메뉴 건너뛰기




Volumn 37, Issue 10, 2009, Pages 3391-3406

Linker histone H1 is present in centromeric chromatin of living human cells next to inner kinetochore proteins

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CENTROMERE PROTEIN A; CENTROMERE PROTEIN B; CENTROMERE PROTEIN C; HISTONE H1; SATELLITE DNA; UNCLASSIFIED DRUG;

EID: 67249123010     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp199     Document Type: Article
Times cited : (16)

References (116)
  • 1
    • 0015545526 scopus 로고
    • Light and electron microscopy of rat kangaroo cells in mitosis, II. Kinetochore structure and function
    • Roos,U.P. (1973) Light and electron microscopy of rat kangaroo cells in mitosis, II. Kinetochore structure and function. Chromosoma, 41 195-220.
    • (1973) Chromosoma , vol.41 , pp. 195-220
    • Roos, U.P.1
  • 3
    • 34250168342 scopus 로고    scopus 로고
    • Conde e Silva,N.C., Black,B.E., Sivolob,A., Filipski,J., Cleveland,D.W. and Prunell,A. (2007) CENP-A-containing nucleosomes: Easier disassembly versus exclusive centromeric localization. J. Mol. Biol., 370 555-573.
    • Conde e Silva,N.C., Black,B.E., Sivolob,A., Filipski,J., Cleveland,D.W. and Prunell,A. (2007) CENP-A-containing nucleosomes: Easier disassembly versus exclusive centromeric localization. J. Mol. Biol., 370 555-573.
  • 4
    • 0021989578 scopus 로고
    • Identification of a familiy of human centromere proteins using autoimmune sera from patients with scleroderma
    • Earnshaw,W.C. and Rothfield,N. (1985) Identification of a familiy of human centromere proteins using autoimmune sera from patients with scleroderma. Chromosoma, 91, 313-321.
    • (1985) Chromosoma , vol.91 , pp. 313-321
    • Earnshaw, W.C.1    Rothfield, N.2
  • 5
    • 0033600872 scopus 로고    scopus 로고
    • Characterisation of a novel kinetochore protein, CENP-H
    • Sugata,N., Munekata,E. and Todokoro,K. (1999) Characterisation of a novel kinetochore protein, CENP-H. J. Biol. Chem., 274, 27343-27346.
    • (1999) J. Biol. Chem , vol.274 , pp. 27343-27346
    • Sugata, N.1    Munekata, E.2    Todokoro, K.3
  • 10
    • 37549071893 scopus 로고    scopus 로고
    • Molecular architecture of the kinetochore-microtubule interface
    • Cheeseman,I.M. and Desai,A. (2008) Molecular architecture of the kinetochore-microtubule interface. Nat. Rev. Mol. Cell Biol., 9 33-46.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 33-46
    • Cheeseman, I.M.1    Desai, A.2
  • 12
    • 67149142163 scopus 로고    scopus 로고
    • Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-A and CENP-B
    • Hellwig,D., Münch,S., Orthaus,S., Hoischen,C., Hemmerich,P. and Diekmann,S. (2008) Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-A and CENP-B. J. Biophoton., 1 245-254.
    • (2008) J. Biophoton , vol.1 , pp. 245-254
    • Hellwig, D.1    Münch, S.2    Orthaus, S.3    Hoischen, C.4    Hemmerich, P.5    Diekmann, S.6
  • 14
    • 3042794631 scopus 로고    scopus 로고
    • Building the centromere: From foundation proteins to 3D organisation
    • Amor,D.J., Kalitsis,P., Sumer,H. and Choo,K.H.A. (2004) Building the centromere: From foundation proteins to 3D organisation. Trends Cell Biol., 14, 359-368.
    • (2004) Trends Cell Biol , vol.14 , pp. 359-368
    • Amor, D.J.1    Kalitsis, P.2    Sumer, H.3    Choo, K.H.A.4
  • 15
    • 0032483564 scopus 로고    scopus 로고
    • Cse4p is a component of the core centromere of Sacharomyces cerevisiae
    • Meluh,P.B., Yang,P., Glowczewski,L., Koshland,D. and Smith,M.M. (1998) Cse4p is a component of the core centromere of Sacharomyces cerevisiae. Cell, 94, 607-613.
    • (1998) Cell , vol.94 , pp. 607-613
    • Meluh, P.B.1    Yang, P.2    Glowczewski, L.3    Koshland, D.4    Smith, M.M.5
  • 17
    • 0034910458 scopus 로고    scopus 로고
    • The role of Drosophila CID in kinetochore formation, cell-cycle progress and heterochromatin interactions
    • Blower,M.D. and Karpen,G.H. (2001) The role of Drosophila CID in kinetochore formation, cell-cycle progress and heterochromatin interactions. Nat. Cell Biol., 3, 730-739.
    • (2001) Nat. Cell Biol , vol.3 , pp. 730-739
    • Blower, M.D.1    Karpen, G.H.2
  • 19
    • 0025311047 scopus 로고
    • CENP-B: A major centromere protein located beneath the kinetochore
    • Cooke,C.A., Bernat,R.L. and Earnshaw,W.C. (1990) CENP-B: A major centromere protein located beneath the kinetochore. J. Cell Biol., 110, 1475-1488.
