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Volumn 83 A, Issue 3, 2013, Pages 273-279

Histone H5-chromatin interactions in situ are strongly modulated by H5 C-terminal phosphorylation

Author keywords

Affinity; Chromatin; Linker histones; Phosphorylation

Indexed keywords

CDCA5 PROTEIN, HUMAN; CDK5 PROTEIN, HUMAN; CELL CYCLE PROTEIN; CYCLIN DEPENDENT KINASE 5; HISTONE; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84874094745     PISSN: 15524922     EISSN: 15524930     Source Type: Journal    
DOI: 10.1002/cyto.a.22221     Document Type: Article
Times cited : (7)

References (68)
  • 1
    • 0023429583 scopus 로고
    • Microheterogeneity in H1 histones and its consequences
    • Cole RD. Microheterogeneity in H1 histones and its consequences. Int J Pept Protein Res 1987; 30: 433-449.
    • (1987) Int J Pept Protein Res , vol.30 , pp. 433-449
    • Cole, R.D.1
  • 4
    • 0033151772 scopus 로고    scopus 로고
    • Histone H1: Location and role
    • Thomas JO. Histone H1: Location and role. Curr Opin Cell Biol 1999; 11: 312-317.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 312-317
    • Thomas, J.O.1
  • 5
    • 0029680555 scopus 로고    scopus 로고
    • The linker histones and chromatin structure: New twists
    • Zlatanova J, van Holde K. The linker histones and chromatin structure: New twists. Prog Nucleic Acid Res Mol Biol 1996; 52: 217-259.
    • (1996) Prog Nucleic Acid Res Mol Biol , vol.52 , pp. 217-259
    • Zlatanova, J.1    van Holde, K.2
  • 6
    • 0017401125 scopus 로고
    • Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule
    • Hartman PG, Chapman GE, Moss T, Bradbury EM. Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule. Eur J Biochem 1977; 77: 45-51.
    • (1977) Eur J Biochem , vol.77 , pp. 45-51
    • Hartman, P.G.1    Chapman, G.E.2    Moss, T.3    Bradbury, E.M.4
  • 7
    • 0020680232 scopus 로고
    • The histone H1 complements of dividing and nondividing cells of the mouse
    • Lennox RW, Cohen LH. The histone H1 complements of dividing and nondividing cells of the mouse. J Biol Chem 1983; 258: 262-268.
    • (1983) J Biol Chem , vol.258 , pp. 262-268
    • Lennox, R.W.1    Cohen, L.H.2
  • 8
    • 0023682238 scopus 로고
    • The production of tissue-specific histone complements during development
    • Lennox RW, Cohen LH. The production of tissue-specific histone complements during development. Biochem Cell Biol 1988; 66: 636-649.
    • (1988) Biochem Cell Biol , vol.66 , pp. 636-649
    • Lennox, R.W.1    Cohen, L.H.2
  • 9
    • 0031030788 scopus 로고    scopus 로고
    • Characterization of the H1.5 gene completes the set of human H1 subtype genes
    • Albig W, Meergans T, Doenecke D. Characterization of the H1.5 gene completes the set of human H1 subtype genes. Gene 1997; 184: 141-148.
    • (1997) Gene , vol.184 , pp. 141-148
    • Albig, W.1    Meergans, T.2    Doenecke, D.3
  • 10
    • 0035092987 scopus 로고    scopus 로고
    • A mammalian oocyte-specific linker histone gene H1oo: Homology with the genes for the oocyte-specific cleavage stage histone (cs-H1) of sea urchin and the B4/H1M histone of the frog
    • Tanaka M, Hennebold JD, Macfarlane J, Adashi EY. A mammalian oocyte-specific linker histone gene H1oo: Homology with the genes for the oocyte-specific cleavage stage histone (cs-H1) of sea urchin and the B4/H1M histone of the frog. Development 2001; 128: 655-664.
