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Volumn 414, Issue 1-2, 2008, Pages 10-18

Global gene expression analysis reveals specific and redundant roles for H1 variants, H1c and H10, in gene expression regulation

Author keywords

Chromatin; Linker histone; Overexpression; Variants

Indexed keywords

HISTONE H1; HISTONE H10; HISTONE H1C; UNCLASSIFIED DRUG;

EID: 41949102793     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2008.01.025     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0037609662 scopus 로고    scopus 로고
    • Mammalian linker-histone subtypes differentially affect gene expression in vivo
    • Alami R., et al. Mammalian linker-histone subtypes differentially affect gene expression in vivo. Proc. Natl. Acad. Sci. U. S. A 100 (2003) 5920-5925
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 5920-5925
    • Alami, R.1
  • 3
    • 0034928521 scopus 로고    scopus 로고
    • Histone variants: are they functionally heterogeneous?
    • REVIEWS0006
    • Brown D.T. Histone variants: are they functionally heterogeneous?. Genome Biol. 2 (2001) REVIEWS0006
    • (2001) Genome Biol. , vol.2
    • Brown, D.T.1
  • 4
    • 0029915879 scopus 로고    scopus 로고
    • Differential effect of H1 variant overexpression on cell cycle progression and gene expression
    • Brown D.T., Alexander B.T., and Sittman D.B. Differential effect of H1 variant overexpression on cell cycle progression and gene expression. Nucleic Acids Res. 24 (1996) 486-493
    • (1996) Nucleic Acids Res. , vol.24 , pp. 486-493
    • Brown, D.T.1    Alexander, B.T.2    Sittman, D.B.3
  • 5
    • 0032472365 scopus 로고    scopus 로고
    • Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome
    • Cirillo L.A., et al. Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome. EMBO J. 17 (1998) 244-254
    • (1998) EMBO J. , vol.17 , pp. 244-254
    • Cirillo, L.A.1
  • 6
    • 0023429583 scopus 로고
    • Microheterogeneity in H1 histones and its consequences
    • Cole R.D. Microheterogeneity in H1 histones and its consequences. Int. J. Pept. Protein Res. 30 (1987) 433-449
    • (1987) Int. J. Pept. Protein Res. , vol.30 , pp. 433-449
    • Cole, R.D.1
  • 7
    • 0037276175 scopus 로고    scopus 로고
    • Statistical tests for differential expression in cDNA microarray experiments
    • Cui X., and Churchill G.A. Statistical tests for differential expression in cDNA microarray experiments. Genome Biol. 4 (2003) 210
    • (2003) Genome Biol. , vol.4 , pp. 210
    • Cui, X.1    Churchill, G.A.2
  • 8
    • 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 R.G., Ayala J., and Skoultchi A.I. Individual somatic H1 subtypes are dispensable for mouse development even in mice lacking the H1(0) replacement subtype. Mol. Cell Biol. 21 (2001) 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
  • 9
    • 29244449333 scopus 로고    scopus 로고
    • Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation
    • Fan Y., et al. Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation. Cell 123 (2005) 1199-1212
    • (2005) Cell , vol.123 , pp. 1199-1212
    • Fan, Y.1
  • 10
    • 26844581712 scopus 로고    scopus 로고
    • Characterisation of human histone H1x
    • Happel N., Schulze E., and Doenecke D. Characterisation of human histone H1x. Biol. Chem. 386 (2005) 541-551
    • (2005) Biol. Chem. , vol.386 , pp. 541-551
    • Happel, N.1    Schulze, E.2    Doenecke, D.3
  • 11
    • 0035958006 scopus 로고    scopus 로고
    • Decreased expression of specific genes in yeast cells lacking histone H1
    • Hellauer K., Sirard E., and Turcotte B. Decreased expression of specific genes in yeast cells lacking histone H1. J. Biol. Chem. 276 (2001) 13587-13592
    • (2001) J. Biol. Chem. , vol.276 , pp. 13587-13592
    • Hellauer, K.1    Sirard, E.2    Turcotte, B.3
  • 13
    • 0021714286 scopus 로고
    • The distribution of H1 histone is nonuniform in chromatin and correlates with different degrees of condensation
    • Huang H.C., and Cole R.D. The distribution of H1 histone is nonuniform in chromatin and correlates with different degrees of condensation. J. Biol. Chem. 259 (1984) 14237-14242
    • (1984) J. Biol. Chem. , vol.259 , pp. 14237-14242
    • Huang, H.C.1    Cole, R.D.2
  • 14
    • 0028559510 scopus 로고
    • Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini
    • Juan L.J., Utley R.T., Adams C.C., Vettese-Dadey M., and Workman J.L. Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini. EMBO J. 13 (1994) 6031-6040
    • (1994) EMBO J. , vol.13 , pp. 6031-6040
