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Volumn 15, Issue 13, 1996, Pages 3421-3429

Identification of two DNA-binding sites on the globular domain of histone H5

Author keywords

Chromatin; DNA binding; Globular domain; Histone H5; Mutagenesis

Indexed keywords

DNA; DNA BINDING PROTEIN; HISTONE H5; MUTANT PROTEIN;

EID: 0030016336     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00708.x     Document Type: Article
Times cited : (131)

References (50)
  • 1
    • 0019157001 scopus 로고
    • The structure of histone HI and its location in chromatin
    • Allan, J., Hartman, P.G., Crane-Robinson, C. and Aviles, F.X. (1980) The structure of histone HI and its location in chromatin. Nature, 288, 675-679.
    • (1980) Nature , vol.288 , pp. 675-679
    • Allan, J.1    Hartman, P.G.2    Crane-Robinson, C.3    Aviles, F.X.4
  • 2
    • 0019628147 scopus 로고
    • Stability of the higher-order structure of chicken erythrocyte chromatin in solution
    • Bates, D.L., Butler, P.J.G., Pearson, E.C. and Thomas, J.O. (1981) Stability of the higher-order structure of chicken erythrocyte chromatin in solution. Eur. J. Biochem., 119, 469-476.
    • (1981) Eur. J. Biochem. , vol.119 , pp. 469-476
    • Bates, D.L.1    Butler, P.J.G.2    Pearson, E.C.3    Thomas, J.O.4
  • 3
    • 0019332577 scopus 로고
    • Primary organization of nucleosomes containing all five histones and DNA 175 and 165 base-pairs long
    • Belyavsky, A.V., Bavykin, S.G., Goguadze, E.G. and Mirzabekov, A.D. (1980) Primary organization of nucleosomes containing all five histones and DNA 175 and 165 base-pairs long. J. Mol. Biol., 139, 519-536.
    • (1980) J. Mol. Biol. , vol.139 , pp. 519-536
    • Belyavsky, A.V.1    Bavykin, S.G.2    Goguadze, E.G.3    Mirzabekov, A.D.4
  • 5
    • 0026560170 scopus 로고
    • Site-directed mutagenesis studies on the binding of the globular domain of linker histone H5 to the nucleosome
    • Buckle, R.S., Maman, J.D. and Allan, J. (1992) Site-directed mutagenesis studies on the binding of the globular domain of linker histone H5 to the nucleosome. J. Mol. Biol., 223, 651-659.
    • (1992) J. Mol. Biol. , vol.223 , pp. 651-659
    • Buckle, R.S.1    Maman, J.D.2    Allan, J.3
  • 6
    • 0019130753 scopus 로고
    • Changes in chromatin folding in solution
    • Butler, P.J.G. and Thomas, J.O. (1980) Changes in chromatin folding in solution. J. Mol. Biol., 140, 505-529.
    • (1980) J. Mol. Biol. , vol.140 , pp. 505-529
    • Butler, P.J.G.1    Thomas, J.O.2
  • 7
    • 0019880525 scopus 로고
    • Exchange of histone H1 between segments of chromatin
    • Caron, F. and Thomas, J.O. (1981) Exchange of histone H1 between segments of chromatin. J. Mol. Biol., 146, 513-537.
    • (1981) J. Mol. Biol. , vol.146 , pp. 513-537
    • Caron, F.1    Thomas, J.O.2
  • 8
    • 0028068811 scopus 로고
    • Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Full assignment, tertiary structure, and comparison with the globular domain of H5
    • Cerf, C., Lippens, G., Ramakrishnan, V., Muyldermans, S., Segers, A., Wyns, L., Wodak, S.J. and Hallenga, K. (1994) Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of H5. Biochemistry, 33, 11079-11086.
    • (1994) Biochemistry , vol.33 , pp. 11079-11086
    • Cerf, C.1    Lippens, G.2    Ramakrishnan, V.3    Muyldermans, S.4    Segers, A.5    Wyns, L.6    Wodak, S.J.7    Hallenga, K.8
  • 9
    • 0028222235 scopus 로고
    • Helix propensities of the amino- Acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabartty, A., Kortemme, T. and Baldwin, R.L. (1994) Helix propensities of the amino- acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Prolein Sci., 3, 843-852.
    • (1994) Prolein Sci. , vol.3 , pp. 843-852
    • Chakrabartty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 10
    • 0022470051 scopus 로고
    • Salt-dependent co-operative interaction of histone H1 with linear DNA
    • Clark, D.J. and Thomas, J.O. (1986) Salt-dependent co-operative interaction of histone H1 with linear DNA. J. Mol. Biol., 187, 569-580.
    • (1986) J. Mol. Biol. , vol.187 , pp. 569-580
    • Clark, D.J.1    Thomas, J.O.2
  • 11