    • (1990) J. Cell Biol , vol.110 , pp. 1475-1488
    • Cooke, C.A.1    Bernat, R.L.2    Earnshaw, W.C.3
  • 20
    • 0024442796 scopus 로고
    • A human centromere antigen (CENP-B) interacts with a short specific sequence in alphoid DNA, a human centromeric satellite
    • Masumoto,H., Masukata,H., Muro,Y., Nozaki,N. and Okazaki,T. (1989) A human centromere antigen (CENP-B) interacts with a short specific sequence in alphoid DNA, a human centromeric satellite. J. Cell Biol. 109, 1963-1973.
    • (1989) J. Cell Biol , vol.109 , pp. 1963-1973
    • Masumoto, H.1    Masukata, H.2    Muro, Y.3    Nozaki, N.4    Okazaki, T.5
  • 21
    • 0027980680 scopus 로고
    • Distribution of CENP-B boxes reflected in CREST centromere antigenic sites on long-range α-satellite DNA arrays of human chromosome 21
    • Ikeno,M., Masumoto,H. and Okazaki,T. (1994) Distribution of CENP-B boxes reflected in CREST centromere antigenic sites on long-range α-satellite DNA arrays of human chromosome 21. Hum. Mol. Genet., 3, 1245-1257.
    • (1994) Hum. Mol. Genet , vol.3 , pp. 1245-1257
    • Ikeno, M.1    Masumoto, H.2    Okazaki, T.3
  • 22
    • 0031720004 scopus 로고    scopus 로고
    • In vitro assembly of the CENP-B/α-satellite DNA/core histone complex: CENP-B causes nucleosome positioning
    • Yoda,K., Ando,S., Okuda,A., Kikuchi,A. and Okazaki,T. (1998) In vitro assembly of the CENP-B/α-satellite DNA/core histone complex: CENP-B causes nucleosome positioning. Genes Cells, 3, 533-548.
    • (1998) Genes Cells , vol.3 , pp. 533-548
    • Yoda, K.1    Ando, S.2    Okuda, A.3    Kikuchi, A.4    Okazaki, T.5
  • 23
    • 0036121561 scopus 로고    scopus 로고
    • Cenp-A, Cenp-B and Cenp-C chromatin complex that contains the I-type alpha-satellite array constitutes the prekinetochore in HeLa cells
    • Ando,S., Yang,H., Nozaki,N., Okazaki,T. and Yoda,K. (2002) Cenp-A, Cenp-B and Cenp-C chromatin complex that contains the I-type alpha-satellite array constitutes the prekinetochore in HeLa cells. Mol. Cell Biol., 22, 2229-2241.
    • (2002) Mol. Cell Biol , vol.22 , pp. 2229-2241
    • Ando, S.1    Yang, H.2    Nozaki, N.3    Okazaki, T.4    Yoda, K.5
  • 24
    • 0035803581 scopus 로고    scopus 로고
    • Crystal structure of the CENP - B protein-DNA complex: The DNA-binding domains of CENP - B induce kinks in the CENP - B box DNA
    • Tanaka,Y., Nureki,O., Kurumizaka,H., Fukai,S., Kawaguchi,S., Ikuta,M., Iwahara,J., Okazaki,T. and Yokoyama,S. (2001) Crystal structure of the CENP - B protein-DNA complex: The DNA-binding domains of CENP - B induce kinks in the CENP - B box DNA. EMBO J., 20, 6612-6618.
    • (2001) EMBO J , vol.20 , pp. 6612-6618
    • Tanaka, Y.1    Nureki, O.2    Kurumizaka, H.3    Fukai, S.4    Kawaguchi, S.5    Ikuta, M.6    Iwahara, J.7    Okazaki, T.8    Yokoyama, S.9
  • 25
    • 0037049465 scopus 로고    scopus 로고
    • CENP-B box is required for de novo centromere chromatin assembly on human alphoid DNA
    • Ohzeki,J., Nakano,M., Okada,T. and Masumoto,H. (2002) CENP-B box is required for de novo centromere chromatin assembly on human alphoid DNA. J. Cell Biol., 159, 765-775.
    • (2002) J. Cell Biol , vol.159 , pp. 765-775
    • Ohzeki, J.1    Nakano, M.2    Okada, T.3    Masumoto, H.4
  • 26
    • 33947153944 scopus 로고    scopus 로고
    • A minimal CENP-A core is required for nucleation and maintenance of a functional human centromere
    • Okamoto,Y., Nakano,M., Ohzeki,J., Larionov,V. and Masumoto,H. (2007) A minimal CENP-A core is required for nucleation and maintenance of a functional human centromere. EMBO J., 26, 1279-1291.
    • (2007) EMBO J , vol.26 , pp. 1279-1291
    • Okamoto, Y.1    Nakano, M.2    Ohzeki, J.3    Larionov, V.4    Masumoto, H.5
  • 28
    • 0026520050 scopus 로고
    • Identification of a subdomain of CENP-B that is necessary and sufficient for localisation to the human centromere
    • Pluta,A.F., Saitoh,N., Goldberg,I. and Earnshaw,W.C. (1992) Identification of a subdomain of CENP-B that is necessary and sufficient for localisation to the human centromere. J. Cell Biol., 116 1081-1093.