    • Juan, L.J.1    Utley, R.T.2    Adams, C.C.3    Vettese-Dadey, M.4    Workman, J.L.5
  • 15
    • 0028052069 scopus 로고
    • Developmentally regulated expression of linker-histone variants in vertebrates
    • Khochbin S., and Wolffe A.P. Developmentally regulated expression of linker-histone variants in vertebrates. Eur. J. Biochem. 225 (1994) 501-510
    • (1994) Eur. J. Biochem. , vol.225 , pp. 501-510
    • Khochbin, S.1    Wolffe, A.P.2
  • 16
    • 0021759125 scopus 로고
    • Differences in evolutionary stability among mammalian H1 subtypes. Implications for the roles of H1 subtypes in chromatin
    • Lennox R.W. Differences in evolutionary stability among mammalian H1 subtypes. Implications for the roles of H1 subtypes in chromatin. J. Biol. Chem. 259 (1984) 669-672
    • (1984) J. Biol. Chem. , vol.259 , pp. 669-672
    • Lennox, R.W.1
  • 17
    • 0020680232 scopus 로고
    • The histone H1 complements of dividing and nondividing cells of the mouse
    • Lennox R.W., and Cohen L.H. The histone H1 complements of dividing and nondividing cells of the mouse. J. Biol. Chem. 258 (1983) 262-268
    • (1983) J. Biol. Chem. , vol.258 , pp. 262-268
    • Lennox, R.W.1    Cohen, L.H.2
  • 18
    • 0021434213 scopus 로고
    • The alterations in H1 histone complement during mouse spermatogenesis and their significance for H1 subtype function
    • Lennox R.W., and Cohen L.H. The alterations in H1 histone complement during mouse spermatogenesis and their significance for H1 subtype function. Dev. Biol. 103 (1984) 80-84
    • (1984) Dev. Biol. , vol.103 , pp. 80-84
    • Lennox, R.W.1    Cohen, L.H.2
  • 19
    • 0033997968 scopus 로고    scopus 로고
    • Normal spermatogenesis in mice lacking the testis-specific linker histone H1t
    • Lin Q., Sirotkin A., and Skoultchi A.I. Normal spermatogenesis in mice lacking the testis-specific linker histone H1t. Mol. Cell Biol. 20 (2000) 2122-2128
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2122-2128
    • Lin, Q.1    Sirotkin, A.2    Skoultchi, A.I.3
  • 20
    • 2542462280 scopus 로고    scopus 로고
    • Reductions in linker histone levels are tolerated in developing spermatocytes but cause changes in specific gene expression
    • Lin Q., et al. Reductions in linker histone levels are tolerated in developing spermatocytes but cause changes in specific gene expression. J. Biol. Chem. 279 (2004) 23525-23535
    • (2004) J. Biol. Chem. , vol.279 , pp. 23525-23535
    • Lin, Q.1
  • 21
    • 14544280215 scopus 로고    scopus 로고
    • Polar nuclear localization of H1T2, a histone H1 variant, required for spermatid elongation and DNA condensation during spermiogenesis
    • Martianov I., et al. Polar nuclear localization of H1T2, a histone H1 variant, required for spermatid elongation and DNA condensation during spermiogenesis. Proc. Natl. Acad. Sci. U. S. A 102 (2005) 2808-2813
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 2808-2813
    • Martianov, I.1
  • 22
    • 0000228352 scopus 로고
    • A Monte Carlo study of thirty internal criterion measures for cluster analysis
    • Milligan G.W. A Monte Carlo study of thirty internal criterion measures for cluster analysis. Psycometrika 46 (1981) 187-189
    • (1981) Psycometrika , vol.46 , pp. 187-189
    • Milligan, G.W.1
  • 23
    • 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. Dynamic binding of histone H1 to chromatin in living cells. Nature 408 (2000) 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
  • 24
    • 0032566724 scopus 로고    scopus 로고
    • Differential nucleosome positioning on Xenopus oocyte and somatic 5 S RNA genes determines both TFIIIA and H1 binding: a mechanism for selective H1 repression
    • Panetta G., Buttinelli M., Flaus A., Richmond T.J., and Rhodes D. Differential nucleosome positioning on Xenopus oocyte and somatic 5 S RNA genes determines both TFIIIA and H1 binding: a mechanism for selective H1 repression. J. Mol. Biol. 282 (1998) 683-697
    • (1998) J. Mol. Biol. , vol.282 , pp. 683-697
    • Panetta, G.1    Buttinelli, M.2    Flaus, A.3    Richmond, T.J.4    Rhodes, D.5
  • 25
    • 0036898577 scopus 로고    scopus 로고
    • Microarray data normalization and transformation
    • Suppl
    • Quackenbush J. Microarray data normalization and transformation. Nat. Genet. 32 (2002) 496-501 Suppl
    • (2002) Nat. Genet. , vol.32 , pp. 496-501
    • Quackenbush, J.1
  • 26
    • 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., and Sweet R.M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362 (1993) 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
  • 27
