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Volumn 27, Issue 22, 2007, Pages 7865-7870

A plasmid model system shows that Drosophila dosage compensation depends on the global acetylation of histone H4 at lysine 16 and is not affected by depletion of common transcription elongation chromatin marks

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H4; LYSINE; LYSINE 16; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 36049007800     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00397-07     Document Type: Article
Times cited : (17)

References (26)
  • 2
    • 33645530936 scopus 로고    scopus 로고
    • High-resolution ChIP-chip analysis reveals that the Drosophila MSL complex selectively identifies active genes on the male X chromosome
    • Alekseyenko, A. A., E. Larschan, W. R. Lai, P. J. Park, and M. I. Kuroda. 2006. High-resolution ChIP-chip analysis reveals that the Drosophila MSL complex selectively identifies active genes on the male X chromosome. Genes Dev. 20:848-857.
    • (2006) Genes Dev , vol.20 , pp. 848-857
    • Alekseyenko, A.A.1    Larschan, E.2    Lai, W.R.3    Park, P.J.4    Kuroda, M.I.5
  • 3
    • 33750463354 scopus 로고    scopus 로고
    • MES-4: An autosome-associated histone methyltransferase that participates in silencing the X chromosomes in the C. elegans germ line
    • Bender, L. B., J. Suh, C. R. Carroll, Y. Fong, I. M. Fingerman, S. D. Briggs, R. Cao, Y. Zhang, V. Reinke, and S. Strome. 2006. MES-4: an autosome-associated histone methyltransferase that participates in silencing the X chromosomes in the C. elegans germ line. Development 133:3907-3917.
    • (2006) Development , vol.133 , pp. 3907-3917
    • Bender, L.B.1    Suh, J.2    Carroll, C.R.3    Fong, Y.4    Fingerman, I.M.5    Briggs, S.D.6    Cao, R.7    Zhang, Y.8    Reinke, V.9    Strome, S.10
  • 6
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 A resolution
    • Davey, C. A., D. F. Sargent, K. Luger, A. W. Maeder, and T. J. Richmond. 2002. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 A resolution. J. Mol. Biol. 319:1097- 1113.
    • (2002) J. Mol. Biol , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 8
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M., and H. Bujard. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89:5547-5551.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 9
    • 29144468972 scopus 로고    scopus 로고
    • Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation
    • Joshi, A. A., and K. Struhl. 2005. Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation. Mol. Cell 20:971-978.
    • (2005) Mol. Cell , vol.20 , pp. 971-978
    • Joshi, A.A.1    Struhl, K.2
  • 10
    • 0030913367 scopus 로고    scopus 로고
    • Sex lethal controls dosage compensation in Drosophila by a non-splicing mechanism
    • Kelley, R. L., J. Wang, L. Bell, and M. I. Kuroda. 1997. Sex lethal controls dosage compensation in Drosophila by a non-splicing mechanism. Nature 387:195-199.
    • (1997) Nature , vol.387 , pp. 195-199
    • Kelley, R.L.1    Wang, J.2    Bell, L.3    Kuroda, M.I.4
  • 12
    • 0026416169 scopus 로고
    • The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily
    • Koelle, M. R., W. S. Talbot, W. A. Segraves, M. T. Bender, P. Cherbas, and D. S. Hogness. 1991. The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily. Cell 67:59-77.
    • (1991) Cell , vol.67 , pp. 59-77
    • Koelle, M.R.1    Talbot, W.S.2    Segraves, W.A.3    Bender, M.T.4    Cherbas, P.5    Hogness, D.S.6
  • 13
    • 29444458753 scopus 로고    scopus 로고
    • Chromatin remodeling in dosage compensation
    • Lucchesi, J. C., W. G. Kelly, and B. Panning. 2005. Chromatin remodeling in dosage compensation. Annu. Rev. Genet. 39:615-651.
    • (2005) Annu. Rev. Genet , vol.39 , pp. 615-651
    • Lucchesi, J.C.1    Kelly, W.G.2    Panning, B.3
  • 14
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., A. W. Mader, R. K. Richmond, D. F. Sargent, and T. J. Richmond. 1997. Crystal structure of the nucleosome core particle at 2.8 A 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
  • 15
    • 15244358670 scopus 로고    scopus 로고
    • Distinction and relationship between elongation rate and processivity of RNA polymerase II in vivo