    • (2001) Development , vol.128 , pp. 655-664
    • Tanaka, M.1    Hennebold, J.D.2    Macfarlane, J.3    Adashi, E.Y.4
  • 11
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen XT, Yu LL, Weir JW, Gorovsky MA. Linker histones are not essential and affect chromatin condensation in vivo. Cell 1995; 82: 47-56.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.T.1    Yu, L.L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 13
    • 0035166077 scopus 로고    scopus 로고
    • Individual somatic H1 subtypes are dispensable for mouse development even in mice lacking the H1(0) replacement subtype
    • Fan Y, Sirotkin A, Russell RG, Ayala J, Skoultchi AI. Individual somatic H1 subtypes are dispensable for mouse development even in mice lacking the H1(0) replacement subtype. Mol Cell Biol 2001; 21: 7933-7943.
    • (2001) Mol Cell Biol , vol.21 , pp. 7933-7943
    • Fan, Y.1    Sirotkin, A.2    Russell, R.G.3    Ayala, J.4    Skoultchi, A.I.5
  • 15
    • 0034881774 scopus 로고    scopus 로고
    • A compendium of the histone H1 family of somatic subtypes: An elusive cast of characters and their characteristics
    • Parseghian MH, Hamkalo BA. A compendium of the histone H1 family of somatic subtypes: An elusive cast of characters and their characteristics. Biochem Cell Biol 2001; 79: 289-304.
    • (2001) Biochem Cell Biol , vol.79 , pp. 289-304
    • Parseghian, M.H.1    Hamkalo, B.A.2
  • 16
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding
    • Carruthers LM, Bednar J, Woodcock CL, Hansen JC. Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding. Biochemistry 1998; 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
  • 17
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions
    • Hansen JC. Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions. Annu Rev Biophys Biomol Struct 2002; 31: 361-392.
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 18
    • 0042388117 scopus 로고    scopus 로고
    • Revisiting the structure and functions of the linker histone C-terminal tail domain
    • Lu X, Hansen JC. Revisiting the structure and functions of the linker histone C-terminal tail domain. Biochem Cell Biol 2003; 81: 173-176.
    • (2003) Biochem Cell Biol , vol.81 , pp. 173-176
    • Lu, X.1    Hansen, J.C.2
  • 19
    • 25444523218 scopus 로고    scopus 로고
    • DNA-induced secondary structure of the carboxyl-terminal domain of histone H1
    • Roque A, Iloro I, Ponte I, Arrondo JL, Suau P. DNA-induced secondary structure of the carboxyl-terminal domain of histone H1. J Biol Chem 2005; 280: 32141-32147.
    • (2005) J Biol Chem , vol.280 , pp. 32141-32147
    • Roque, A.1    Iloro, I.2    Ponte, I.3    Arrondo, J.L.4    Suau, P.5
  • 20
    • 0020980777 scopus 로고
    • Phosphorylation of H1 histones
    • Hohmann P. Phosphorylation of H1 histones. Mol Cell Biochem 1983; 57: 81-92.
    • (1983) Mol Cell Biochem , vol.57 , pp. 81-92
    • Hohmann, P.1
  • 21
    • 0026441880 scopus 로고
    • Reversible histone modifications and the cell cycle
    • Bradbury EM. Reversible histone modifications and the cell cycle. Bioessays 1992; 14: 9-16.
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 22
    • 0030068951 scopus 로고    scopus 로고
    • In vivo phosphorylation of histone H1 variants during the cell cycle
    • Talasz H, Helliger W, Puschendorf B, Lindner H. In vivo phosphorylation of histone H1 variants during the cell cycle. Biochemistry 1996; 35: 1761-1767.
    • (1996) Biochemistry , vol.35 , pp. 1761-1767
    • Talasz, H.1    Helliger, W.2    Puschendorf, B.3    Lindner, H.4
  • 23
    • 33646569673 scopus 로고    scopus 로고
    • Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: Identification of a novel phosphorylation site on histone H1
    • Sarg B, Helliger W, Talasz H, Forg B, Lindner HH. Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: Identification of a novel phosphorylation site on histone H1. J Biol Chem 2006; 281: 6573-6580.
    • (2006) J Biol Chem , vol.281 , pp. 6573-6580
    • Sarg, B.1    Helliger, W.2    Talasz, H.3    Forg, B.4    Lindner, H.H.5
  • 24
    • 0025764058 scopus 로고
    • Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs
    • Hill CS, Rimmer JM, Green BN, Finch JT, Thomas JO. Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs. EMBO J 1991; 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
  • 25
    • 0026545414 scopus 로고
    • Chromatin condensation: Does histone H1 dephosphorylation play a role?