    • 0031835433 scopus 로고    scopus 로고
    • Role of histone H1 as an architectural determinant of chromatin structure and as a specific repressor of transcription on Xenopus oocyte 5S rRNA genes
    • Sera T., and Wolffe A.P. Role of histone H1 as an architectural determinant of chromatin structure and as a specific repressor of transcription on Xenopus oocyte 5S rRNA genes. Mol. Cell Biol. 18 (1998) 3668-3680
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3668-3680
    • Sera, T.1    Wolffe, A.P.2
  • 28
    • 0030576509 scopus 로고    scopus 로고
    • Linker histone H1 regulates specific gene expression but not global transcription in vivo
    • Shen X., and Gorovsky M.A. Linker histone H1 regulates specific gene expression but not global transcription in vivo. Cell 86 (1996) 475-483
    • (1996) Cell , vol.86 , pp. 475-483
    • Shen, X.1    Gorovsky, M.A.2
  • 30
    • 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. Histone H1 variants play individual roles in transcription regulation in the DT40 chicken B cell line. Biochem. Biophys. Res. Commun. 268 (2000) 501-508
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 501-508
    • Takami, Y.1    Nishi, R.2    Nakayama, T.3
  • 31
    • 0030068951 scopus 로고    scopus 로고
    • In vivo phosphorylation of histone H1 variants during the cell cycle
    • Talasz H., Helliger W., Puschendorf B., and Lindner H. In vivo phosphorylation of histone H1 variants during the cell cycle. Biochemistry 35 (1996) 1761-1767
    • (1996) Biochemistry , vol.35 , pp. 1761-1767
    • Talasz, H.1    Helliger, W.2    Puschendorf, B.3    Lindner, H.4
  • 32
    • 23344444308 scopus 로고    scopus 로고
    • HANP1/H1T2, a novel histone H1-like protein involved in nuclear formation and sperm fertility
    • Tanaka H., et al. HANP1/H1T2, a novel histone H1-like protein involved in nuclear formation and sperm fertility. Mol. Cell Biol. 25 (2005) 7107-7119
    • (2005) Mol. Cell Biol. , vol.25 , pp. 7107-7119
    • Tanaka, H.1
  • 33
    • 23044489675 scopus 로고    scopus 로고
    • H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain
    • Th'ng J.P., Sung R., Ye M., and Hendzel M.J. H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain. J. Biol. Chem. 280 (2005) 27809-27814
    • (2005) J. Biol. Chem. , vol.280 , pp. 27809-27814
    • Th'ng, J.P.1    Sung, R.2    Ye, M.3    Hendzel, M.J.4
  • 34
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma F., Koller T., and Klug A. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J. Cell Biol. 83 (1979) 403-427
    • (1979) J. Cell Biol. , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 35
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher V.G., Tibshirani R., and Chu G. Significance analysis of microarrays applied to the ionizing radiation response. Proc. Natl. Acad. Sci. U. S. A 98 (2001) 5116-5121
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 36
    • 0003903126 scopus 로고
    • New York, Springer-Verlag
    • van Holde K. Chromatin (1988), New York, Springer-Verlag
    • (1988) Chromatin
    • van Holde, K.1
  • 37
    • 0021705781 scopus 로고
    • Histone-H1-dependent chromatin superstructures and the suppression of gene activity
    • Weintraub H. Histone-H1-dependent chromatin superstructures and the suppression of gene activity. Cell 38 (1984) 17-27
    • (1984) Cell , vol.38 , pp. 17-27
    • Weintraub, H.1
  • 38
    • 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., and Matzuk M.M. HILS1 is a spermatid-specific linker histone H1-like protein implicated in chromatin remodeling during mammalian spermiogenesis. Proc. Natl. Acad. Sci. U. S. A 100 (2003) 10546-10551
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 10546-10551
    • Yan, W.1    Ma, L.2    Burns, K.H.3    Matzuk, M.M.4
  • 39
    • 1342294092 scopus 로고    scopus 로고
    • Normalization for cDNA microarray data: a robust composite method addressing single and multiple slide systematic variation
    • Yang Y.H., et al. Normalization for cDNA microarray data: a robust composite method addressing single and multiple slide systematic variation. Nucleic Acids Res. 30 (2002) e15
    • (2002) Nucleic Acids Res. , vol.30
    • Yang, Y.H.1
  • 40
    • 0027082560 scopus 로고
    • Histone H1 and transcription: still an enigma? J
    • Zlatanova J., and Van Holde K. Histone H1 and transcription: still an enigma? J. Cell Sci. 103 Pt 4 (1992) 889-895
    • (1992) Cell Sci. , vol.103 , Issue.PART 4 , pp. 889-895
    • Zlatanova, J.1    Van Holde, K.2


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