    • (1992) J. Cell Biol , vol.116 , pp. 1081-1093
    • Pluta, A.F.1    Saitoh, N.2    Goldberg, I.3    Earnshaw, W.C.4
  • 30
    • 0028871185 scopus 로고
    • Analysis of protein-DNA and protein-protein interactions of centromere protein B (CENP-B) and properties of the DNA-CENP-B complex in the cell cycle
    • Kitagawa,K., Masumoto,H., Ikeda,M. and Okazaki,T. (1995) Analysis of protein-DNA and protein-protein interactions of centromere protein B (CENP-B) and properties of the DNA-CENP-B complex in the cell cycle. Mol. Cell Biol., 15, 1602-1612.
    • (1995) Mol. Cell Biol , vol.15 , pp. 1602-1612
    • Kitagawa, K.1    Masumoto, H.2    Ikeda, M.3    Okazaki, T.4
  • 31
    • 29244481979 scopus 로고    scopus 로고
    • Human centromere protein B induces translational positioning of nucleosomes on α-satellite sequences
    • Tanaka,Y., Tachiwana,H., Yoda,K., Masumoto,H. and Okazaki,T. (2005) Human centromere protein B induces translational positioning of nucleosomes on α-satellite sequences. J. Biol. Chem., 280, 41609-41618.
    • (2005) J. Biol. Chem , vol.280 , pp. 41609-41618
    • Tanaka, Y.1    Tachiwana, H.2    Yoda, K.3    Masumoto, H.4    Okazaki, T.5
  • 32
    • 0021806832 scopus 로고
    • Ant-ikinetochore antibodies: Use as probes for inactive centromeres
    • Merry,D.E., Pathak,S., Hsu,T.C. and Brinkley,B.R. (1985) Ant-ikinetochore antibodies: Use as probes for inactive centromeres. Am. J. Hum. Genet., 37, 425-430.
    • (1985) Am. J. Hum. Genet , vol.37 , pp. 425-430
    • Merry, D.E.1    Pathak, S.2    Hsu, T.C.3    Brinkley, B.R.4
  • 33
    • 0022254326 scopus 로고
    • Three related centromere proteins are absent from the inactive centromere of a stable isodicentric chromosome
    • Earnshaw,W.C. and Migeon,B.R. (1985) Three related centromere proteins are absent from the inactive centromere of a stable isodicentric chromosome. Chromosoma, 92, 290-296.
    • (1985) Chromosoma , vol.92 , pp. 290-296
    • Earnshaw, W.C.1    Migeon, B.R.2
  • 34
    • 0024333605 scopus 로고
    • Visualisation of centrometric proteins CENP-B and CENP-C on a stable dicentric chromosome in cytological spreads
    • Earnshaw,W.C., Ratrie,H. 3rd and Stetten,G. (1989) Visualisation of centrometric proteins CENP-B and CENP-C on a stable dicentric chromosome in cytological spreads. Chromosoma, 98, 1-12.
    • (1989) Chromosoma , vol.98 , pp. 1-12
    • Earnshaw, W.C.1    Ratrie 3rd, H.2    Stetten, G.3
  • 39
    • 0028287114 scopus 로고
    • CENP-C is required for maintaining proper kinetochore size and for a timely transition to anaphase
    • Tomkiel,J., Cooke,C.A., Saitoh,H., Bernat,R.L. and Earnshaw,W.C. (1994) CENP-C is required for maintaining proper kinetochore size and for a timely transition to anaphase. J. Cell Biol., 125, 531-545.
    • (1994) J. Cell Biol , vol.125 , pp. 531-545
    • Tomkiel, J.1    Cooke, C.A.2    Saitoh, H.3    Bernat, R.L.4    Earnshaw, W.C.5
  • 40
    • 0029927081 scopus 로고    scopus 로고
    • Identification of overlapping DNA-binding and centromere-targeting domains in the human kinetochore protein CENP-C
    • Yang,C.H., Tomkiel,J., Saitoh,H., Johnson,D.H. and Earnshaw,W.C. (1996) Identification of overlapping DNA-binding and centromere-targeting domains in the human kinetochore protein CENP-C. Mol. Cell Biol., 16, 3576-3586.
    • (1996) Mol. Cell Biol , vol.16 , pp. 3576-3586
    • Yang, C.H.1    Tomkiel, J.2    Saitoh, H.3    Johnson, D.H.4    Earnshaw, W.C.5
  • 41
    • 0028077549 scopus 로고
    • Human centromere protein C (CENP-C) is a DNA-binding protein which possesses a novel DNA-binding motif
    • Sugimot,K., Yata,H., Muro,Y. and Himeno,M. (1994) Human centromere protein C (CENP-C) is a DNA-binding protein which possesses a novel DNA-binding motif. J. Biochem., 116, 877-881.
    • (1994) J. Biochem , vol.116 , pp. 877-881
    • Sugimot, K.1    Yata, H.2    Muro, Y.3    Himeno, M.4
  • 43
    • 1242294403 scopus 로고    scopus 로고
    • CENP-B interacts with CENP-C domains containing Mif2 regions responsible for centromere localization
    • Suzuki,N., Nagano,M., Nozaki,N., Egashira,S., Okazaki,T. and Masumoto,H. (2004) CENP-B interacts with CENP-C domains containing Mif2 regions responsible for centromere localization. J. Biol. Chem., 279 5934-5946.
