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Volumn 271, Issue 17, 2004, Pages 3459-3469

The role of histones in chromatin remodelling during mammalian spermiogenesis

Author keywords

Bromodomain; Chromodomain; Epigenetics; Histone chaperone; Histone structure

Indexed keywords

HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; PROTAMINE;

EID: 4544376137     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04266.x     Document Type: Review
Times cited : (216)

References (97)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F. & Richmond, T.J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 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
  • 3
    • 0344198456 scopus 로고    scopus 로고
    • Chromatin remodeling by ATP-dependent molecular machines
    • Lusser, A. & Kadonaga, J.T. (2003) Chromatin remodeling by ATP-dependent molecular machines. Bioessays 25, 1192-1200.
    • (2003) Bioessays , vol.25 , pp. 1192-1200
    • Lusser, A.1    Kadonaga, J.T.2
  • 4
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner, B.M. (1993) Decoding the nucleosome. Cell 75, 5-8.
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 5
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D. & Allis, C.D. (2000) The language of covalent histone modifications. Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 6
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner, B.M. (2002) Cellular memory and the histone code. Cell 111, 285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 7
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: From genomic organization to genomic regulation
    • Khorasanizadeh, S. (2004) The nucleosome: from genomic organization to genomic regulation. Cell 116, 259-272.
    • (2004) Cell , vol.116 , pp. 259-272
    • Khorasanizadeh, S.1
  • 8
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • Malik, H.S. & Henikoff, S. (2003) Phylogenomics of the nucleosome. Nat. Struct. Biol. 10, 882-891.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 9
    • 0042232734 scopus 로고    scopus 로고
    • A haploid affair: Core histone transitions during spermatogenesis
    • Lewis, J.D., Abbott, D.W. & Ausio, J. (2003) A haploid affair: core histone transitions during spermatogenesis. Biochem. Cell Biol. 81, 131-140.
    • (2003) Biochem. Cell Biol. , vol.81 , pp. 131-140
    • Lewis, J.D.1    Abbott, D.W.2    Ausio, J.3
  • 10
    • 0029770092 scopus 로고    scopus 로고
    • Expression of the mouse testicular histone gene Hit during spermatogenesis
    • Drabent, B., Bode, C., Bramlage, B. & Doenecke, D. (1996) Expression of the mouse testicular histone gene Hit during spermatogenesis. Histochem. Cell Biol. 106, 247-251.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 247-251
    • Drabent, B.1    Bode, C.2    Bramlage, B.3    Doenecke, D.4
  • 11
    • 0347504935 scopus 로고    scopus 로고
    • Isolation and characterization of a novel cDNA encoding a DNA-binding protein (Hils1) specifically expressed in testicular haploid germ cells
    • Iguchi, N., Tanaka, H., Yomogida, K. & Nishimune, Y. (2003) Isolation and characterization of a novel cDNA encoding a DNA-binding protein (Hils1) specifically expressed in testicular haploid germ cells. Int. J. Androl. 26, 354-365.
    • (2003) Int. J. Androl. , vol.26 , pp. 354-365
    • Iguchi, N.1    Tanaka, H.2    Yomogida, K.3    Nishimune, Y.4
  • 12
    • 0025049911 scopus 로고
    • Structural and functional analysis of the rat testis-specific histone Hit gene
    • Grimes, S.R., Wolfe, S.A., Anderson, J.V., Stein, G.S. & Stein, J.L. (1990) Structural and functional analysis of the rat testis-specific histone Hit gene. J. Cell Biochem. 44, 1-17.
    • (1990) J. Cell Biochem. , vol.44 , pp. 1-17
    • Grimes, S.R.1    Wolfe, S.A.2    Anderson, J.V.3    Stein, G.S.4    Stein, J.L.5
  • 14
    • 0033921812 scopus 로고    scopus 로고
    • Spermatogenesis proceeds normally in mice without linker histone Hlt
    • Drabent, B., Saftig, P., Bode, C. & Doenecke, D. (2000) Spermatogenesis proceeds normally in mice without linker histone Hlt. Histochem. Cell Biol. 113, 433-442.
