • 46
    • 0018363156 scopus 로고
    • DNA folding by histones: The kinetics of chromatin core particle reassembly and the interaction of nucleosomes with histones
    • Stein, A. (1979) DNA folding by histones: The kinetics of chromatin core particle reassembly and the interaction of nucleosomes with histones, J. Mol. Biol. 130, 103-134.
    • (1979) J. Mol. Biol. , vol.130 , pp. 103-134
    • Stein, A.1
  • 47
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: A model system for study of higher order structure
    • Simpson, R. T., Thoma, F., and Brubaker, J. M. (1985) Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: a model system for study of higher order structure, Cell 42, 799-808.
    • (1985) Cell , vol.42 , pp. 799-808
    • Simpson, R.T.1    Thoma, F.2    Brubaker, J.M.3
  • 48
    • 0028199928 scopus 로고
    • Dynamics of the interactions of histones H2A, H2B and H3, H4 with torsionally stressed DNA
    • Jackson, S., Brooks, W., and Jackson, V. (1994) Dynamics of the interactions of histones H2A, H2B and H3, H4 with torsionally stressed DNA, Biochemistry 33, 5392-5403.
    • (1994) Biochemistry , vol.33 , pp. 5392-5403
    • Jackson, S.1    Brooks, W.2    Jackson, V.3
  • 49
  • 50
    • 0032502688 scopus 로고    scopus 로고
    • 2 tetramer within a nucleoprotein particle requires a reorientation of the H3-H3 interface
    • 2 tetramer within a nucleoprotein particle requires a reorientation of the H3-H3 interface, J. Biol. Chem. 273, 9261-9269.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9261-9269
    • Hamiche, A.1    Richard-Foy, H.2
  • 51
    • 0032496272 scopus 로고    scopus 로고
    • Folding of chromatin in the presence of heterogeneous histone H1 binding to nucleosomes
    • Howe, L., Iskandar, M., and Ausio, J. (1998) Folding of chromatin in the presence of heterogeneous histone H1 binding to nucleosomes, J. Biol. Chem. 273, 11625-11629.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11625-11629
    • Howe, L.1    Iskandar, M.2    Ausio, J.3
  • 52
    • 0033067219 scopus 로고    scopus 로고
    • Assembly of defined nucleosomal and chromatin arrays from pure components
    • Caruthers, L. M., Tse, C., Walker, K. P., and Hansen, J. C., (1999) Assembly of defined nucleosomal and chromatin arrays from pure components, Methods Enzymol. 304, 19-35.
    • (1999) Methods Enzymol. , vol.304 , pp. 19-35
    • Caruthers, L.M.1    Tse, C.2    Walker, K.P.3    Hansen, J.C.4
  • 53
    • 0023105676 scopus 로고
    • Binding mode of nucleosome-assembly protein (AP-1) and histones
    • Ishmi, Y., Kojima, M., Yamada, M., and Hanaoka, F. (1987) Binding mode of nucleosome-assembly protein (AP-1) and histones, Eur. J. Biochem. 162, 19-24.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 19-24
    • Ishmi, Y.1    Kojima, M.2    Yamada, M.3    Hanaoka, F.4
  • 55
    • 0028363760 scopus 로고
    • Formation and stability of higher order chromatin structures. Contributions of the histone octamer
    • Schwarz, P. M., and Hansen, J. C. (1994) Formation and stability of higher order chromatin structures. Contributions of the histone octamer, J. Biol. Chem. 269, 16284-16289.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16284-16289
    • Schwarz, P.M.1    Hansen, J.C.2
  • 56
    • 0025318655 scopus 로고
    • Transcription factor requirements for in vitro formation of transcriptionally competent 5S rRNA gene chromatin
    • Felts, S. J., Weil, P. A., and Chalkley, R. (1990) Transcription factor requirements for in vitro formation of transcriptionally competent 5S rRNA gene chromatin, Mol. Cell. Biol. 10, 2390-2401.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2390-2401
    • Felts, S.J.1    Weil, P.A.2    Chalkley, R.3
  • 57
    • 0030768938 scopus 로고    scopus 로고
    • The H3/H4 tetramer blocks transcript elongation by RNA Polymerase II in vitro
    • Chang, C.-H., and Luse, D. S. (1997) The H3/H4 tetramer blocks transcript elongation by RNA Polymerase II in vitro, J. Biol. Chem. 272, 23427-23434.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23427-23434
    • Chang, C.-H.1    Luse, D.S.2
  • 58
    • 0026512523 scopus 로고
    • Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase
    • O'Neill, T. E., Roberge, M., and Bradbury, E. M. (1992) Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase, J. Mol. Biol. 223, 67-78.