    • Roth SY, Allis CD. Chromatin condensation: Does histone H1 dephosphorylation play a role? Trends Biochem Sci 1992; 17: 93-98.
    • (1992) Trends Biochem Sci , vol.17 , pp. 93-98
    • Roth, S.Y.1    Allis, C.D.2
  • 26
    • 0016337102 scopus 로고
    • Molecular basis of control of mitotic cell division in eukaryotes
    • Bradbury EM, Inglis RJ, Matthews HR, Langan TA. Molecular basis of control of mitotic cell division in eukaryotes. Nature 1974; 249: 553-556.
    • (1974) Nature , vol.249 , pp. 553-556
    • Bradbury, E.M.1    Inglis, R.J.2    Matthews, H.R.3    Langan, T.A.4
  • 27
    • 0015506446 scopus 로고
    • Synthesis and turnover of DNA-bound histone during maturation of avian red blood cells
    • Appels R, Wells JR. Synthesis and turnover of DNA-bound histone during maturation of avian red blood cells. J Mol Biol 1972; 70: 425-434.
    • (1972) J Mol Biol , vol.70 , pp. 425-434
    • Appels, R.1    Wells, J.R.2
  • 28
    • 0023428462 scopus 로고
    • Regulation of histone and beta A-globin gene expression during differentiation of chicken erythroid cells
    • Affolter M, Cote J, Renaud J, Ruiz-Carrillo A. Regulation of histone and beta A-globin gene expression during differentiation of chicken erythroid cells. Mol Cell Biol 1987; 7: 3663-3672.
    • (1987) Mol Cell Biol , vol.7 , pp. 3663-3672
    • Affolter, M.1    Cote, J.2    Renaud, J.3    Ruiz-Carrillo, A.4
  • 29
    • 0017580797 scopus 로고
    • Phosphorylation and dephosphorylation of histone V (H5): Controlled condensation of avian erythrocyte chromatin
    • Sung MT. Phosphorylation and dephosphorylation of histone V (H5): Controlled condensation of avian erythrocyte chromatin. Biochemistry 1977; 16: 286-290.
    • (1977) Biochemistry , vol.16 , pp. 286-290
    • Sung, M.T.1
  • 30
    • 0021104510 scopus 로고
    • Exchange of histones H1 and H5 between chromatin fragments. A preference of H5 for higher-order structures
    • Thomas JO, Rees C. Exchange of histones H1 and H5 between chromatin fragments. A preference of H5 for higher-order structures. Eur J Biochem 1983; 134: 109-115.
    • (1983) Eur J Biochem , vol.134 , pp. 109-115
    • Thomas, J.O.1    Rees, C.2
  • 31
    • 0021710745 scopus 로고
    • Interactions of H1 and H5 histones with polynucleotides of B- and Z-DNA conformations
    • Mura CV, Stollar BD. Interactions of H1 and H5 histones with polynucleotides of B- and Z-DNA conformations. Biochemistry 1984; 23: 6147-6152.
    • (1984) Biochemistry , vol.23 , pp. 6147-6152
    • Mura, C.V.1    Stollar, B.D.2
  • 33
    • 0019332869 scopus 로고
    • The binding of histones H1 and H5 to chromatin in chicken erythrocyte nuclei
    • Kumar NM, Walker IO. The binding of histones H1 and H5 to chromatin in chicken erythrocyte nuclei. Nucleic Acids Res 1980; 8: 3535-3551.
    • (1980) Nucleic Acids Res , vol.8 , pp. 3535-3551
    • Kumar, N.M.1    Walker, I.O.2
  • 34
    • 0025259589 scopus 로고
    • Replacement of histone H1 by H5 in vivo does not change the nucleosome repeat length of chromatin but increases its stability
    • Sun JM, Ali Z, Lurz R, Ruiz-Carrillo A. Replacement of histone H1 by H5 in vivo does not change the nucleosome repeat length of chromatin but increases its stability. EMBO J 1990; 9: 1651-1658.