    • (2000) Histochem. Cell Biol. , vol.113 , pp. 433-442
    • Drabent, B.1    Saftig, P.2    Bode, C.3    Doenecke, D.4
  • 15
    • 0033997968 scopus 로고    scopus 로고
    • Normal spermatogenesis in mice lacking the testis-specific linker histone Hlt
    • Lin, Q., Sirotkin, A. & Skoultchi, A.T. (2000) Normal spermatogenesis in mice lacking the testis-specific linker histone Hlt. Mol. Cell Biol. 20, 2122-2128.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2122-2128
    • Lin, Q.1    Sirotkin, A.2    Skoultchi, A.T.3
  • 16
    • 0035145808 scopus 로고    scopus 로고
    • Mice with a targeted disruption of the Hit gene are fertile and undergo normal changes in structural chromosomal proteins during spermiogenesis
    • Fantz, D.A., Hatfield, W.R., Horvath, G., Kistler, M.K. & Kistler, W.S. (2001) Mice with a targeted disruption of the Hit gene are fertile and undergo normal changes in structural chromosomal proteins during spermiogenesis. Biol. Reprod. 64, 425-431.
    • (2001) Biol. Reprod. , vol.64 , pp. 425-431
    • Fantz, D.A.1    Hatfield, W.R.2    Horvath, G.3    Kistler, M.K.4    Kistler, W.S.5
  • 18
    • 0028860948 scopus 로고
    • DNA- and chromatin-condensing properties of rat testes Hla and Hlt compared to those of rat liver Hlbdec; Hlt is a poor condenser of chromatin
    • Khadake, J.R. & Rao, M.R. (1995) DNA- and chromatin-condensing properties of rat testes Hla and Hlt compared to those of rat liver Hlbdec; Hlt is a poor condenser of chromatin. Biochemistry 34, 15792-15801.
    • (1995) Biochemistry , vol.34 , pp. 15792-15801
    • Khadake, J.R.1    Rao, M.R.2
  • 19
    • 0022404576 scopus 로고
    • Histone variants in rat spermatogonia and primary spermatocytes
    • Meistrich, M.L., Bucci, L.R., Trostle-Weige, P.K. & Brock, W.A. (1985) Histone variants in rat spermatogonia and primary spermatocytes. Dev. Biol. 112, 230-340.
    • (1985) Dev. Biol. , vol.112 , pp. 230-340
    • Meistrich, M.L.1    Bucci, L.R.2    Trostle-Weige, P.K.3    Brock, W.A.4
  • 20
    • 0000053117 scopus 로고    scopus 로고
    • Testicular expression of the mouse histone H1.1 gene
    • Franke, K., Drabent, B. & Doenecke, D. (1998) Testicular expression of the mouse histone H1.1 gene. Histochem. Cell Biol. 109, 383-390.
    • (1998) Histochem. Cell Biol. , vol.109 , pp. 383-390
    • Franke, K.1    Drabent, B.2    Doenecke, D.3
  • 22
    • 2542462280 scopus 로고    scopus 로고
    • Reductions in linker histone levels are tolerated in developing spermatocytes but cause changes in specific gene expression
    • Lin, Q., Inselman, A., Han, X., Xu, H., Zhang, W., Handel, M.A. & Skoultchi, A.I. (2004) Reductions in linker histone levels are tolerated in developing spermatocytes but cause changes in specific gene expression. J. Biol. Chem. 279, 23525-23532.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23525-23532
    • Lin, Q.1    Inselman, A.2    Han, X.3    Xu, H.4    Zhang, W.5    Handel, M.A.6    Skoultchi, A.I.7
  • 23
    • 0042838274 scopus 로고    scopus 로고
    • HILS1 is a spermatid-specific linker histone H1-like protein implicated in chromatin remodeling during mammalian spermiogenesis
    • Yan, W., Ma, L., Burns, K.H. & Matzuk, M.M. (2003) HILS1 is a spermatid-specific linker histone H1-like protein implicated in chromatin remodeling during mammalian spermiogenesis. Proc. Natl Acad. Sci. USA 100, 10546-10551.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10546-10551
    • Yan, W.1    Ma, L.2    Burns, K.H.3    Matzuk, M.M.4
  • 25
    • 0030589491 scopus 로고    scopus 로고
    • Testis-specific expression of a novel human H3 histone gene
    • Witt, O., Albig, W. & Doenecke, D. (1996) Testis-specific expression of a novel human H3 histone gene. Exp. Cell Res. 229, 301-306.