    • (1992) J. Mol. Biol. , vol.223 , pp. 67-78
    • O'Neill, T.E.1    Roberge, M.2    Bradbury, E.M.3
  • 59
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication- independent nucleosome assembly
    • Ahmad, K., and Henikoff, S. (2002) The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly, Mol. Cell 9, 1191-1200.
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 60
    • 0026733468 scopus 로고
    • A nucleosome core is transferred out of the path of a transcribing polymerase
    • Clark, D. J., and Felsenfeld, G. (1992) A nucleosome core is transferred out of the path of a transcribing polymerase, Cell 71, 11-22.
    • (1992) Cell , vol.71 , pp. 11-22
    • Clark, D.J.1    Felsenfeld, G.2
  • 61
    • 0028125847 scopus 로고
    • A histone octamer can step around a transcribing polymerase without leaving the template
    • Studitsky, V. M., Clark, D. J., and Felsenfeld, G. (1994) A histone octamer can step around a transcribing polymerase without leaving the template, Cell 76, 371-382.
    • (1994) Cell , vol.76 , pp. 371-382
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 62
    • 0028850059 scopus 로고
    • Overcoming a nucleosomal barrier to transcription
    • Studitsky, V. M., Clark, D. J., and Felsenfeld, G. (1995) Overcoming a nucleosomal barrier to transcription, Cell 83, 19-27.
    • (1995) Cell , vol.83 , pp. 19-27
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 63
    • 0031451329 scopus 로고    scopus 로고
    • Mechanism of transcription through the nucleosome by eukaryotic RNA Polymerase
    • Studitsky, V. M., Kassavetis, G. A., Geiduschek, E. P., and Felsenfeld, G. (1997) Mechanism of transcription through the nucleosome by eukaryotic RNA Polymerase, Science 278, 1960-1963.
    • (1997) Science , vol.278 , pp. 1960-1963
    • Studitsky, V.M.1    Kassavetis, G.A.2    Geiduschek, E.P.3    Felsenfeld, G.4
  • 64
    • 0023663417 scopus 로고
    • Nucleosomes inhibit the initiation of transcription but allow chain elongation with displacement of histones
    • Lorch, Y., LaPointe, J. W., and Kornberg, R. D. (1987) Nucleosomes inhibit the initiation of transcription but allow chain elongation with displacement of histones, Cell 49, 203-210.
    • (1987) Cell , vol.49 , pp. 203-210
    • Lorch, Y.1    LaPointe, J.W.2    Kornberg, R.D.3
  • 65
    • 0028279576 scopus 로고
    • Octamer displacement and redistribution in transcription of single nucleosomes
    • O'Donahue, M.-F., Duband-Goulet, I., Hamiche, A., and Prunell, A. (1994) Octamer displacement and redistribution in transcription of single nucleosomes, Nucleic Acids Res. 22, 937-945.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 937-945
    • O'Donahue, M.-F.1    Duband-Goulet, I.2    Hamiche, A.3    Prunell, A.4
  • 66
    • 0029008063 scopus 로고
    • Mechanism of Nucleosome Dissociation Produced by Transcription Elongation in a Short Chromatin Template
    • Gallego, F., Fernandez-Busquets, X., and Daban, J.-R. (1995) Mechanism of Nucleosome Dissociation Produced by Transcription Elongation in a Short Chromatin Template, Biochemistry 34, 6711-6719.
    • (1995) Biochemistry , vol.34 , pp. 6711-6719
    • Gallego, F.1    Fernandez-Busquets, X.2    Daban, J.-R.3
  • 67
    • 0019888448 scopus 로고
    • The sites of deposition of newly synthesized histone
    • Jackson, V., Marshall, S., and Chalkley, R. (1981) The sites of deposition of newly synthesized histone, Nucleic Acids Res. 9, 4563-4581.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 4563-4581
    • Jackson, V.1    Marshall, S.2    Chalkley, R.3
  • 68
    • 0027507943 scopus 로고
    • Disruption of the nucleosomes at the replication fork
    • Gruss, C., Wu, J., Koller, T., and Sogo, J. M. (1993) Disruption of the nucleosomes at the replication fork, EMBO J. 12, 4563-4545.
    • (1993) EMBO J. , vol.12 , pp. 4563-14545
    • Gruss, C.1    Wu, J.2    Koller, T.3    Sogo, J.M.4
  • 69
    • 0029011919 scopus 로고
    • The p150 and p60 subunits of chromatin assembly factor 1: A molecular link between newly synthesized histones and DNA replication
    • Kaufman, P. D., Kobayashi, R., Kessler, N., and Stillman, B. (1995) The p150 and p60 subunits of chromatin assembly factor 1: A molecular link between newly synthesized histones and DNA replication, Cell 81, 1105-1114.