    • (2004) J. Biol. Chem , vol.279 , pp. 5934-5946
    • Suzuki, N.1    Nagano, M.2    Nozaki, N.3    Egashira, S.4    Okazaki, T.5    Masumoto, H.6
  • 45
    • 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
  • 46
    • 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
  • 47
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger,K., Mäder,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    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 48
    • 0034711232 scopus 로고    scopus 로고
    • The core histone N-termini function independently of linker histones during chromatin condensation
    • Carruthers,L.M. and Hansen,J.C. (2000) The core histone N-termini function independently of linker histones during chromatin condensation. J. Biol. Chem., 275, 37285-37290.
    • (2000) J. Biol. Chem , vol.275 , pp. 37285-37290
    • Carruthers, L.M.1    Hansen, J.C.2
  • 49
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • Woodcock,C.L., Skoutchi,A.I. and Fan,Y. (2006) Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res., 14, 17-25.
    • (2006) Chromosome Res , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoutchi, A.I.2    Fan, Y.3
  • 50
    • 33745020770 scopus 로고    scopus 로고
    • Determinants of histone H1 mobility and chromatin binding in living cells
    • Catez,F., Ueda,T. and Bustin,M. (2006) Determinants of histone H1 mobility and chromatin binding in living cells. Nat. Struct. Mol. Biol., 13, 305-310.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 305-310
    • Catez, F.1    Ueda, T.2    Bustin, M.3
  • 51
    • 0026517738 scopus 로고
    • A relationship between the helical twist of DNA and the ordered positioning of nucleosomes in all eukaryotic cells
    • Widom,J. (1992) A relationship between the helical twist of DNA and the ordered positioning of nucleosomes in all eukaryotic cells. Proc. Natl. Acad. Sci. USA, 89, 1095-1099.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1095-1099
    • Widom, J.1
  • 52
    • 34548267126 scopus 로고    scopus 로고
    • Tetrameric structure of centromeric nucleosomes in interphase Drosophila cells
    • Dalal,Y., Wang,H., Lindsay,S. and Henikoff,S. (2007) Tetrameric structure of centromeric nucleosomes in interphase Drosophila cells. PLoS Biol., 5, e218.
    • (2007) PLoS Biol , vol.5
    • Dalal, Y.1    Wang, H.2    Lindsay, S.3    Henikoff, S.4
  • 53
    • 34250316190 scopus 로고    scopus 로고
    • Scm3 is essential to recruit the histone H3 variant Cse4 to centromeres and to maintain a functional kinetochore
    • Camahort,R., Li,B., Florens,L., Sanson,S.K., Washburn,M.P. and Gerton,J.L. (2007) Scm3 is essential to recruit the histone H3 variant Cse4 to centromeres and to maintain a functional kinetochore. Mol. Cell, 26, 853-865.
    • (2007) Mol. Cell , vol.26 , pp. 853-865
    • Camahort, R.1    Li, B.2    Florens, L.3    Sanson, S.K.4    Washburn, M.P.5    Gerton, J.L.6
  • 54
    • 34250173486 scopus 로고    scopus 로고
    • Nonhistone Scm3 and histones CenH3-H4 assemble the core of centromere-specific nucleosomes
    • Mizuguchi,G., Xiao,H., Wisniewski,J., Smith,M.M. and Wu,C. (2007) Nonhistone Scm3 and histones CenH3-H4 assemble the core of centromere-specific nucleosomes. Cell, 129, 1153-1164.
    • (2007) Cell , vol.129 , pp. 1153-1164
    • Mizuguchi, G.1    Xiao, H.2    Wisniewski, J.3    Smith, M.M.4    Wu, C.5
  • 55
    • 34547112848 scopus 로고    scopus 로고
    • Scm3, an essential S. cerevisiae centromere protein required for G2/M progression and Cse4 localization
    • Stoler,S., Rogers,K., Weitze,S., Morey,L., Fitzgerald-Hayes,M. and Baker,R.E. (2007) Scm3, an essential S. cerevisiae centromere protein required for G2/M progression and Cse4 localization. Proc. Natl. Acad. Sci. USA, 104, 10571-10576.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10571-10576
    • Stoler, S.1    Rogers, K.2    Weitze, S.3    Morey, L.4    Fitzgerald-Hayes, M.5    Baker, R.E.6
  • 57
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organisation of the nucleosome and of the salt dependent superstructure of chromatin
    • Thoma,F., Koller,T. and Klug,A. (1979) Involvement of histone H1 in the organisation of the nucleosome and of the salt dependent superstructure of chromatin. J. Cell Biol., 83, 403-427.
    • (1979) J. Cell Biol , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 58
    • 0030956032 scopus 로고    scopus 로고
    • Histone structure and the organuisation of the nucleosome
    • Ramakrishnan,V. (1997) Histone structure and the organuisation of the nucleosome. Annu. Rev. Biophys. Biomol. Struct., 26, 83-112.
    • (1997) Annu. Rev. Biophys. Biomol. Struct , vol.26 , pp. 83-112
    • Ramakrishnan, V.1
  • 59
    • 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
  • 60
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • Hendzel,M.J., Lever,M.A., Crawford,E. and Thǹg,J.P. (2004) The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. J. Biol. Chem., 279, 20028-20034.