    • (1996) Exp. Cell Res. , vol.229 , pp. 301-306
    • Witt, O.1    Albig, W.2    Doenecke, D.3
  • 26
    • 0021140807 scopus 로고
    • Isolation and characterization of TH3, a germ cell-specific variant of histone 3 in rat testis
    • Trostle-Weige, P.K., Meistrich, M.L., Brock, W.A. & Nishioka, K. (1984) Isolation and characterization of TH3, a germ cell-specific variant of histone 3 in rat testis. J. Biol. Chem. 259, 8769-8776.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8769-8776
    • Trostle-Weige, P.K.1    Meistrich, M.L.2    Brock, W.A.3    Nishioka, K.4
  • 27
    • 0036591877 scopus 로고    scopus 로고
    • Centromeres and variant histones: What, where, when and why?
    • Smith, M.M. (2002) Centromeres and variant histones: what, where, when and why? Curr. Opin. Cell Biol. 14, 279-285.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 279-285
    • Smith, M.M.1
  • 29
    • 0030729630 scopus 로고    scopus 로고
    • Differential expression of the murine histone genes H3.3A and H3.3B
    • Bramlage, B., Kosciessa, U. & Doenecke, D. (1997) Differential expression of the murine histone genes H3.3A and H3.3B. Differentiation 62, 13-20.
    • (1997) Differentiation , vol.62 , pp. 13-20
    • Bramlage, B.1    Kosciessa, U.2    Doenecke, D.3
  • 30
    • 0032739343 scopus 로고    scopus 로고
    • A retroviral gene trap insertion into the histone 3.3A gene causes partial neonatal lethality, stunted growth, neuromuscular deficits and male sub-fertility in transgenic mice
    • Couldrey, C., Carlton, M.B., Nolan, P.M., Colledge, W.H. & Evans, M.J. (1999) A retroviral gene trap insertion into the histone 3.3A gene causes partial neonatal lethality, stunted growth, neuromuscular deficits and male sub-fertility in transgenic mice. Hum. Mol. Genet. 8, 2489-2495.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2489-2495
    • Couldrey, C.1    Carlton, M.B.2    Nolan, P.M.3    Colledge, W.H.4    Evans, M.J.5
  • 31
    • 0030853167 scopus 로고    scopus 로고
    • The localization of histone H3.3 in germ line chromatin of Drosophila males as established with a histone H3.3-specific antiserum
    • Akhmanova, A., Miedema, K., Wang, Y., van Bruggen, M., Berden, J.H., Moudrianakis, E.N. & Hennig, W. (1997) The localization of histone H3.3 in germ line chromatin of Drosophila males as established with a histone H3.3-specific antiserum. Chromosoma 106, 335-347.
