메뉴 건너뛰기




Volumn 23, Issue 23, 2003, Pages 8626-8636

The Dynamic Mobility of Histone H1 Is Regulated by Cyclin/CDK Phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CYCLIN A; CYCLIN DEPENDENT KINASE 2; CYCLIN E; GREEN FLUORESCENT PROTEIN; HISTONE H1; HYBRID PROTEIN; PROTEIN P21; SERINE; THREONINE;

EID: 0242721659     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.23.8626-8636.2003     Document Type: Article
Times cited : (139)

References (51)
  • 1
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin
    • Bednar, J., R. A. Horowitz, S. A. Grigoryev, L. M. Carruthers, J. C. Hansen, A. J. Koster, and C. L. Woodcock. 1998. Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Proc. Natl. Acad. Sci. USA 95:14173-14178.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14173-14178
    • Bednar, J.1    Horowitz, R.A.2    Grigoryev, S.A.3    Carruthers, L.M.4    Hansen, J.C.5    Koster, A.J.6    Woodcock, C.L.7
  • 2
    • 0035371920 scopus 로고    scopus 로고
    • Visualizing chromosome dynamics with GFP
    • Belmont, A. S. 2001. Visualizing chromosome dynamics with GFP. Trends Cell Biol. 11:250-257.
    • (2001) Trends Cell Biol. , vol.11 , pp. 250-257
    • Belmont, A.S.1
  • 3
    • 0034935019 scopus 로고    scopus 로고
    • Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling
    • Bhattacharjee, R. N., G. C. Banks, K. W. Trotter, H. L. Lee, and T. K. Archer. 2001. Histone H1 phosphorylation by Cdk2 selectively modulates mouse mammary tumor virus transcription through chromatin remodeling. Mol. Cell. Biol. 21:5417-5425.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5417-5425
    • Bhattacharjee, R.N.1    Banks, G.C.2    Trotter, K.W.3    Lee, H.L.4    Archer, T.K.5
  • 4
    • 0034090341 scopus 로고    scopus 로고
    • Immunofluorescent studies of human chromosomes with antibodies against phosphorylated H1 histone
    • Boggs, B. A., C. D. Allis, and A. C. Chinault. 2000. Immunofluorescent studies of human chromosomes with antibodies against phosphorylated H1 histone. Chromosoma 108:485-490.
    • (2000) Chromosoma , vol.108 , pp. 485-490
    • Boggs, B.A.1    Allis, C.D.2    Chinault, A.C.3
  • 5
    • 0036348409 scopus 로고    scopus 로고
    • Chromatin structure and dynamics: State-of-the-art
    • Bradbury, E. M. 2002. Chromatin structure and dynamics: state-of-the-art. Mol. Cell 10:13-19.
    • (2002) Mol. Cell , vol.10 , pp. 13-19
    • Bradbury, E.M.1
  • 6
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury, E. M. 1992. Reversible histone modifications and the chromosome cell cycle. Bioessays 14:9-16.
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 7
    • 0016236883 scopus 로고
    • Control of cell division by very lysine rich histone (F1) phosphorylation
    • Bradbury, E. M., R. J. Inglis, and H. R. Matthews. 1974. Control of cell division by very lysine rich histone (F1) phosphorylation. Nature 247:257-261.
    • (1974) Nature , vol.247 , pp. 257-261
    • Bradbury, E.M.1    Inglis, R.J.2    Matthews, H.R.3
  • 8
    • 0029915879 scopus 로고    scopus 로고
    • Differential effect of H1 variant overexpression on cell cycle progression and gene expression
    • Brown, D. T., B. T. Alexander, and D. B. Sittman. 1996. Differential effect of H1 variant overexpression on cell cycle progression and gene expression. Nucleic Acids Res. 24:486-493.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 486-493
    • Brown, D.T.1    Alexander, B.T.2    Sittman, D.B.3
  • 9
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding
    • Carruthers, L. M., J. Bednar, C. L. Woodcock, and J. C. Hansen. 1998. Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: mechanistic ramifications for higher-order chromatin folding. Biochemistry 37:14776-14787.