    • (1995) Cell , vol.81 , pp. 1105-1114
    • Kaufman, P.D.1    Kobayashi, R.2    Kessler, N.3    Stillman, B.4
  • 70
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D., and Allis, C. D. (2000) The language of covalent histone modifications, Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 71
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner, B. M. (2002) Cellular memory and the histone code, Cell 111, 285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 72
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription
    • Kireeva, M. L., Walter, W., Tchernakjenko, V., Bondarenko, V., Kashlev, M., and Studitsky, V. M. (2002) Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription, Mol. Cell 9, 541-552.
    • (2002) Mol. Cell , vol.9 , pp. 541-552
    • Kireeva, M.L.1    Walter, W.2    Tchernakjenko, V.3    Bondarenko, V.4    Kashlev, M.5    Studitsky, V.M.6
  • 73
    • 0020660260 scopus 로고
    • Eukaryotic RNA polymerase II binds to nucleosome cores from transcribed genes
    • Baer, R. W., and Rhodes, D. (1983) Eukaryotic RNA polymerase II binds to nucleosome cores from transcribed genes, Nature 301, 482-488.
    • (1983) Nature , vol.301 , pp. 482-488
    • Baer, R.W.1    Rhodes, D.2
  • 74
    • 0032808150 scopus 로고    scopus 로고
    • Quantitation of RNA polymerase II and its transcription factors in an HeLa cell: Little soluble holoenzyme but significant amounts of polymerases attached to the nuclear substructure
    • Kimura, H., Tao, Y., Roeder, R. G., and Cook, P. R. (1999) Quantitation of RNA polymerase II and its transcription factors in an HeLa cell: little soluble holoenzyme but significant amounts of polymerases attached to the nuclear substructure, Mol. Cell. Biol. 19, 5383-5392.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5383-5392
    • Kimura, H.1    Tao, Y.2    Roeder, R.G.3    Cook, P.R.4
  • 76
    • 0020816370 scopus 로고
    • A protein which facilitates assembly of nucleosome-like structures in vitro in mammalian cells
    • Ishimi, Y., Yasuda, H., Hirosumi, J., Hanaoka, F. and Yamada, M. (1983) A protein which facilitates assembly of nucleosome-like structures in vitro in mammalian cells. J. Biochem. 94, 735-744.
    • (1983) J. Biochem. , vol.94 , pp. 735-744
    • Ishimi, Y.1    Yasuda, H.2    Hirosumi, J.3    Hanaoka, F.4    Yamada, M.5
  • 77
    • 12544258222 scopus 로고    scopus 로고
    • Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
    • Park, Y.-J., Chodaparambil, V., Bao, Y., McBryant, S. J., and Luger, K. (2005) Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding, J. Biol. Chem. 280, 1817-1825.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1817-1825
    • Park, Y.-J.1    Chodaparambil, V.2    Bao, Y.3    McBryant, S.J.4    Luger, K.5
  • 78
    • 0038054272 scopus 로고    scopus 로고
    • Genome-wide expression analysis of NAP1 in Saccharomyces cerevisiae
    • Ohkuni, K., Shirahige, K., and Kikuchi, A. (2003) Genome-wide expression analysis of NAP1 in Saccharomyces cerevisiae, Biochem. Biophys. Res. Commun. 306, 5-9.
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 5-9
    • Ohkuni, K.1    Shirahige, K.2    Kikuchi, A.3
  • 79
    • 0032513211 scopus 로고    scopus 로고
    • Assembly, remodeling, and histone binding capabilities of yeast nucleosome assembly protein 1
    • McQuibban, G. A., Commisso-Cappelli, C. N., and Lewis, P. N. (1998) Assembly, remodeling, and histone binding capabilities of yeast nucleosome assembly protein 1, J. Biol. Chem. 273, 6582-6590.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6582-6590
    • McQuibban, G.A.1    Commisso-Cappelli, C.N.2    Lewis, P.N.3
  • 80
    • 0031026487 scopus 로고    scopus 로고
    • Histones in transit: Cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells
    • Chang, L., Loranger, S. S., Mizzen, C., Ernst, S. G., Allis, C. D., and Annunziato, A. T. (1997) Histones in transit: cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells, Biochemistry 36, 469-480.