    • (1997) Chromosoma , vol.106 , pp. 335-347
    • Akhmanova, A.1    Miedema, K.2    Wang, Y.3    Van Bruggen, M.4    Berden, J.H.5    Moudrianakis, E.N.6    Hennig, W.7
  • 32
    • 1242342240 scopus 로고    scopus 로고
    • Histone H3.3 is enriched in covalent modifications associated with active chromatin
    • McKittrick, E., Gafken, P.R., Ahmad, K. & Henikoff, S. (2004) Histone H3.3 is enriched in covalent modifications associated with active chromatin. Proc. Natl Acad. Sci. USA 101, 1525-1530.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1525-1530
    • McKittrick, E.1    Gafken, P.R.2    Ahmad, K.3    Henikoff, S.4
  • 33
    • 0024522822 scopus 로고
    • S-phase-specific transcription regulatory elements are present in a replication-independent testis-specific H2B histone gene
    • Hwang, I. & Chae, C.B. (1989) S-phase-specific transcription regulatory elements are present in a replication-independent testis-specific H2B histone gene. Mol. Cell. Biol. 9, 1005-1013.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1005-1013
    • Hwang, I.1    Chae, C.B.2
  • 34
    • 0029979781 scopus 로고    scopus 로고
    • Molecular cloning of mouse somatic and testis-specific H2B histone genes containing a methylated CpG island
    • Choi, Y.C., Gu, W., Hecht, N.B., Feinberg, A.P. & Chae, C.B. (1996) Molecular cloning of mouse somatic and testis-specific H2B histone genes containing a methylated CpG island. DNA Cell Biol. 15, 495-504.
    • (1996) DNA Cell Biol. , vol.15 , pp. 495-504
    • Choi, Y.C.1    Gu, W.2    Hecht, N.B.3    Feinberg, A.P.4    Chae, C.B.5
  • 37
    • 0041856070 scopus 로고    scopus 로고
    • Somatic histones are components of the perinuclear theca in bovine spermatozoa
    • Tovich, P.R. & Oko, R.J. (2003) Somatic histones are components of the perinuclear theca in bovine spermatozoa. J. Biol. Chem. 278, 32431-32438.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32431-32438
    • Tovich, P.R.1    Oko, R.J.2
  • 38
    • 0035891432 scopus 로고    scopus 로고
    • The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis
    • Aul, R.B. & Oko, R.J. (2001) The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis. Dev. Biol. 239, 376-387.
    • (2001) Dev. Biol. , vol.239 , pp. 376-387
    • Aul, R.B.1    Oko, R.J.2
  • 39
    • 0021020468 scopus 로고
    • Structural organization of the meiotic prophase chromatin in the rat testis
    • Rao, B.J., Brahmachari, S.K. & Rao, M.R. (1983) Structural organization of the meiotic prophase chromatin in the rat testis. J. Biol. Chem. 258, 13478-13485.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13478-13485
    • Rao, B.J.1    Brahmachari, S.K.2    Rao, M.R.3
  • 40
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou, E.P., Pilch, D.R., Orr, A.H., Tvanova, V.S. & Bonner, W.M. (1998) DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273, 5858-5868.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Tvanova, V.S.4    Bonner, W.M.5
  • 42
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large nonhistone region
    • Pehrson, J.R. & Fried, V.A. (1992) MacroH2A, a core histone containing a large nonhistone region. Science 257, 1398-1400.
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 43
    • 0035877759 scopus 로고    scopus 로고
    • MACROH2A2, a new member of the MACROH2A core histone family
    • Costanzi, C. & Pehrson, J.R. (2001) MACROH2A2, a new member of the MACROH2A core histone family. J. Biol. Chem. 276, 21776-21784.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21776-21784
    • Costanzi, C.1    Pehrson, J.R.2
  • 44
    • 0035394053 scopus 로고    scopus 로고
    • Histone variant macroH2A contains two distinct macrochromatin domains capable of directing macroH2A to the inactive X chromosome
    • Chadwick, B.P., Valley. C.M. & Willard, H.F. (2001) Histone variant macroH2A contains two distinct macrochromatin domains capable of directing macroH2A to the inactive X chromosome. Nucleic Acids Res. 29, 2699-2705.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2699-2705
    • Chadwick, B.P.1    Valley, C.M.2    Willard, H.F.3
  • 45
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi, C. & Pehrson, J.R. (1998) Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393, 599-601.