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.L.3    Hansen, J.C.4
  • 10
    • 0036668636 scopus 로고    scopus 로고
    • Competition between histone H1 and HMGN proteins for chromatin binding sites
    • Catez, F., D. T. Brown, T. Misteli, and M. Bustin. 2002. Competition between histone H1 and HMGN proteins for chromatin binding sites. EMBO Rep. 3:760-766.
    • (2002) EMBO Rep. , vol.3 , pp. 760-766
    • Catez, F.1    Brown, D.T.2    Misteli, T.3    Bustin, M.4
  • 11
    • 1842329732 scopus 로고    scopus 로고
    • Histone H1b phosphorylation is dependent upon ongoing transcription and replication in normal and ras-transformed mouse fibroblasts
    • Chadee, D. N., C. D. Allis, J. A. Wright, and J. R. Davie. 1997. Histone H1b phosphorylation is dependent upon ongoing transcription and replication in normal and ras-transformed mouse fibroblasts. J. Biol. Chem. 272:8113-8116.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8113-8116
    • Chadee, D.N.1    Allis, C.D.2    Wright, J.A.3    Davie, J.R.4
  • 12
    • 0037028251 scopus 로고    scopus 로고
    • Histone H1(S)-3 phosphorylation in Ha-ras oncogene-transformed mouse fibroblasts
    • Chadee, D. N., C. P. Peltier, and J. R. Davie. 2002. Histone H1(S)-3 phosphorylation in Ha-ras oncogene-transformed mouse fibroblasts. Oncogene 21:8397-8403.
    • (2002) Oncogene , vol.21 , pp. 8397-8403
    • Chadee, D.N.1    Peltier, C.P.2    Davie, J.R.3
  • 13
    • 0029120154 scopus 로고
    • Increased phosphorylation of histone H1 in mouse fibroblasts transformed with oncogenes or constitutively active mitogen-activated protein kinase kinase
    • Chadee, D. N., W. R. Taylor, R. A. Hurta, C. D. Allis, J. A. Wright, and J. R. Davie. 1995. Increased phosphorylation of histone H1 in mouse fibroblasts transformed with oncogenes or constitutively active mitogen-activated protein kinase kinase. J. Biol. Chem. 270:20098-20105.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20098-20105
    • Chadee, D.N.1    Taylor, W.R.2    Hurta, R.A.3    Allis, C.D.4    Wright, J.A.5    Davie, J.R.6
  • 14
    • 0031106457 scopus 로고    scopus 로고
    • Where is the globular domain of linker histone located on the nucleosome?
    • Crane-Robinson, C. 1997. Where is the globular domain of linker histone located on the nucleosome? Trends Biochem. Sci. 22:75-77.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 75-77
    • Crane-Robinson, C.1
  • 15
    • 0027938043 scopus 로고
    • A mutant form of the Ran/TC4 protein disrupts nuclear function in Xenopus laevis egg extracts by inhibiting the RCC1 protein, a regulator of chromosome condensation
    • Dasso, M., T. Seki, Y. Azuma, T. Ohba, and T. Nishimoto. 1994. A mutant form of the Ran/TC4 protein disrupts nuclear function in Xenopus laevis egg extracts by inhibiting the RCC1 protein, a regulator of chromosome condensation. EMBO J. 13:5732-5744.
    • (1994) EMBO J. , vol.13 , pp. 5732-5744
    • Dasso, M.1    Seki, T.2    Azuma, Y.3    Ohba, T.4    Nishimoto, T.5
  • 16
    • 0037144862 scopus 로고    scopus 로고
    • Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin
    • Dou, Y., J. Bowen, Y. Liu, and M. A. Gorovsky. 2002. Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin. J. Cell Biol. 158:1161-1170.
    • (2002) J. Cell Biol. , vol.158 , pp. 1161-1170
    • Dou, Y.1    Bowen, J.2    Liu, Y.3    Gorovsky, M.A.4
  • 17
    • 0033637116 scopus 로고    scopus 로고
    • Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch
    • Dou, Y., and M. A. Gorovsky. 2000. Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch. Mol. Cell 6:225-231.