    • Mason, P. B., and K. Struhl. 2005. Distinction and relationship between elongation rate and processivity of RNA polymerase II in vivo. Mol. Cell 17:831-840.
    • (2005) Mol. Cell , vol.17 , pp. 831-840
    • Mason, P.B.1    Struhl, K.2
  • 16
    • 1242342240 scopus 로고    scopus 로고
    • Histone H3.3 is enriched in covalent modifications associated with active chromatin
    • McKittrick, E., P. R. Galken, K. Ahmad, and S. Henikoff. 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    Galken, P.R.2    Ahmad, K.3    Henikoff, S.4
  • 17
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profiling of histone H3.3 replacement patterns
    • Mito, Y., J. G. Henikoff, and S. Henikoff. 2005. Genome-scale profiling of histone H3.3 replacement patterns. Nat. Genet. 37:1090-1097.
    • (2005) Nat. Genet , vol.37 , pp. 1090-1097
    • Mito, Y.1    Henikoff, J.G.2    Henikoff, S.3
  • 18
    • 0348166011 scopus 로고    scopus 로고
    • Probing chromatin immunoprecipitates with CpG-island microarrays to identify genomic sites occupied by DNA-binding proteins
    • Oberley, M. J., and P. J. Farnham. 2003. Probing chromatin immunoprecipitates with CpG-island microarrays to identify genomic sites occupied by DNA-binding proteins. Methods Enzymol. 371:577-596.
    • (2003) Methods Enzymol , vol.371 , pp. 577-596
    • Oberley, M.J.1    Farnham, P.J.2
  • 19
    • 0025765764 scopus 로고
    • The complex set of late transcripts from the Drosophila sex determination gene sex-lethal encodes multiple related polypeptides
    • Samuels, M. E., P. Schedl, and T. W. Cline. 1991. The complex set of late transcripts from the Drosophila sex determination gene sex-lethal encodes multiple related polypeptides. Mol. Cell. Biol. 11:3584-3602.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 3584-3602
    • Samuels, M.E.1    Schedl, P.2    Cline, T.W.3
  • 20
    • 0037478652 scopus 로고    scopus 로고
    • Male-specific lethal complex of Drosophila targets activated regions of the X chromosome for chromatin remodeling
    • Sass, G. L., A. Pannuti, and J. C. Lucchesi. 2003. Male-specific lethal complex of Drosophila targets activated regions of the X chromosome for chromatin remodeling. Proc. Natl. Acad. Sci. USA 100:8287-8291.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8287-8291
    • Sass, G.L.1    Pannuti, A.2    Lucchesi, J.C.3
  • 21
  • 22
    • 0037663448 scopus 로고    scopus 로고
    • Drosophila FACT contributes to Hox gene expression through physical and functional interactions with GAGA factor
    • Shimojima, T., M. Okada, T. Nakayama, H. Ueda, K. Okawa, A. Iwamatsu, H. Handa, and S. Hirose. 2003. Drosophila FACT contributes to Hox gene expression through physical and functional interactions with GAGA factor. Genes Dev. 17:1605-1616.
    • (2003) Genes Dev , vol.17 , pp. 1605-1616
    • Shimojima, T.1    Okada, M.2    Nakayama, T.3    Ueda, H.4    Okawa, K.5    Iwamatsu, A.6    Handa, H.7    Hirose, S.8
  • 23
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak, M., H. Ishii, J. M. Sun, M. J. Pazin, J. R. Davie, and C. L. Peterson. 2006. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311:844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 24
    • 0035943734 scopus 로고    scopus 로고
    • Linking global histone acetylation to the transcription enhancement of X-chromosomal genes in Drosophila males
    • Smith, E. R., C. D. Allis, and J. C. Lucchesi. 2001. Linking global histone acetylation to the transcription enhancement of X-chromosomal genes in Drosophila males. J. Biol. Chem. 276:31483-31486.
    • (2001) J. Biol. Chem , vol.276 , pp. 31483-31486
    • Smith, E.R.1    Allis, C.D.2    Lucchesi, J.C.3
  • 25
    • 0033988212 scopus 로고    scopus 로고
    • The Drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation
    • Smith, E. R., A. Pannuti, W. Gu, A. Steurnagel, R. G. Cook, C. D. Allis, and J. C. Lucchesi. 2000. The Drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation. Mol. Cell. Biol. 20:312-318.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 312-318
    • Smith, E.R.1    Pannuti, A.2    Gu, W.3    Steurnagel, A.4    Cook, R.G.5    Allis, C.D.6    Lucchesi, J.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.