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 46
    • 0034735914 scopus 로고    scopus 로고
    • Higher concentrations of histone macroH2A in the Barr body are correlated with higher nucleosome density
    • Perche, P., Vourc'h, C., Konecny, L., Souchier, C., Robert-Nicoud, M., Dimitrov, S. & Khochbin, S. (2000) Higher concentrations of histone macroH2A in the Barr body are correlated with higher nucleosome density. Curr. Biol. 10, 1531-1534.
    • (2000) Curr. Biol. , vol.10 , pp. 1531-1534
    • Perche, P.1    Vourc'h, C.2    Konecny, L.3    Souchier, C.4    Robert-Nicoud, M.5    Dimitrov, S.6    Khochbin, S.7
  • 47
    • 0030975594 scopus 로고    scopus 로고
    • Developmental and tissue expression patterns of histone macroH2A1 subtypes
    • Pehrson, J.R., Costanzi, C. & Dharia, C. (1997) Developmental and tissue expression patterns of histone macroH2A1 subtypes. J. Cell Biochem. 65, 107-113.
    • (1997) J. Cell Biochem. , vol.65 , pp. 107-113
    • Pehrson, J.R.1    Costanzi, C.2    Dharia, C.3
  • 48
    • 0033568076 scopus 로고    scopus 로고
    • Messenger RNAs encoding mouse histone macroH2A 1 isoforms are expressed at similar levels in male and female cells and result from alternative splicing
    • Rasmussen, T.P., Huang, T., Mastrangelo, M.A., Loring, J., Panning, B. & Jaenisch, R. (1999) Messenger RNAs encoding mouse histone macroH2A 1 isoforms are expressed at similar levels in male and female cells and result from alternative splicing. Nucleic Acids Res. 27, 3685-3689.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3685-3689
    • Rasmussen, T.P.1    Huang, T.2    Mastrangelo, M.A.3    Loring, J.4    Panning, B.5    Jaenisch, R.6
  • 49
    • 0034255999 scopus 로고    scopus 로고
    • Histone MacroH2A1.2 is concentrated in the XY-body by the early pachytene stage of spermatogenesis
    • HoyerFender, S., Costanzi, C. & Pehrson, J.R. (2000) Histone MacroH2A1.2 is concentrated in the XY-body by the early pachytene stage of spermatogenesis. Exp. Cell Res. 258, 254-260.
    • (2000) Exp. Cell Res. , vol.258 , pp. 254-260
    • Hoyerfender, S.1    Costanzi, C.2    Pehrson, J.R.3
  • 50
    • 0034778403 scopus 로고    scopus 로고
    • M31 and macroH2A1.2 colocalise at the pseudoautosomal region during mouse meiosis
    • Turner, J.M., Burgoyne, P.S. & Singh, P.B. (2001) M31 and macroH2A1.2 colocalise at the pseudoautosomal region during mouse meiosis. J. Cell Sci. 114, 3367-3375.
    • (2001) J. Cell Sci. , vol.114 , pp. 3367-3375
    • Turner, J.M.1    Burgoyne, P.S.2    Singh, P.B.3
  • 51
    • 0035228079 scopus 로고    scopus 로고
    • X-chromosome inactivation: Counting, choice and initiation
    • Avner, P. & Heard, E. (2001) X-chromosome inactivation: counting, choice and initiation. Nat. Rev. Genet. 2, 59-67.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 59-67
    • Avner, P.1    Heard, E.2
  • 52
    • 0030804089 scopus 로고    scopus 로고
    • Xist RNA is associated with the transcriptionally inactive XY body in mammalian male meiosis
    • Ayoub, N., Richler, C. & Wahrman, J. (1997) Xist RNA is associated with the transcriptionally inactive XY body in mammalian male meiosis. Chromosoma 106, 1-10.
    • (1997) Chromosoma , vol.106 , pp. 1-10
    • Ayoub, N.1    Richler, C.2    Wahrman, J.3
  • 53
    • 0034627795 scopus 로고    scopus 로고
    • The murine heterochromatin protein M31 is associated with the chromocenter in round spermatids and is a component of mature spermatozoa
    • HoyerFender, S., Singh, P.B. & Motzkus, D. (2000) The murine heterochromatin protein M31 is associated with the chromocenter in round spermatids and is a component of mature spermatozoa. Exp. Cell Res. 254, 72-79.