    • (2000) Mol. Cell , vol.6 , pp. 225-231
    • Dou, Y.1    Gorovsky, M.A.2
  • 18
    • 0033213394 scopus 로고    scopus 로고
    • Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal
    • Dou, Y., C. A. Mizzen, M. Abrams, C. D. Allis, and M. A. Gorovsky. 1999. Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal. Mol. Cell 4:641-647.
    • (1999) Mol. Cell , vol.4 , pp. 641-647
    • Dou, Y.1    Mizzen, C.A.2    Abrams, M.3    Allis, C.D.4    Gorovsky, M.A.5
  • 20
    • 0033621414 scopus 로고    scopus 로고
    • Effects of H1 histone variant overexpression on chromatin structure
    • Gunjan, A., B. T. Alexander, D. B. Sittman, and D. T. Brown. 1999. Effects of H1 histone variant overexpression on chromatin structure. J. Biol. Chem. 274:37950-37956.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37950-37956
    • Gunjan, A.1    Alexander, B.T.2    Sittman, D.B.3    Brown, D.T.4
  • 21
    • 0030000430 scopus 로고    scopus 로고
    • Effects of cell cycle dependent histone H1 phosphorylation on chromatin structure and chromatin replication
    • Halmer, L., and C. Gruss. 1996. Effects of cell cycle dependent histone H1 phosphorylation on chromatin structure and chromatin replication. Nucleic Acids Res. 24:1420-1427.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1420-1427
    • Halmer, L.1    Gruss, C.2
  • 22
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions
    • Hansen, J. C. 2002. Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions. Annu. Rev. Biophys. Biomol. Struct. 31:361-392.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 23
    • 0029909105 scopus 로고    scopus 로고
    • Increased histone H1 phosphorylation and relaxed chromatin structure in Rb-deficient fibroblasts
    • Herrera, R. E., F. Chen, and R. A. Weinberg. 1996. Increased histone H1 phosphorylation and relaxed chromatin structure in Rb-deficient fibroblasts. Proc. Natl. Acad. Sci. USA 93:11510-11515.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11510-11515
    • Herrera, R.E.1    Chen, F.2    Weinberg, R.A.3
  • 25
    • 0032544921 scopus 로고    scopus 로고
    • Development of a bicistronic vector driven by the human polypeptide chain elongation factor 1alpha promoter for creation of stable mammalian cell lines that express very high levels of recombinant proteins
    • Hobbs, S., S. Jitrapakdee, and J. C. Wallace. 1998. Development of a bicistronic vector driven by the human polypeptide chain elongation factor 1alpha promoter for creation of stable mammalian cell lines that express very high levels of recombinant proteins. Biochem. Biophys. Res. Commun. 252:368-372.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 368-372
    • Hobbs, S.1    Jitrapakdee, S.2    Wallace, J.C.3
  • 27
    • 0035106336 scopus 로고    scopus 로고
    • Macromolecular dynamics in living cell nuclei revealed by fluorescence redistribution after photobleaching
    • Houtsmuller, A. B., and W. Vermeulen. 2001. Macromolecular dynamics in living cell nuclei revealed by fluorescence redistribution after photobleaching. Histochem. Cell Biol. 115:13-21.
    • (2001) Histochem. Cell Biol. , vol.115 , pp. 13-21
    • Houtsmuller, A.B.1    Vermeulen, W.2
  • 28
    • 0032496272 scopus 로고    scopus 로고
    • Folding of chromatin in the presence of heterogeneous histone H1 binding to nucleosomes
    • Howe, L., M. Iskandar, and J. Ausio. 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
  • 29
    • 0023066848 scopus 로고
    • H1 histone phosphorylation, cell cycle progression and chromatin structure
    • Langan, T. A., and T. C. Chambers. 1987. H1 histone phosphorylation, cell cycle progression and chromatin structure. Prog. Clin. Biol. Res. 249:215-223.