    • (1997) Biochemistry , vol.36 , pp. 469-480
    • Chang, L.1    Loranger, S.S.2    Mizzen, C.3    Ernst, S.G.4    Allis, C.D.5    Annunziato, A.T.6
  • 81
    • 0037011167 scopus 로고    scopus 로고
    • A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B
    • Mosammaparast, N., Ewart, C. S., and Pemberton, L. F. (2002) A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B, EMBO J. 23, 6527-6538.
    • (2002) EMBO J. , vol.23 , pp. 6527-6538
    • Mosammaparast, N.1    Ewart, C.S.2    Pemberton, L.F.3
  • 82
    • 0036236469 scopus 로고    scopus 로고
    • Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro
    • Asahara, H., Tartae-Deckert, S., Nakagawa, T., Ikehara, T., Hirose, F., Hunter, T., Ito, T, and Montminy, M. (2002) Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro, Mol. Cell. Biol. 22, 2974-2983.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2974-2983
    • Asahara, H.1    Tartae-Deckert, S.2    Nakagawa, T.3    Ikehara, T.4    Hirose, F.5    Hunter, T.6    Ito, T.7    Montminy, M.8
  • 83
    • 0033898468 scopus 로고    scopus 로고
    • p300-Mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone
    • Ito, T., Ikehara, T., Nakagawa, T., Kraus, W. L., and Muramatsu, M. (2000) p300-Mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone, Genes Dev. 14, 1899-1907.
    • (2000) Genes Dev. , vol.14 , pp. 1899-1907
    • Ito, T.1    Ikehara, T.2    Nakagawa, T.3    Kraus, W.L.4    Muramatsu, M.5
  • 84
    • 0028799432 scopus 로고
    • Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer
    • Walter, P. P., Owen-Hughes, T. A., Cote, J., and Workman, J. L. (1995) Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer, Mol. Cell. Biol. 15, 6178-6187.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6178-6187
    • Walter, P.P.1    Owen-Hughes, T.A.2    Cote, J.3    Workman, J.L.4
  • 85
    • 0347539781 scopus 로고    scopus 로고
    • Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities
    • Bruno, M., Flaus, A., Stockdale, C., Rencurel, C., Ferreira, H., and Owen-Hughes, T. (2003) Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities, Mol. Cell 12, 1599-1606.
    • (2003) Mol. Cell , vol.12 , pp. 1599-1606
    • Bruno, M.1    Flaus, A.2    Stockdale, C.3    Rencurel, C.4    Ferreira, H.5    Owen-Hughes, T.6
  • 86
    • 1942439629 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodeling: Farewell to the tuna-can octamer?
    • Flaus, A., and Owen-Hughes, T. (2004) Mechanisms for ATP-dependent chromatin remodeling: farewell to the tuna-can octamer? Current Opinion in Genetics and Development 14, 165-173.
    • (2004) Current Opinion in Genetics and Development , vol.14 , pp. 165-173
    • Flaus, A.1    Owen-Hughes, T.2
  • 87
    • 0032498273 scopus 로고    scopus 로고
    • FACT, a factor that facilitates transcript elongation through nucleosomes
    • Orphanides, G., LeRoy, G., Chang, C. H., Luse, D. S., and Reinberg, D. (1998) FACT, a factor that facilitates transcript elongation through nucleosomes, Cell 92, 105-116.
    • (1998) Cell , vol.92 , pp. 105-116
    • Orphanides, G.1    Leroy, G.2    Chang, C.H.3    Luse, D.S.4    Reinberg, D.5
  • 89
    • 0033566129 scopus 로고    scopus 로고
    • The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins
    • Orphanides, G., Wu, W. H., Lane, W. S., Hampsey, M., and Reinberg, D. (1999) The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins, Nature 400, 284-288.
    • (1999) Nature , vol.400 , pp. 284-288
    • Orphanides, G.1    Wu, W.H.2    Lane, W.S.3    Hampsey, M.4    Reinberg, D.5
  • 91
    • 0033593241 scopus 로고    scopus 로고
    • Nucleosome Dynamics. III. Histone tail-dependent fluctuation of nucleosomes between open and closed DNA conformations. Implications for chromatin dynamics and the linking number paradox. A relaxation study of mononucleosomes on DNA Minicircles
    • De Lucia, P., Alilat, M., Sivolob, A., and Prunell, A. (1999) Nucleosome Dynamics. III. Histone tail-dependent fluctuation of nucleosomes between open and closed DNA conformations. Implications for chromatin dynamics and the linking number paradox. A relaxation study of mononucleosomes on DNA Minicircles, J. Mol. Biol. 285, 1101-1119.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1101-1119
    • De Lucia, P.1    Alilat, M.2    Sivolob, A.3    Prunell, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.