    • (2000) Exp. Cell Res. , vol.254 , pp. 72-79
    • HoyerFender, S.1    Singh, P.B.2    Motzkus, D.3
  • 55
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein. T. & Allis, C.D. (2001) Translating the histone code. Science 293, 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 56
    • 0015384797 scopus 로고
    • Amino-terminal sequences and sites of in vivo acetylation of trout-testis histones 3 and IIb 2
    • Candido, E.P. & Dixon, G.H. (1972) Amino-terminal sequences and sites of in vivo acetylation of trout-testis histones 3 and IIb 2. Proc. Natl Acad. Sci. USA 69, 2015-2019.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 2015-2019
    • Candido, E.P.1    Dixon, G.H.2
  • 57
    • 0016759174 scopus 로고
    • Partial characterization of a new basic nuclear protein from rat testis elongated spermatids
    • Grimes, S.R. Jr, Platz, R.D., Meistrich, M.L. & Hnilica, L.S. (1975) Partial characterization of a new basic nuclear protein from rat testis elongated spermatids. Biochem. Biophys. Res. Commun. 67, 182-189.
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 182-189
    • Grimes Jr., S.R.1    Platz, R.D.2    Meistrich, M.L.3    Hnilica, L.S.4
  • 58
    • 0020488059 scopus 로고
    • Histone H4 hyperacetylation and rapid turnover of its acetyl groups in transcriptionally inactive rooster testis spermatids
    • Oliva, R. & Mezquita, C. (1982) Histone H4 hyperacetylation and rapid turnover of its acetyl groups in transcriptionally inactive rooster testis spermatids. Nucleic Acids Res. 10, 8049-8059.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 8049-8059
    • Oliva, R.1    Mezquita, C.2
  • 60
    • 0034659231 scopus 로고    scopus 로고
    • De novo nucleosome assembly: New pieces in an old puzzle
    • Verreault, A. (2000) De novo nucleosome assembly: new pieces in an old puzzle. Genes Dev. 14, 1430-1438.
    • (2000) Genes Dev. , vol.14 , pp. 1430-1438
    • Verreault, A.1
  • 61
    • 1642353297 scopus 로고    scopus 로고
    • Transient DNA strand breaks during mouse and human spermiogenesis: New insights in stage specificity and link to chromatin remodeling
    • Marcon, L. & Boissonneault, G. (2004) Transient DNA strand breaks during mouse and human spermiogenesis: new insights in stage specificity and link to chromatin remodeling. Biol. Reprod. 70, 910-918.
    • (2004) Biol. Reprod. , vol.70 , pp. 910-918
    • Marcon, L.1    Boissonneault, G.2
  • 62
    • 0018954102 scopus 로고
    • Acid-soluble nuclear proteins of the testis during spermatogenesis in the winter flounder. Loss of the high mobility group proteins
    • Kennedy. B.P. & Davies, P.L. (1980) Acid-soluble nuclear proteins of the testis during spermatogenesis in the winter flounder. Loss of the high mobility group proteins. J. Biol. Chem. 255, 2533-2539.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2533-2539
    • Kennedy, B.P.1    Davies, P.L.2
  • 63
    • 0019877314 scopus 로고
    • Phosphorylation of a group of high molecular weight basic nuclear proteins during spermatogenesis in the winter flounder
    • Kennedy, B.P. & Davies, P.L. (1981) Phosphorylation of a group of high molecular weight basic nuclear proteins during spermatogenesis in the winter flounder. J. Biol. Chem. 256, 9254-9259.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9254-9259
    • Kennedy, B.P.1    Davies, P.L.2
  • 64
    • 0023030892 scopus 로고
    • Marked differences in the ability of distinct protamines to disassemble nucleosomal core particles in vitro
    • Oliva, R. & Mezquita, C. (1986) Marked differences in the ability of distinct protamines to disassemble nucleosomal core particles in vitro. Biochemistry 25, 6508-6511.