    • (1987) Prog. Clin. Biol. Res. , vol.249 , pp. 215-223
    • Langan, T.A.1    Chambers, T.C.2
  • 30
    • 0024455114 scopus 로고
    • Mammalian growth-associated H1 histone kinase: A homolog of cdc2+/CDC28 protein kinases controlling mitotic entry in yeast and frog cells
    • Langan, T. A., J. Gautier, M. Lohka, R. Hollingsworth, S. Moreno, P. Nurse, J. Maller, and R. A. Sclafani. 1989. Mammalian growth-associated H1 histone kinase: a homolog of cdc2+/CDC28 protein kinases controlling mitotic entry in yeast and frog cells. Mol. Cell. Biol. 9:3860-3868.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3860-3868
    • Langan, T.A.1    Gautier, J.2    Lohka, M.3    Hollingsworth, R.4    Moreno, S.5    Nurse, P.6    Maller, J.7    Sclafani, R.A.8
  • 31
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever, M. A., J. P. Th'ng, X. Sun, and M. J. Hendzel. 2000. Rapid exchange of histone H1.1 on chromatin in living human cells. Nature 408:873-876.
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 32
    • 0032498902 scopus 로고    scopus 로고
    • Interphase cell cycle dynamics of a late replicating, heterochromatic homogenously staining region: Precise choreography of condensation/decondensation and intranuclear positioning
    • Li, G., G. Sudlow, and A. S. Belmont. 1998. Interphase cell cycle dynamics of a late replicating, heterochromatic homogenously staining region: precise choreography of condensation/decondensation and intranuclear positioning. J. Cell Biol. 140:975-989.
    • (1998) J. Cell Biol. , vol.140 , pp. 975-989
    • Li, G.1    Sudlow, G.2    Belmont, A.S.3
  • 34
    • 0028348459 scopus 로고
    • Generation and characterization of novel antibodies highly selective for phosphorylated linker histone H1 in Tetrahymena and HeLa cells
    • Lu, M. J., C. A. Dadd, C. A. Mizzen, C. A. Perry, D. R. McLachlan, A. T. Annunziato, and C. D. Allis. 1994. Generation and characterization of novel antibodies highly selective for phosphorylated linker histone H1 in Tetrahymena and HeLa cells. Chromosoma 103:111-121.
    • (1994) Chromosoma , vol.103 , pp. 111-121
    • Lu, M.J.1    Dadd, C.A.2    Mizzen, C.A.3    Perry, C.A.4    McLachlan, D.R.5    Annunziato, A.T.6    Allis, C.D.7
  • 35
    • 0029155905 scopus 로고
    • Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei
    • Lu, M. J., S. S. Mpoke, C. A. Dadd, and C. D. Allis. 1995. Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei. Mol. Biol. Cell 6:1077-1087.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1077-1087
    • Lu, M.J.1    Mpoke, S.S.2    Dadd, C.A.3    Allis, C.D.4
  • 36
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli, T., A. Gunjan, R. Hock, M. Bustin, and D. T. Brown. 2000. Dynamic binding of histone H1 to chromatin in living cells. Nature 408:877-881.
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 38
    • 23444445850 scopus 로고
    • Chromosome condensation in Xenopus mitotic extracts without histone H1
    • Ohsumi, K., C. Katagiri, and T. Kishimoto. 1993. Chromosome condensation in Xenopus mitotic extracts without histone H1. Science 262:2033-2035.
    • (1993) Science , vol.262 , pp. 2033-2035
    • Ohsumi, K.1    Katagiri, C.2    Kishimoto, T.3
  • 39
    • 0034881774 scopus 로고    scopus 로고
    • A compendium of the histone H1 family of somatic subtypes: An elusive cast of characters and their characteristics
    • Parseghian, M. H., and B. A. Hamkalo. 2001. A compendium of the histone H1 family of somatic subtypes: an elusive cast of characters and their characteristics. Biochem. Cell Biol. 79:289-304.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 289-304
    • Parseghian, M.H.1    Hamkalo, B.A.2
  • 40
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D., and T. Misteli. 2000. High mobility of proteins in the mammalian cell nucleus. Nature 404:604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 41
    • 0026545414 scopus 로고
    • Chromatin condensation: Does histone H1 dephosphorylation play a role?