    • 0024264685 scopus 로고
    • Differences in the binding of H1 variants to DNA: Cooperativity and linker-length related distribution
    • Clark, D.J. and Thomas, J.O. (1988) Differences in the binding of H1 variants to DNA: cooperativity and linker-length related distribution. Eur. J. Biochem., 178, 225-233.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 225-233
    • Clark, D.J.1    Thomas, J.O.2
  • 12
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3γ/fork head DNA-recognition motif resembles histone H5
    • Clark, K.L., Halay, E.D., Lai, E. and Burley, S.K. (1993) Co-crystal structure of the HNF-3γ/fork head DNA-recognition motif resembles histone H5. Nature, 364, 412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 13
    • 0024375866 scopus 로고
    • Binding of the globular domain of linker histones H5/H1 to the nucleosome - A hypothesis
    • Crane-Robinson, C. and Ptitsyn, O.B. (1989) Binding of the globular domain of linker histones H5/H1 to the nucleosome - A hypothesis. Protein Engng, 2, 577-582.
    • (1989) Protein Engng , vol.2 , pp. 577-582
    • Crane-Robinson, C.1    Ptitsyn, O.B.2
  • 14
    • 0022703478 scopus 로고
    • Structuring of H1 histone. Evidence of high-affinity binding sites for phosphate ions
    • de Petrocellis, L., Quagliarotti, G., Tomei, L. and Geraci, G. (1986) Structuring of H1 histone. Evidence of high-affinity binding sites for phosphate ions. Eur. J. Biochem., 156, 143-148.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 143-148
    • De Petrocellis, L.1    Quagliarotti, G.2    Tomei, L.3    Geraci, G.4
  • 15
    • 0025311114 scopus 로고
    • DNA and protein determinants of nucleosome positioning on sea urchin 5S RNA gene sequences in vitro
    • Dong, F. Hansen, J.C. and van Holde, K.E. (1990) DNA and protein determinants of nucleosome positioning on sea urchin 5S RNA gene sequences in vitro. Proc. Natl Acad. Sci. USA, 87, 5724-5728.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5724-5728
    • Dong, F.1    Hansen, J.C.2    Van Holde, K.E.3
  • 16
    • 0026663825 scopus 로고
    • Co-operative binding of the globular domain of histone H5 to DNA
    • Draves, P.H., Lowary, P.T. and Widom, J. (1992) Co-operative binding of the globular domain of histone H5 to DNA. J. Mol. Biol., 225, 1105-1121.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1105-1121
    • Draves, P.H.1    Lowary, P.T.2    Widom, J.3
  • 17
    • 0028446542 scopus 로고
    • Expression of chicken linker histones in E. coli: Sources of problems and methods for overcoming some of the difficulties
    • Gerchman, S.E., Graziano, V. and Ramakrishnan, V. (1994) Expression of chicken linker histones in E. coli: sources of problems and methods for overcoming some of the difficulties. Protein Expr. Purif., 5, 242-251.
    • (1994) Protein Expr. Purif. , vol.5 , pp. 242-251
    • Gerchman, S.E.1    Graziano, V.2    Ramakrishnan, V.3
  • 18
    • 0028314834 scopus 로고
    • Histone H1 is located in the interior of the chromatin 30 nm filament
    • Graziano, V., Gerchman, S.E., Schneider, D.K. and Ramakrishnan, V. (1994) Histone H1 is located in the interior of the chromatin 30 nm filament. Nature, 368, 351-354.
    • (1994) Nature , vol.368 , pp. 351-354
    • Graziano, V.1    Gerchman, S.E.2    Schneider, D.K.3    Ramakrishnan, V.4
  • 19
    • 0027248504 scopus 로고
    • Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome
    • Hayes, J.J. and Wolffe, A.P. (1993) Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome. Proc. Natl Acad. Sci. USA, 90, 6415-6419.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6415-6419
    • Hayes, J.J.1    Wolffe, A.P.2
  • 20
    • 0028031310 scopus 로고
    • Contacts of the globular domain of histone H5 and core histones with DNA in a 'chromatosome'
    • Hayes, J.J., Pruss, D. and Wolffe, A.P. (1994) Contacts of the globular domain of histone H5 and core histones with DNA in a 'chromatosome'. Proc. Natl Acad. Sci. USA, 91, 7817-7821.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7817-7821
    • Hayes, J.J.1    Pruss, D.2    Wolffe, A.P.3
  • 21
    • 0025056959 scopus 로고