    • (1986) Biochemistry , vol.25 , pp. 6508-6511
    • Oliva, R.1    Mezquita, C.2
  • 65
    • 0023657268 scopus 로고
    • Factors affecting nucleosome disassembly by protamines in vitro. Histone hyperacetylation and chromatin structure, time dependence, and the size of the sperm nuclear proteins
    • Oliva, R., Bazett-Jones, D., Mezquita, C. & Dixon, G.H. (1987) Factors affecting nucleosome disassembly by protamines in vitro. Histone hyperacetylation and chromatin structure, time dependence, and the size of the sperm nuclear proteins. J. Biol. Chem. 262, 17016-17025.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17016-17025
    • Oliva, R.1    Bazett-Jones, D.2    Mezquita, C.3    Dixon, G.H.4
  • 66
    • 0042090936 scopus 로고    scopus 로고
    • Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein
    • Pivot-Pajot, C., Caron, C., Govin, J., Vion, A., Rousseaux, S. & Khochbin, S. (2003) Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein. Mol. Cell. Biol. 23, 5354-5365.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5354-5365
    • Pivot-Pajot, C.1    Caron, C.2    Govin, J.3    Vion, A.4    Rousseaux, S.5    Khochbin, S.6
  • 67
    • 0242348752 scopus 로고    scopus 로고
    • Histone lysine methylation: A signature for chromatin function
    • Sims, R.J., Nishioka, K. & Reinberg, D. (2003) Histone lysine methylation: a signature for chromatin function. Trends Genet. 19, 629-639.
    • (2003) Trends Genet. , vol.19 , pp. 629-639
    • Sims, R.J.1    Nishioka, K.2    Reinberg, D.3
  • 70
    • 0141613756 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3, what for?
    • Prigent, C. & Dimitrov, S. (2003) Phosphorylation of serine 10 in histone H3, what for? J. Cell Sci. 116, 3677-3685.
    • (2003) J. Cell Sci. , vol.116 , pp. 3677-3685
    • Prigent, C.1    Dimitrov, S.2
  • 71
    • 2542440487 scopus 로고    scopus 로고
    • Phosphorylation of histone H2A inhibits transcription on chromatin templates
    • Zhang, Y., Griffin, K., Mondai, N. & Parvin, J.D. (2004) Phosphorylation of histone H2A inhibits transcription on chromatin templates. J. Biol. Chem. 279, 21866-21872.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21866-21872
    • Zhang, Y.1    Griffin, K.2    Mondai, N.3    Parvin, J.D.4
  • 76
    • 0010115729 scopus 로고    scopus 로고
    • Ubiquitination of histone H3 in elongating spermatids of rat testes
    • Chen, H.Y., Sun, J.M., Zhang, Y., Davie, J.R. & Meistrich, M.L. (1998) Ubiquitination of histone H3 in elongating spermatids of rat testes. J. Biol. Chem. 273, 13165-13169.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13165-13169
    • Chen, H.Y.1    Sun, J.M.2    Zhang, Y.3    Davie, J.R.4    Meistrich, M.L.5
  • 77
    • 0024117989 scopus 로고
    • The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity
    • Sung, P., Prakash, S. & Prakash, L. (1988) The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity. Genes Dev. 2, 1476-1485.
    • (1988) Genes Dev. , vol.2 , pp. 1476-1485
    • Sung, P.1    Prakash, S.2    Prakash, L.3
  • 79
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R.K., Clarkson, M.J., Tremethick, D.J. & Luger, K. (2000) Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 7, 1121-1124.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 80
    • 11144355550 scopus 로고    scopus 로고
    • SWRred not shaken; mixing the histones
    • Korber, P. & Horz, W. (2004) SWRred not shaken; mixing the histones. Cell 117, 5-7.