    • (2004) J. Biol. Chem , vol.279 , pp. 20028-20034
    • Hendzel, M.J.1    Lever, M.A.2    Crawford, E.3    Thǹg, J.P.4
  • 62
    • 0034680588 scopus 로고    scopus 로고
    • Two DNA binding sites on the globular domain of histone H5 are required for binding to both bulk and 5S reconstituted nucleosomes
    • Duggan,M.M. and Thomas,J.O. (2000) Two DNA binding sites on the globular domain of histone H5 are required for binding to both bulk and 5S reconstituted nucleosomes. J. Mol. Biol., 304, 21-33.
    • (2000) J. Mol. Biol , vol.304 , pp. 21-33
    • Duggan, M.M.1    Thomas, J.O.2
  • 63
    • 0033151772 scopus 로고    scopus 로고
    • Histone H1: Location and role
    • Thomas,J.O. (1999) Histone H1: Location and role. Curr. Opin. Cell Biol., 11, 312-317.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 312-317
    • Thomas, J.O.1
  • 64
    • 0032972980 scopus 로고    scopus 로고
    • The location of linker histone in the nucleosome
    • Travers,A.A. (1999) The location of linker histone in the nucleosome. Trends Biochem. Sci., 24, 4-7.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 4-7
    • Travers, A.A.1
  • 65
    • 33746845357 scopus 로고    scopus 로고
    • Localisation of linker histone in Chromatosomes by cryo-atomic force microscopy
    • Sheng,S., Czajkowsky,D.M. and Shao,Z. (2006) Localisation of linker histone in Chromatosomes by cryo-atomic force microscopy. Biophys. J. 91, L35-L37.
    • (2006) Biophys. J , vol.91
    • Sheng, S.1    Czajkowsky, D.M.2    Shao, Z.3
  • 66
    • 33644800314 scopus 로고    scopus 로고
    • Mapping the interaction surface of the linker H1 with the nucleosome of native chromatin in vivo
    • Brown,D., Izard,T. and Misteli,T. (2006) Mapping the interaction surface of the linker H1 with the nucleosome of native chromatin in vivo. Nat. Struct. Mol. Biol., 13, 250-255.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 250-255
    • Brown, D.1    Izard, T.2    Misteli, T.3
  • 67
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever,M.A., Thǹg,J.P., Sun,X. and Hendzel,M.J. (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    Thǹg, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 68
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli,T., Gunjan,A., Hock,R., Bustin,M. and Brown,D.T. (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
  • 69
    • 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
  • 70
    • 12144283465 scopus 로고    scopus 로고
    • Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins
    • Chen,D., Dundr,M., Wang,C., Leung,A., Lamond,A., Misteli,T. and Huang,S. (2005) Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins. J. Cell Biol., 168 41-54.
    • (2005) J. Cell Biol , vol.168 , pp. 41-54
    • Chen, D.1    Dundr, M.2    Wang, C.3    Leung, A.4    Lamond, A.5    Misteli, T.6    Huang, S.7
  • 71
    • 0031022333 scopus 로고    scopus 로고
    • H1-mediated repression of transcription factor binding to a stably positioned nucleosome
    • Juan,L., Utley,R.T., Vignali,M., Bohm,L. and Workman,J.L. (1997) H1-mediated repression of transcription factor binding to a stably positioned nucleosome. J. Biol. Chem., 272, 3635-3640.
    • (1997) J. Biol. Chem , vol.272 , pp. 3635-3640
    • Juan, L.1    Utley, R.T.2    Vignali, M.3    Bohm, L.4    Workman, J.L.5
  • 72
    • 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 Hamkalo,B.A. (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
  • 73
    • 0035854055 scopus 로고    scopus 로고
    • Histone H1 diversity: Bridging regulatory signals to linker histone function
    • Khochbin,S. (2001) Histone H1 diversity: Bridging regulatory signals to linker histone function. Gene, 271, 1-12.
    • (2001) Gene , vol.271 , pp. 1-12
    • Khochbin, S.1
  • 74
    • 44649186259 scopus 로고    scopus 로고
    • The histone H1 family: Specific members, specific functions?
    • Izzo,A., Kamieniarz,K. and Schneider,R. (2008) The histone H1 family: specific members, specific functions? Biol. Chem., 389, 333-343.
    • (2008) Biol. Chem , vol.389 , pp. 333-343
    • Izzo, A.1    Kamieniarz, K.2    Schneider, R.3
  • 75
    • 0041886608 scopus 로고    scopus 로고
    • Histone H1 and the dynamic regulation of chromatin function
    • Brown,D.T. (2003) Histone H1 and the dynamic regulation of chromatin function. Biochem. Cell Biol., 81, 221-227.
    • (2003) Biochem. Cell Biol , vol.81 , pp. 221-227
    • Brown, D.T.1
  • 76
    • 3843120056 scopus 로고    scopus 로고
    • What functions do linker histones provide?
    • Harvey,A.C. and Downs,J.A. (2004) What functions do linker histones provide? Mol. Microbiol., 53, 771-775.