    • Core histone-DNA interactions in sea urchin sperm chromatin: The N-terminal tail of H2B interacts with linker DNA
    • Hill, C.S. and Thomas, J.O. (1990) Core histone-DNA interactions in sea urchin sperm chromatin: the N-terminal tail of H2B interacts with linker DNA. Eur. J. Biochem., 187, 145-153.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 145-153
    • Hill, C.S.1    Thomas, J.O.2
  • 22
    • 0025764058 scopus 로고
    • Histone-DNA interactions and their modulation by phosphorylation of Ser-Pro-X-Lys/Arg- Motifs
    • Hill, C.S., Rimmer, J.M., Green, B.N., Finch, J.T. and Thomas, J.O. (1991) Histone-DNA interactions and their modulation by phosphorylation of Ser-Pro-X-Lys/Arg- motifs. EMBO J., 10, 1939-1948.
    • (1991) EMBO J. , vol.10 , pp. 1939-1948
    • Hill, C.S.1    Rimmer, J.M.2    Green, B.N.3    Finch, J.T.4    Thomas, J.O.5
  • 23
    • 0026674251 scopus 로고
    • α-Helix stability in proteins. II Factors that influence stability at an internal position
    • Horovitz, A., Matthews, J.M. and Fersht, A.R. (1992) α-Helix stability in proteins. II Factors that influence stability at an internal position. J. Mol. Biol., 227, 560-568.
    • (1992) J. Mol. Biol. , vol.227 , pp. 560-568
    • Horovitz, A.1    Matthews, J.M.2    Fersht, A.R.3
  • 25
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt, O., Grunert, H.-P. and Hahn, U. (1990) A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene, 96, 125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.-P.2    Hahn, U.3
  • 26
    • 0025884566 scopus 로고
    • Extended C-terminal tail of wheat histone H2A interacts with DNA of the linker region
    • Lindsey, G.G., Orgeig, S., Thompson, P., Davies, N. and Maeder, D.L. (1991) Extended C-terminal tail of wheat histone H2A interacts with DNA of the linker region. J. Mol. Biol., 218, 805-813.
    • (1991) J. Mol. Biol. , vol.218 , pp. 805-813
    • Lindsey, G.G.1    Orgeig, S.2    Thompson, P.3    Davies, N.4    Maeder, D.L.5
  • 27
    • 0025098741 scopus 로고
    • Chromatin superstructure-dependent crosslinking with DNA of the histone H5 residues Thr1, His25 and His62
    • Mirzabekov, A.D., Pruss, D.V. and Ebralidse, K.K. (1989) Chromatin superstructure-dependent crosslinking with DNA of the histone H5 residues Thr1, His25 and His62. J. Mol. Biol. 211, 479-491.
    • (1989) J. Mol. Biol. , vol.211 , pp. 479-491
    • Mirzabekov, A.D.1    Pruss, D.V.2    Ebralidse, K.K.3
  • 28
    • 0028053165 scopus 로고
    • DNA sequence organization in chromatosomes
    • Muyldermans, S. and Travers, A.A. (1994) DNA sequence organization in chromatosomes. J. Mol. Biol., 235, 855-870.
    • (1994) J. Mol. Biol. , vol.235 , pp. 855-870
    • Muyldermans, S.1    Travers, A.A.2
  • 30
    • 0017358203 scopus 로고
    • Action of micrococcal nuclease on chromatin and the location of histone H1
    • Noll, M. and Kornberg, R.D. (1977) Action of micrococcal nuclease on chromatin and the location of histone H1. J. Mol. Biol., 109, 393-404.
    • (1977) J. Mol. Biol. , vol.109 , pp. 393-404
    • Noll, M.1    Kornberg, R.D.2
  • 31
    • 0024380891 scopus 로고
    • Thymidine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin
    • Pehrson, J.R. (1989) Thymidine 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
  • 32
    • 0028130301 scopus 로고
    • Linker histones H1 and H5 prevent mobility of positioned nucleosomes
    • Pennings, S., Meersseman, G. and Bradbury, E.M. (1994) Linker histones H1 and H5 prevent mobility of positioned nucleosomes. Proc. Natl Acad. Sci. USA, 91, 10275-10279.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10275-10279
    • Pennings, S.1    Meersseman, G.2    Bradbury, E.M.3
  • 33
    • 0029152586 scopus 로고
    • Nucleosomal anatomy - Where are the histones?
    • Pruss, D., Hayes, J.J. and Wolffe, A.P. (1995) Nucleosomal anatomy - where are the histones? BioEssays, 17, 161-170.
    • (1995) BioEssays , vol.17 , pp. 161-170
    • Pruss, D.1    Hayes, J.J.2    Wolffe, A.P.3
  • 35
    • 0027402969 scopus 로고
    • Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J.T., Graziano, V., Lee, P.L. and Sweet, R.M. (1993) Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding. Nature, 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 36