    • (2004) Cell , vol.117 , pp. 5-7
    • Korber, P.1    Horz, W.2
  • 81
    • 0025203527 scopus 로고
    • The centromere specific histone CENP-A is selectively retained in discrete foci in mammalian sperm nuclei
    • Palmer, D.K., O'Day, K. & Margolis, R.L. (1990) The centromere specific histone CENP-A is selectively retained in discrete foci in mammalian sperm nuclei. Chromosoms 100, 32-36.
    • (1990) Chromosoms , vol.100 , pp. 32-36
    • Palmer, D.K.1    O'Day, K.2    Margolis, R.L.3
  • 82
  • 83
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • Tagami, H., Ray-Gallet, D., Almouzni, G. & Nakatani, Y. (2004) Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell 116, 51-61.
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 84
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ. variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi, G., Shen, X., Landry, J., Wu, W.H., Sen, S. & Wu, C. (2004) ATP-driven exchange of histone H2AZ. variant catalyzed by SWR1 chromatin remodeling complex. Science 303, 343-348.
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 85
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-Related ATPase swrlp deposits histone variant H2A.Z into Euchromatin
    • online publication E131
    • Kobor, M.S., Venkatasubrahmanyam, S., Meneghini, M.D., Gin, J.W., Jennings, J.L., Link, A.J., Madhani, H.D. & Rine, J. (2004) A protein complex containing the conserved Swi2/Snf2-Related ATPase swrlp deposits histone variant H2A.Z into Euchromatin. PLoS Biol. 2, online publication E131.
    • (2004) PLoS Biol. , vol.2
    • Kobor, M.S.1    Venkatasubrahmanyam, S.2    Meneghini, M.D.3    Gin, J.W.4    Jennings, J.L.5    Link, A.J.6    Madhani, H.D.7    Rine, J.8
  • 86
    • 1942502859 scopus 로고    scopus 로고
    • The nuclear Hat1p/Hat2p complex; a molecular link between type B histone acetyltransferases and chromatin assembly
    • Ai, X. & Parthun, M.R. (2004) The nuclear Hat1p/Hat2p complex; a molecular link between type B histone acetyltransferases and chromatin assembly. Mol. Cell 14, 195-205.
    • (2004) Mol. Cell , vol.14 , pp. 195-205
    • Ai, X.1    Parthun, M.R.2
  • 87
    • 0027153906 scopus 로고
    • Ultrastructural localization of a nuclear autoantigenic sperm protein in spermatogenic cells and spermatozoa
    • Lee, Y.H. & O'Rand, M.G. (1993) Ultrastructural localization of a nuclear autoantigenic sperm protein in spermatogenic cells and spermatozoa. Anat. Rec. 236, 442-448.
    • (1993) Anat. Rec. , vol.236 , pp. 442-448
    • Lee, Y.H.1    O'Rand, M.G.2
  • 89
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: An acetyl-lysine binding domain
    • Zeng, L. & Zhou, M.M. (2002) Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 513, 124-128.
    • (2002) FEBS Lett. , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.M.2
  • 90
    • 0042817937 scopus 로고    scopus 로고
    • Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis
    • Umehara, T. & Horikoshi, M. (2003) Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis. J. Biol. Chem. 278, 35660-35667.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35660-35667
    • Umehara, T.1    Horikoshi, M.2
  • 91
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle, W., Wang, Y. & Allis, CD. (2003) Binary switches and modification cassettes in histone biology and beyond. Nature 425, 475-479.
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 93
    • 0037311294 scopus 로고    scopus 로고
    • Histone chaperones and nucleosome assembly
    • Akey, C.W. & Luger. K. (2003) Histone chaperones and nucleosome assembly. Curr. Opin. Struct. Biol. 13, 6-14.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 6-14
    • Akey, C.W.1    Luger, K.2
  • 96
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D.I. & Metoz, F. (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 97
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J.T., Graziano, V., Lee, P.L. & Sweet, R.M. (1993) Crystal structure of 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


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