    • (2004) Mol. Microbiol , vol.53 , pp. 771-775
    • Harvey, A.C.1    Downs, J.A.2
  • 77
    • 0037092507 scopus 로고    scopus 로고
    • Extracellular matrix histone H1 binds to perlecan, is present in regenerating skeletal muscle and stimulates myoblast proliferation
    • Henriques,J.P., Casar,J.C., Fuentealba,L., Carey,D.J. and Brandan,E. (2002) Extracellular matrix histone H1 binds to perlecan, is present in regenerating skeletal muscle and stimulates myoblast proliferation. J. Cell Sci., 115, 2041-2051.
    • (2002) J. Cell Sci , vol.115 , pp. 2041-2051
    • Henriques, J.P.1    Casar, J.C.2    Fuentealba, L.3    Carey, D.J.4    Brandan, E.5
  • 78
    • 0037099013 scopus 로고    scopus 로고
    • A novel linker histone-like protein is associated with cytoplasmic filaments in C. elegans
    • Jedrusik,M.A., Vogt,S., Claus,P. and Schulze,E. (2002) A novel linker histone-like protein is associated with cytoplasmic filaments in C. elegans. J. Cell Sci., 115, 2881-2891.
    • (2002) J. Cell Sci , vol.115 , pp. 2881-2891
    • Jedrusik, M.A.1    Vogt, S.2    Claus, P.3    Schulze, E.4
  • 80
    • 0037490067 scopus 로고    scopus 로고
    • Suppression of homologous recombination by the S. cerevisiae linker histone
    • Downs,J.A., Kosmidou,E., Morgan,A. and Jackson,S.P. (2003) Suppression of homologous recombination by the S. cerevisiae linker histone. Mol. Cell., 11, 1685-1692.
    • (2003) Mol. Cell , vol.11 , pp. 1685-1692
    • Downs, J.A.1    Kosmidou, E.2    Morgan, A.3    Jackson, S.P.4
  • 81
    • 39149098441 scopus 로고    scopus 로고
    • H1 histone subtype constitution and phosphorylation state of the ageing cell system of human peripheral blood lymphocytes
    • Happel,N., Doenecke,D., Sekeri-Pataryas,K.E. and Sourlingas,T.G. (2008) H1 histone subtype constitution and phosphorylation state of the ageing cell system of human peripheral blood lymphocytes. Exp. Gerontol., 43, 184-199.
    • (2008) Exp. Gerontol , vol.43 , pp. 184-199
    • Happel, N.1    Doenecke, D.2    Sekeri-Pataryas, K.E.3    Sourlingas, T.G.4
  • 82
    • 33947524604 scopus 로고    scopus 로고
    • Histone variants - the structure behind the function
    • Ausio,J. (2006) Histone variants - the structure behind the function. Brief Funct. Genomic. Proteomic., 5, 228-243.
    • (2006) Brief Funct. Genomic. Proteomic , vol.5 , pp. 228-243
    • Ausio, J.1
  • 83
    • 0031030788 scopus 로고    scopus 로고
    • Characterization of the H1.5 gene completes the set of human H1 subtype genes
    • Albig,W., Meergans,T. and Doenecke,D. (1997) Characterization of the H1.5 gene completes the set of human H1 subtype genes. Gene, 184, 141-148.
    • (1997) Gene , vol.184 , pp. 141-148
    • Albig, W.1    Meergans, T.2    Doenecke, D.3
  • 84
    • 0034673371 scopus 로고    scopus 로고
    • Histone H1 variants play individual roles in transcription regulation in the DT40 chicken B cell line
    • Takami,Y., Nishi,R. and Nakayama,T. (2000) Histone H1 variants play individual roles in transcription regulation in the DT40 chicken B cell line. Biochem. Biophys. Res. Commun., 268, 501-508.
    • (2000) Biochem. Biophys. Res. Commun , vol.268 , pp. 501-508
    • Takami, Y.1    Nishi, R.2    Nakayama, T.3
  • 86
    • 14644388222 scopus 로고    scopus 로고
    • The dynamics of histone H1 function in chromatin
    • Bustin,M., Catez,F. and Lim,J.-H. (2005) The dynamics of histone H1 function in chromatin. Mol. Cell, 17, 617-620.
    • (2005) Mol. Cell , vol.17 , pp. 617-620
    • Bustin, M.1    Catez, F.2    Lim, J.-H.3
  • 87
    • 33845687060 scopus 로고    scopus 로고
    • Loss of linker histone H1 in cellular senescence
    • Funayama,R., Saito,M., Tanobe,H. and Ishikawa,F. (2006) Loss of linker histone H1 in cellular senescence. J. Cell Biol., 175, 869-880.
    • (2006) J. Cell Biol , vol.175 , pp. 869-880
    • Funayama, R.1    Saito, M.2    Tanobe, H.3    Ishikawa, F.4
  • 88
    • 0035164583 scopus 로고    scopus 로고
    • Distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin II: Distribution in human adult fibroblasts
    • Parseghian,M.H., Newcomb,R.L. and Hamkalo,B.A. (2001) Distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin II: Distribution in human adult fibroblasts. J. Cell. Biochem., 83, 643-659.