    • (1990) EMBO J , vol.9 , pp. 1651-1658
    • Sun, J.M.1    Ali, Z.2    Lurz, R.3    Ruiz-Carrillo, A.4
  • 35
    • 0037160123 scopus 로고    scopus 로고
    • Linker histone subtype composition and affinity for chromatin in situ in nucleated mature erythrocytes
    • Koutzamani E, Loborg H, Sarg B, Lindner HH, Rundquist I. Linker histone subtype composition and affinity for chromatin in situ in nucleated mature erythrocytes. J Biol Chem 2002; 277: 44688-44694.
    • (2002) J Biol Chem , vol.277 , pp. 44688-44694
    • Koutzamani, E.1    Loborg, H.2    Sarg, B.3    Lindner, H.H.4    Rundquist, I.5
  • 36
    • 34250218537 scopus 로고    scopus 로고
    • Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin
    • Orrego M, Ponte I, Roque A, Buschati N, Mora X, Suau P. Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin. BMC Biol 2007; 5: 22.
    • (2007) BMC Biol , vol.5 , pp. 22
    • Orrego, M.1    Ponte, I.2    Roque, A.3    Buschati, N.4    Mora, X.5    Suau, P.6
  • 37
    • 0027216094 scopus 로고
    • Phosphorylation weakens DNA binding by peptides containing multiple SPKK sequences
    • Green GR, Lee HJ, Poccia DL. Phosphorylation weakens DNA binding by peptides containing multiple SPKK sequences. J Biol Chem 1993; 268: 11247-11255.
    • (1993) J Biol Chem , vol.268 , pp. 11247-11255
    • Green, G.R.1    Lee, H.J.2    Poccia, D.L.3
  • 38
    • 0029120154 scopus 로고
    • Increased phosphorylation of histone H1 in mouse fibroblasts transformed with oncogenes or constitutively active mitogen-activated protein kinase kinase
    • Chadee DN, Taylor WR, Hurta RR, Allis CD, Wright JA, Davie JR. Increased phosphorylation of histone H1 in mouse fibroblasts transformed with oncogenes or constitutively active mitogen-activated protein kinase kinase. J Biol Chem 1995; 270: 20098-20105.
    • (1995) J Biol Chem , vol.270 , pp. 20098-20105
    • Chadee, D.N.1    Taylor, W.R.2    Hurta, R.R.3    Allis, C.D.4    Wright, J.A.5    Davie, J.R.6
  • 39
    • 0029155905 scopus 로고
    • Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei
    • Lu MJ, Mpoke SS, Dadd CA, Allis CD. Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei. Mol Biol Cell 1995; 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
  • 40
    • 0029909105 scopus 로고    scopus 로고
    • Increased histone H1 phosphorylation and relaxed chromatin structure in Rb-deficient fibroblasts
    • Herrera RE, Chen F, Weinberg RA. Increased histone H1 phosphorylation and relaxed chromatin structure in Rb-deficient fibroblasts. Proc Natl Acad Sci USA 1996; 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
  • 42
    • 0037144862 scopus 로고    scopus 로고
    • Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin
    • Dou Y, Bowen J, Liu Y, Gorovsky MA. Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin. J Cell Biol 2002; 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
  • 43
    • 0033610814 scopus 로고    scopus 로고
    • In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor
    • Talasz H, Sapojnikova N, Helliger W, Lindner H, Puschendorf B. In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor. J Biol Chem 1998; 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
  • 44
    • 0030849670 scopus 로고    scopus 로고
    • DNA binding fluorochromes as probes for histone H1-chromatin interactions in situ
    • Loborg H, Rundquist I. DNA binding fluorochromes as probes for histone H1-chromatin interactions in situ. Cytometry 1997; 28: 212-219.
    • (1997) Cytometry , vol.28 , pp. 212-219
    • Loborg, H.1    Rundquist, I.2
  • 45
    • 0034192337 scopus 로고    scopus 로고
    • Affinity of linker histones for chromatin in situ analyzed using DAPI as a cytochemical probe
    • Loborg H, Rundquist I. Affinity of linker histones for chromatin in situ analyzed using DAPI as a cytochemical probe. Cytometry 2000; 40: 1-9.
