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Volumn 123, Issue 2, 2005, Pages 233-248

Histone Variant H2A.Z Marks the 5′ Ends of Both Active and Inactive Genes in Euchromatin (DOI:10.1016/j.cell.2005.10.002);Histone variant H2A.Z Marks the 5′ ends of both active and inactive genes in euchromatin

Author keywords

[No Author keywords available]

Indexed keywords

BDF 1 PROTEIN; HISTONE H2A; HISTONE H3; HISTONE H4; PROTEIN; PROTEIN MYB; REB 1 PROTEIN; SWR 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 26844511498     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.06.046     Document Type: Erratum
Times cited : (545)

References (44)
  • 1
    • 0038719686 scopus 로고    scopus 로고
    • Reb1p-dependent DNA bending effects nucleosome positioning and constitutive transcription at the yeast profilin promoter
    • M. Angermayr, U. Oechsner, and W. Bandlow Reb1p-dependent DNA bending effects nucleosome positioning and constitutive transcription at the yeast profilin promoter J. Biol. Chem. 278 2003 17918 17926
    • (2003) J. Biol. Chem. , vol.278 , pp. 17918-17926
    • Angermayr, M.1    Oechsner, U.2    Bandlow, W.3
  • 4
    • 0037318210 scopus 로고    scopus 로고
    • Transcriptional interactions between yeast tRNA genes, flanking genes and Ty elements: A genomic point of view
    • E.C. Bolton, and J.D. Boeke Transcriptional interactions between yeast tRNA genes, flanking genes and Ty elements: a genomic point of view Genome Res. 13 2003 254 263
    • (2003) Genome Res. , vol.13 , pp. 254-263
    • Bolton, E.C.1    Boeke, J.D.2
  • 6
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • A.S. Clarke, J.E. Lowell, S.J. Jacobson, and L. Pillus Esa1p is an essential histone acetyltransferase required for cell cycle progression Mol. Cell. Biol. 19 1999 2515 2526
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2515-2526
    • Clarke, A.S.1    Lowell, J.E.2    Jacobson, S.J.3    Pillus, L.4
  • 7
    • 0035076210 scopus 로고    scopus 로고
    • Histone acetylation at promoters is differentially affected by specific activators and repressors
    • J. Deckert, and K. Struhl Histone acetylation at promoters is differentially affected by specific activators and repressors Mol. Cell. Biol. 21 2001 2726 2735
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2726-2735
    • Deckert, J.1    Struhl, K.2
  • 8
    • 0033558878 scopus 로고    scopus 로고
    • The boundaries of the silenced HMR domain in Saccharomyces cerevisiae
    • D. Donze, C.R. Adams, J. Rine, and R.T. Kamakaka The boundaries of the silenced HMR domain in Saccharomyces cerevisiae Genes Dev. 13 1999 698 708
    • (1999) Genes Dev. , vol.13 , pp. 698-708
    • Donze, D.1    Adams, C.R.2    Rine, J.3    Kamakaka, R.T.4
  • 9
    • 22344437987 scopus 로고    scopus 로고
    • Fast and systematic genome-wide discovery of conserved regulatory elements using a non-alignment based approach
    • O. Elemento, and S. Tavazoie Fast and systematic genome-wide discovery of conserved regulatory elements using a non-alignment based approach Genome Biol. 6 2005 R18
    • (2005) Genome Biol. , vol.6 , pp. 18
    • Elemento, O.1    Tavazoie, S.2
  • 10
    • 0032498622 scopus 로고    scopus 로고
    • Pheromone-regulated genes required for yeast mating differentiation
    • S. Erdman, L. Lin, M. Malczynski, and M. Snyder Pheromone-regulated genes required for yeast mating differentiation J. Cell Biol. 140 1998 461 483
    • (1998) J. Cell Biol. , vol.140 , pp. 461-483
    • Erdman, S.1    Lin, L.2    Malczynski, M.3    Snyder, M.4
  • 11
    • 0036829024 scopus 로고    scopus 로고
    • General regulatory factors (GRFs) as genome partitioners
    • G. Fourel, T. Miyake, P.A. Defossez, R. Li, and E. Gilson General regulatory factors (GRFs) as genome partitioners J. Biol. Chem. 277 2002 41736 41743
    • (2002) J. Biol. Chem. , vol.277 , pp. 41736-41743
    • Fourel, G.1    Miyake, T.2    Defossez, P.A.3    Li, R.4    Gilson, E.5
  • 12
    • 16644373292 scopus 로고    scopus 로고
    • Noise minimization in eukaryotic gene expression