    • (2001) J. Cell. Biochem , vol.83 , pp. 643-659
    • Parseghian, M.H.1    Newcomb, R.L.2    Hamkalo, B.A.3
  • 89
    • 35148817893 scopus 로고    scopus 로고
    • G1 phase-dependent nucleolar accumulation of human histone H1x
    • Stoldt,S., Wenzel,D., Schulze,E., Doenecke,D. and Happel,N. (2007) G1 phase-dependent nucleolar accumulation of human histone H1x. Biol. Cell, 99, 541-552.
    • (2007) Biol. Cell , vol.99 , pp. 541-552
    • Stoldt, S.1    Wenzel, D.2    Schulze, E.3    Doenecke, D.4    Happel, N.5
  • 90
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu,C.D. and Kerppola,T.K. (2003) Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol., 21, 539-545.
    • (2003) Nat. Biotechnol , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 91
    • 33644861986 scopus 로고    scopus 로고
    • Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions
    • Shyu,Y.J., Liu,H., Deng,X. and Hu,C.D. (2006) Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. Biotechniques, 40, 61-66.
    • (2006) Biotechniques , vol.40 , pp. 61-66
    • Shyu, Y.J.1    Liu, H.2    Deng, X.3    Hu, C.D.4
  • 92
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • Kerppola,T.K. (2008) Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu. Rev. Biophys., 37, 465-487.
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 93
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy,A. (2001) Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods, 24 289-296.
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.1
  • 94
    • 0037238461 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser
    • Karpova,T.S., Baumann,C.T., He,L., Wu,X., Grammer,A., Lipsky,P., Hager,G.L. and McNally,J.G. (2003) Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J. Microscopy, 209, 56-70.
    • (2003) J. Microscopy , vol.209 , pp. 56-70
    • Karpova, T.S.1    Baumann, C.T.2    He, L.3    Wu, X.4    Grammer, A.5    Lipsky, P.6    Hager, G.L.7    McNally, J.G.8
  • 95
    • 3242703137 scopus 로고    scopus 로고
    • Functional complementation of human centromere Protein A (CENP-A) by Cse4 from S. cerevisiae
    • Wieland,G., Orthaus,S., Ohndorf,S., Diekmann,S. and Hemmerich,P. (2004) Functional complementation of human centromere Protein A (CENP-A) by Cse4 from S. cerevisiae. Mol. Cell Biol., 24, 6620-6630.
    • (2004) Mol. Cell Biol , vol.24 , pp. 6620-6630
    • Wieland, G.1    Orthaus, S.2    Ohndorf, S.3    Diekmann, S.4    Hemmerich, P.5
  • 96
    • 0031430689 scopus 로고    scopus 로고
    • Varied expression patterns of human H1 histone genes in different cell lines
    • Meergans,T., Albig,W. and Doenecke,D. (1997) Varied expression patterns of human H1 histone genes in different cell lines. DNA Cell Biol., 16, 1041-1049.
    • (1997) DNA Cell Biol , vol.16 , pp. 1041-1049
    • Meergans, T.1    Albig, W.2    Doenecke, D.3
  • 97
    • 0033850576 scopus 로고    scopus 로고
    • The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: Distribution in human fetal fibroblasts
    • Parseghian,M.H., Newcomb,R.L., Winokur,S.T. and Hamkalo,B.A. (2000) The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: Distribution in human fetal fibroblasts. Chromosome Res., 8, 405-424.
    • (2000) Chromosome Res , vol.8 , pp. 405-424
    • Parseghian, M.H.1    Newcomb, R.L.2    Winokur, S.T.3    Hamkalo, B.A.4
  • 98
    • 34347222583 scopus 로고    scopus 로고
    • Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells
    • Kerppola,T.K. (2006) Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat. Protoc., 1, 1278-1286.
    • (2006) Nat. Protoc , vol.1 , pp. 1278-1286
    • Kerppola, T.K.1
  • 99
    • 0036241055 scopus 로고    scopus 로고
    • Visulisation of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu,C.D., Chinenov,Y. and Kerppola,T.K. (2002) Visulisation of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell, 9, 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 100
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson,G.H., Knobel,S.M., Sharif,W.D., Kain,S.R. and Piston,D.W. (1997) Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J., 73, 2782-2790.
    • (1997) Biophys. J , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 101
    • 0033021944 scopus 로고    scopus 로고
    • Three photoconvertible forms of green fluorescent protein identified by spectral hole-burning
    • Creemers,T.M., Lock,A.J., Subramaniam,V., Jovin,T.M. and Völker,S. (1999) Three photoconvertible forms of green fluorescent protein identified by spectral hole-burning. Nat. Struct. Biol., 6, 557-560.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 557-560
    • Creemers, T.M.1    Lock, A.J.2    Subramaniam, V.3    Jovin, T.M.4    Völker, S.5
  • 102
    • 0034877121 scopus 로고    scopus 로고
    • Light-induced flickering of DsRed provides evidence for distinct and interconvertible fluorescent states
    • Malvezzi-Campeggi,F., Jahnz,M., Heinze,K.G., Dittrich,P. and Schwille,P. (2001) Light-induced flickering of DsRed provides evidence for distinct and interconvertible fluorescent states. Biophys. J., 81, 882-887.
    • (2001) Biophys. J , vol.81 , pp. 882-887
    • Malvezzi-Campeggi, F.1    Jahnz, M.2    Heinze, K.G.3    Dittrich, P.4    Schwille, P.5
  • 103
    • 0034053143 scopus 로고    scopus 로고
    • One-and two-photon excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins
    • Volkmer,A., Subramaniam,V., Birch,D. and Jovin,T. (2000) One-and two-photon excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins. Biophys. J., 78, 1589-1598.