    • (2000) Cytometry , vol.40 , pp. 1-9
    • Loborg, H.1    Rundquist, I.2
  • 46
    • 33750705925 scopus 로고    scopus 로고
    • Analyses of linker histone-chromatin interactions in situ
    • Rundquist I, Lindner HH. Analyses of linker histone-chromatin interactions in situ. Biochem Cell Biol 2006; 84: 427-436.
    • (2006) Biochem Cell Biol , vol.84 , pp. 427-436
    • Rundquist, I.1    Lindner, H.H.2
  • 47
    • 1942534139 scopus 로고    scopus 로고
    • Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions
    • Kostova NN, Srebreva L, Markov DV, Rundquist I. Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions. Cytometry Part A 2004; 58A: 132-139.
    • (2004) Cytometry Part A , vol.58 A , pp. 132-139
    • Kostova, N.N.1    Srebreva, L.2    Markov, D.V.3    Rundquist, I.4
  • 48
    • 0020806761 scopus 로고
    • A rapid and convenient method for the purification of chicken erythrocyte histone H5
    • Srebreva L, Zlatanova J. A rapid and convenient method for the purification of chicken erythrocyte histone H5. J Biochem Biophys Methods 1983; 8: 85-86.
    • (1983) J Biochem Biophys Methods , vol.8 , pp. 85-86
    • Srebreva, L.1    Zlatanova, J.2
  • 49
    • 0032557660 scopus 로고    scopus 로고
    • The microheterogeneity of the mammalian H1° histone. Evidence for an age-dependent deamidation
    • Lindner H, Sarg B, Hoertnagl B, Helliger W. The microheterogeneity of the mammalian H1° histone. Evidence for an age-dependent deamidation. J Biol Chem 1998; 273: 13324-13330.
    • (1998) J Biol Chem , vol.273 , pp. 13324-13330
    • Lindner, H.1    Sarg, B.2    Hoertnagl, B.3    Helliger, W.4
  • 50
    • 0026555376 scopus 로고
    • High-performance capillary electrophoresis of core histones and their acetylated modified derivatives
    • Lindner H, Helliger W, Dirschlmayer A, Jaquemar M, Puschendorf B. High-performance capillary electrophoresis of core histones and their acetylated modified derivatives. Biochem J 1992; 283: 467-471.
    • (1992) Biochem J , vol.283 , pp. 467-471
    • Lindner, H.1    Helliger, W.2    Dirschlmayer, A.3    Jaquemar, M.4    Puschendorf, B.5
  • 52
    • 0027210786 scopus 로고
    • Application of high-performance capillary electrophoresis to the analysis of H1 histones
    • Lindner H, Wurm M, Dirschlmayer A, Sarg B, Helliger W. Application of high-performance capillary electrophoresis to the analysis of H1 histones. Electrophoresis 1993; 14: 480-485.
    • (1993) Electrophoresis , vol.14 , pp. 480-485
    • Lindner, H.1    Wurm, M.2    Dirschlmayer, A.3    Sarg, B.4    Helliger, W.5
  • 53
    • 0028914407 scopus 로고
    • Effect of buffer composition on the migration order and separation of histone H1 subtypes
    • Lindner H, Helliger W, Sarg B, Meraner C. Effect of buffer composition on the migration order and separation of histone H1 subtypes. Electrophoresis 1995; 16: 604-610.
    • (1995) Electrophoresis , vol.16 , pp. 604-610
    • Lindner, H.1    Helliger, W.2    Sarg, B.3    Meraner, C.4
  • 55
    • 0033572585 scopus 로고    scopus 로고
    • The N-terminally acetylated form of mammalian histone H1°, but not that of avian histone H5, increases with age
    • Sarg B, Helliger W, Hoertnagl B, Puschendorf B, Lindner H. The N-terminally acetylated form of mammalian histone H1°, but not that of avian histone H5, increases with age. Arch Biochem Biophys 1999; 372: 333-339.
    • (1999) Arch Biochem Biophys , vol.372 , pp. 333-339
    • Sarg, B.1    Helliger, W.2    Hoertnagl, B.3    Puschendorf, B.4    Lindner, H.5
  • 56
    • 0018190058 scopus 로고
    • Sites of in vivo phosphorylation of histone H5
    • Sung MT, Freedlender EF. Sites of in vivo phosphorylation of histone H5. Biochemistry 1978; 17: 1884-1890.