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90°
    • Schultz, S.C., Shields, G.C. and Steitz, T.A. (1991) Crystal structure of a CAP-DNA complex: the DNA is bent by 90°. Science, 253, 1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 37
    • 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
  • 38
    • 0024195819 scopus 로고
    • Footprinting of linker histones H5 and H1 on the nucleosome
    • Staynov, D.Z. and Crane-Robinson, C. (1988) Footprinting of linker histones H5 and H1 on the nucleosome. EMBO J., 7, 3685-3691.
    • (1988) EMBO J. , vol.7 , pp. 3685-3691
    • Staynov, D.Z.1    Crane-Robinson, C.2
  • 40
    • 0029117147 scopus 로고
    • Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA
    • Teo, S.-H., Grasser, K.D., Hardman, C.H., Broadhurst, R.W., Laue, E.D. and Thomas, J.O. (1995) Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA. EMBO J., 14, 3844-3853.
    • (1995) EMBO J. , vol.14 , pp. 3844-3853
    • Teo, S.-H.1    Grasser, K.D.2    Hardman, C.H.3    Broadhurst, R.W.4    Laue, E.D.5    Thomas, J.O.6
  • 41
    • 0017903377 scopus 로고
    • The study of histone-histone associations by chemical cross-linking
    • Thomas, J.O. and Kornberg, R.D. (1978) The study of histone-histone associations by chemical cross-linking. Methods Cell Biol., 18, 429-440.
    • (1978) Methods Cell Biol. , vol.18 , pp. 429-440
    • Thomas, J.O.1    Kornberg, R.D.2
  • 42
    • 0023054104 scopus 로고
    • Selective radiolabelling and identification of a strong nucleosome binding site on the globular domain of histone H5
    • Thomas, J.O. and Wilson, C.M. (1986) Selective radiolabelling and identification of a strong nucleosome binding site on the globular domain of histone H5. EMBO J., 5, 3531-3537.
    • (1986) EMBO J. , vol.5 , pp. 3531-3537
    • Thomas, J.O.1    Wilson, C.M.2
  • 43
    • 0026597552 scopus 로고
    • Cooperative binding of the globular domains of histones H1 and H5 to DNA
    • Thomas, J.O., Rees, C. and Finch, J.T. (1992) Cooperative binding of the globular domains of histones H1 and H5 to DNA. Nucleic Acids Res., 20, 187-194.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 187-194
    • Thomas, J.O.1    Rees, C.2    Finch, J.T.3
  • 44
    • 0030009322 scopus 로고    scopus 로고
    • A DNA sequence for positioning chromatosomes
    • Travers, A.A. and Muyldermans, S. (1996) A DNA sequence for positioning chromatosomes. J. Mol. Biol., 257, 486-491.
    • (1996) J. Mol. Biol. , vol.257 , pp. 486-491
    • Travers, A.A.1    Muyldermans, S.2
  • 45
    • 0029091306 scopus 로고
    • A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: Restriction by linker histones
    • Ura, K., Hayes, J.J. and Wolffe, A.P. (1995) A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: restriction by linker histones. EMBO J., 14, 3752-3765.
    • (1995) EMBO J. , vol.14 , pp. 3752-3765
    • Ura, K.1    Hayes, J.J.2    Wolffe, A.P.3
  • 46
    • 0027452325 scopus 로고
    • Preferential binding of histone H1 to four-way helical junction DNA
    • Varga-Weisz, P., van Holde, K. and Zlatanova, J. (1993) Preferential binding of histone H1 to four-way helical junction DNA. J. Biol. Chem., 268, 20699-20700.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20699-20700
    • Varga-Weisz, P.1    Van Holde, K.2    Zlatanova, J.3
  • 49
    • 0025730049 scopus 로고
    • Histone and histone gene compilation and alignment update
    • Wells, D. and Brown, D. (1991) Histone and histone gene compilation and alignment update. Nucleic Acids Res., 19 (Suppl.), 2173-2188.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.SUPPL. , pp. 2173-2188
    • Wells, D.1    Brown, D.2
  • 50
    • 0024550346 scopus 로고
    • A comprehensive compilation of histones and histone genes
    • Wells, D. and McBride, C. (1989) A comprehensive compilation of histones and histone genes. Nucleic Acids Res., 17 (Suppl.), 311-346.
    • (1989) Nucleic Acids Res. , vol.17 , Issue.SUPPL. , pp. 311-346
    • Wells, D.1    McBride, C.2


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