    • (2000) Biophys. J , vol.78 , pp. 1589-1598
    • Volkmer, A.1    Subramaniam, V.2    Birch, D.3    Jovin, T.4
  • 104
    • 33750708280 scopus 로고    scopus 로고
    • Sensitivity of CFP/YFP and GFP/mCherry pairs to donor photobleaching on FRET determination by fluorescence lifetime imaging microscopy in living cells
    • Tramier,M., Zahid,M., Mevel,J.C., Masse,M.J. and Coppey-Moisan,M. (2006) Sensitivity of CFP/YFP and GFP/mCherry pairs to donor photobleaching on FRET determination by fluorescence lifetime imaging microscopy in living cells. Microsc. Res. Tech., 69, 933-939.
    • (2006) Microsc. Res. Tech , vol.69 , pp. 933-939
    • Tramier, M.1    Zahid, M.2    Mevel, J.C.3    Masse, M.J.4    Coppey-Moisan, M.5
  • 105
    • 39449096363 scopus 로고    scopus 로고
    • KNL1 and the CENP-H/I/K comoplex coordinately direct kinetochore assembly in vertebrates
    • Cheeseman,I.M., Hori,T., Fukagawa,T. and Desai,A. (2008) KNL1 and the CENP-H/I/K comoplex coordinately direct kinetochore assembly in vertebrates. Mol. Biol. Cell, 19, 587-594.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 587-594
    • Cheeseman, I.M.1    Hori, T.2    Fukagawa, T.3    Desai, A.4
  • 106
  • 107
    • 0036149461 scopus 로고    scopus 로고
    • An inducible helix-Gly-Gly-helix motif in the N-terminal domain of histone H1e: A CD and NMR study
    • Vila,R., Ponte,I., Jimenez,M.A., Rico,M. and Suau,P. (2002) An inducible helix-Gly-Gly-helix motif in the N-terminal domain of histone H1e: A CD and NMR study. Protein Sci., 11, 214-220.
    • (2002) Protein Sci , vol.11 , pp. 214-220
    • Vila, R.1    Ponte, I.2    Jimenez, M.A.3    Rico, M.4    Suau, P.5
  • 110
    • 1542330121 scopus 로고    scopus 로고
    • Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localised with the centromeric region in interphase
    • Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K. (2004) Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localised with the centromeric region in interphase. Genes Cells, 9, 105-120.
    • (2004) Genes Cells , vol.9 , pp. 105-120
    • Obuse, C.1    Yang, H.2    Nozaki, N.3    Goto, S.4    Okazaki, T.5    Yoda, K.6
  • 111
    • 26844581712 scopus 로고    scopus 로고
    • Characterisation of human histone H1x
    • Happel,N., Schulze,E. and Doenecke,D. (2005) Characterisation of human histone H1x. Biol. Chem., 386, 541-551.
    • (2005) Biol. Chem , vol.386 , pp. 541-551
    • Happel, N.1    Schulze, E.2    Doenecke, D.3
  • 112
    • 34547106299 scopus 로고    scopus 로고
    • H1x with different properties from other linker histones is required for mitotic progression
    • Takata,H., Matsunaga,S., Moriomoto,A., Ono-Maniwa,R., Uchiyama,S. and Fukui,K. (2007) H1x with different properties from other linker histones is required for mitotic progression. FEBS Lett., 581, 3783-3788.
    • (2007) FEBS Lett , vol.581 , pp. 3783-3788
    • Takata, H.1    Matsunaga, S.2    Moriomoto, A.3    Ono-Maniwa, R.4    Uchiyama, S.5    Fukui, K.6
  • 113
    • 0035833993 scopus 로고    scopus 로고
    • Distinctive higher-order chromatin structure at mammalian centromeres
    • Gilbert,N. and Allan,J. (2001) Distinctive higher-order chromatin structure at mammalian centromeres. Proc. Natl. Acad. Sci. USA, 98, 11949-11954.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11949-11954
    • Gilbert, N.1    Allan, J.2
  • 115
    • 33846199534 scopus 로고    scopus 로고
    • Centromere identity maintained by nucleosomes assembled with histone H3 containing the CENP-A targeting domain
    • Black,B.E., Jansen,L.E.T., Maddox,P.S., Foltz,D.R., Desai,A.B., Shah,J.V. and Cleveland,D.W. (2007) Centromere identity maintained by nucleosomes assembled with histone H3 containing the CENP-A targeting domain. Mol. Cell, 25, 309-322.
    • (2007) Mol. Cell , vol.25 , pp. 309-322
    • Black, B.E.1    Jansen, L.E.T.2    Maddox, P.S.3    Foltz, D.R.4    Desai, A.B.5    Shah, J.V.6    Cleveland, D.W.7
  • 116
    • 0023430518 scopus 로고
    • Anionic regions in nuclear proteins
    • Earnshaw,W.C. (1987) Anionic regions in nuclear proteins. J. Cell Biol., 105, 1479-1482.
    • (1987) J. Cell Biol , vol.105 , pp. 1479-1482
    • Earnshaw, W.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.