    • Roth, S. Y., and C. D. Allis. 1992. Chromatin condensation: does histone H1 dephosphorylation play a role? Trends Biochem. Sci. 17:93-98.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 93-98
    • Roth, S.Y.1    Allis, C.D.2
  • 42
    • 0018780567 scopus 로고
    • H1 histone subfractions of mammalian testes. 1. Organ specificity in the rat
    • Seyedin, S. M., and W. S. Kistler. 1979. H1 histone subfractions of mammalian testes. 1. Organ specificity in the rat. Biochemistry 18:1371-1375.
    • (1979) Biochemistry , vol.18 , pp. 1371-1375
    • Seyedin, S.M.1    Kistler, W.S.2
  • 43
    • 0028988585 scopus 로고
    • Inhibitors of mammalian G1 cyclin-dependent kinases
    • Sherr, C. J., and J. M. Roberts. 1995. Inhibitors of mammalian G1 cyclin-dependent kinases. Genes Dev. 9:1149-1163.
    • (1995) Genes Dev. , vol.9 , pp. 1149-1163
    • Sherr, C.J.1    Roberts, J.M.2
  • 45
    • 0030068951 scopus 로고    scopus 로고
    • In vivo phosphorylation of histone H1 variants during the cell cycle
    • Talasz, H., W. Helliger, B. Puschendorf, and H. Lindner. 1996. In vivo phosphorylation of histone H1 variants during the cell cycle. Biochemistry 35:1761-1767.
    • (1996) Biochemistry , vol.35 , pp. 1761-1767
    • Talasz, H.1    Helliger, W.2    Puschendorf, B.3    Lindner, H.4
  • 46
    • 0033610814 scopus 로고    scopus 로고
    • In vitro binding of Hi histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor
    • Talasz, H., N. Sapojnikova, W. Helliger, H. Lindner, and B. Puschendorf. 1998. In vitro binding of Hi histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor. J. Biol. Chem. 273:32236-32243.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32236-32243
    • Talasz, H.1    Sapojnikova, N.2    Helliger, W.3    Lindner, H.4    Puschendorf, B.5
  • 47
    • 0029615477 scopus 로고
    • Fibroblasts transformed by combinations of ras, myc and mutant p53 exhibit increased phosphorylation of histone H1 that is independent of metastatic potential
    • Taylor, W. R., D. N. Chadee, C. D. Allis, J. A. Wright, and J. R. Davie. 1995. Fibroblasts transformed by combinations of ras, myc and mutant p53 exhibit increased phosphorylation of histone H1 that is independent of metastatic potential. FEBS Lett. 377:51-53.
    • (1995) FEBS Lett. , vol.377 , pp. 51-53
    • Taylor, W.R.1    Chadee, D.N.2    Allis, C.D.3    Wright, J.A.4    Davie, J.R.5
  • 48
    • 0032972980 scopus 로고    scopus 로고
    • The location of the linker histone on the nucleosome
    • Travers, A. 1999. The location of the linker histone on the nucleosome. Trends Biochem. Sci. 24:4-7.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 4-7
    • Travers, A.1
  • 49
    • 0033612538 scopus 로고    scopus 로고
    • Large-scale chromatin unfolding and remodeling induced by VP16 acidic activation domain
    • Tumbar, T., G. Sudlow, and A. S. Belmont. 1999. Large-scale chromatin unfolding and remodeling induced by VP16 acidic activation domain. J. Cell Biol. 145:1341-1354.
    • (1999) J. Cell Biol. , vol.145 , pp. 1341-1354
    • Tumbar, T.1    Sudlow, G.2    Belmont, A.S.3
  • 50
    • 0031790607 scopus 로고    scopus 로고
    • Location and function of linker histones
    • Vignali, M., and J. L. Workman. 1998. Location and function of linker histones. Nat. Struct. Biol. 5:1025-1028.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1025-1028
    • Vignali, M.1    Workman, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.