    • (1978) Biochemistry , vol.17 , pp. 1884-1890
    • Sung, M.T.1    Freedlender, E.F.2
  • 58
    • 79961124094 scopus 로고    scopus 로고
    • Histone H1 interphase phosphorylation becomes largely established in G1 or early S phase and differs in G1 between T-lymphoblastoid cells and normal T cells
    • Gréen A, Sarg B, Gréen H, Lonn A, Lindner HH, Rundquist I. Histone H1 interphase phosphorylation becomes largely established in G1 or early S phase and differs in G1 between T-lymphoblastoid cells and normal T cells. Epigenetics Chromatin 2011; 4: 15.
    • (2011) Epigenetics Chromatin , vol.4 , pp. 15
    • Gréen, A.1    Sarg, B.2    Gréen, H.3    Lonn, A.4    Lindner, H.H.5    Rundquist, I.6
  • 59
    • 0020491435 scopus 로고
    • Characterization of highly phosphorylated subcomponents of rat thymus H1 histone
    • Langan TA. Characterization of highly phosphorylated subcomponents of rat thymus H1 histone. J Biol Chem 1982; 257: 14835-14846.
    • (1982) J Biol Chem , vol.257 , pp. 14835-14846
    • Langan, T.A.1
  • 60
    • 0018802768 scopus 로고
    • Phosphorlyation of H1 and H5 histones by cyclic AMP-dependent protein kinase reduces DNA binding
    • Fasy TM, Inoue A, Johnson EM, Allfrey VG. Phosphorlyation of H1 and H5 histones by cyclic AMP-dependent protein kinase reduces DNA binding. Biochim Biophys Acta 1979; 564: 322-334.
    • (1979) Biochim Biophys Acta , vol.564 , pp. 322-334
    • Fasy, T.M.1    Inoue, A.2    Johnson, E.M.3    Allfrey, V.G.4
  • 62
    • 0024465335 scopus 로고
    • SPKK, a new nucleic acid-binding unit of protein found in histone
    • Suzuki M. SPKK, a new nucleic acid-binding unit of protein found in histone. EMBO J 1989; 8: 797-804.
    • (1989) EMBO J , vol.8 , pp. 797-804
    • Suzuki, M.1
  • 63
    • 70349655631 scopus 로고    scopus 로고
    • Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF
    • Clausell J, Happel N, Hale TK, Doenecke D, Beato M. Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF. PLoS One 2009; 4: e0007243.
    • (2009) PLoS One , vol.4
    • Clausell, J.1    Happel, N.2    Hale, T.K.3    Doenecke, D.4    Beato, M.5
  • 64
    • 49249102932 scopus 로고    scopus 로고
    • Phosphorylation of the carboxy-terminal domain of histone H1: Effects on secondary structure and DNA condensation
    • Roque A, Ponte I, Arrondo JL, Suau P. Phosphorylation of the carboxy-terminal domain of histone H1: Effects on secondary structure and DNA condensation. Nucleic Acids Res 2008; 36: 4719-4726.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4719-4726
    • Roque, A.1    Ponte, I.2    Arrondo, J.L.3    Suau, P.4
  • 65
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • Hendzel MJ, Lever MA, Crawford E, Th'ng JP. The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. J Biol Chem 2004; 279: 20028-20034.
    • (2004) J Biol Chem , vol.279 , pp. 20028-20034
    • Hendzel, M.J.1    Lever, M.A.2    Crawford, E.3    Th'ng, J.P.4
  • 66
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever MA, Th'ng JP, Sun X, Hendzel MJ. Rapid exchange of histone H1.1 on chromatin in living human cells. Nature 2000; 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
  • 67
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli T, Gunjan A, Hock R, Bustin M, Brown DT. Dynamic binding of histone H1 to chromatin in living cells. Nature 2000; 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
  • 68
    • 33745020770 scopus 로고    scopus 로고
    • Determinants of histone H1 mobility and chromatin binding in living cells
    • Catez F, Ueda T, Bustin M. Determinants of histone H1 mobility and chromatin binding in living cells. Nat Struct Mol Biol 2006; 13: 305-310.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 305-310
    • Catez, F.1    Ueda, T.2    Bustin, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.