    • 10.1371/journal.pbio.0020137
    • H.B. Fraser, A.E. Hirsh, G. Giaever, J. Kumm, and M.B. Eisen Noise minimization in eukaryotic gene expression PLoS Biol. 2 2004 e137 10.1371/journal.pbio.0020137
    • (2004) PLoS Biol. , vol.2 , pp. 137
    • Fraser, H.B.1    Hirsh, A.E.2    Giaever, G.3    Kumm, J.4    Eisen, M.B.5
  • 14
    • 0034735578 scopus 로고    scopus 로고
    • Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating
    • M.G. Heiman, and P. Walter Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating J. Cell Biol. 151 2000 719 730
    • (2000) J. Cell Biol. , vol.151 , pp. 719-730
    • Heiman, M.G.1    Walter, P.2
  • 15
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • L. Howe, D. Auston, P. Grant, S. John, R.G. Cook, J.L. Workman, and L. Pillus Histone H3 specific acetyltransferases are essential for cell cycle progression Genes Dev. 15 2001 3144 3154
    • (2001) Genes Dev. , vol.15 , pp. 3144-3154
    • Howe, L.1    Auston, D.2    Grant, P.3    John, S.4    Cook, R.G.5    Workman, J.L.6    Pillus, L.7
  • 16
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • W.W. Hwang, S. Venkatasubrahmanyam, A.G. Ianculescu, A. Tong, C. Boone, and H.D. Madhani A conserved RING finger protein required for histone H2B monoubiquitination and cell size control Mol. Cell 11 2003 261 266
    • (2003) Mol. Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1    Venkatasubrahmanyam, S.2    Ianculescu, A.G.3    Tong, A.4    Boone, C.5    Madhani, H.D.6
  • 17
    • 0025123264 scopus 로고
    • REB1, a yeast DNA-binding protein with many targets, is essential for growth and bears some resemblance to the oncogene myb
    • Q.D. Ju, B.E. Morrow, and J.R. Warner REB1, a yeast DNA-binding protein with many targets, is essential for growth and bears some resemblance to the oncogene myb Mol. Cell. Biol. 10 1990 5226 5234
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5226-5234
    • Ju, Q.D.1    Morrow, B.E.2    Warner, J.R.3
  • 19
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • A. Kimura, T. Umehara, and M. Horikoshi Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing Nat. Genet. 32 2002 370 377
    • (2002) Nat. Genet. , vol.32 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 20
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
    • 10.1371/journal.pbio.0020131
    • M.S. Kobor, S. Venkatasubrahmanyam, M.D. Meneghini, J.W. Gin, J. Jennings, A.J. Link, H.D. Madhani, and J. Rine A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin PLoS Biol. 2 2004 e131 10.1371/journal.pbio.0020131
    • (2004) PLoS Biol. , vol.2 , pp. 131
    • Kobor, M.S.1    Venkatasubrahmanyam, S.2    Meneghini, M.D.3    Gin, J.W.4    Jennings, J.5    Link, A.J.6    Madhani, H.D.7    Rine, J.8
  • 21
    • 0037524702 scopus 로고    scopus 로고
    • The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: Linking transcriptional elongation to histone methylation
    • N.J. Krogan, J. Dover, A. Wood, J. Schneider, J. Heidt, M.A. Boateng, K. Dean, O.W. Ryan, A. Golshani, and M. Johnston The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: Linking transcriptional elongation to histone methylation Mol. Cell 11 2003 721 729
    • (2003) Mol. Cell , vol.11 , pp. 721-729
    • Krogan, N.J.1    Dover, J.2    Wood, A.3    Schneider, J.4    Heidt, J.5    Boateng, M.A.6    Dean, K.7    Ryan, O.W.8    Golshani, A.9    Johnston, M.10
  • 23
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • S.K. Kurdistani, S. Tavazoie, and M. Grunstein Mapping global histone acetylation patterns to gene expression Cell 117 2004 721 733
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 24
    • 0037291760 scopus 로고    scopus 로고
    • Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries
    • A.G. Ladurner, C. Inouye, R. Jain, and R. Tjian Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries Mol. Cell 11 2003 365 376
    • (2003) Mol. Cell , vol.11 , pp. 365-376
    • Ladurner, A.G.1    Inouye, C.2    Jain, R.3    Tjian, R.4
  • 25
    • 3543023310 scopus 로고    scopus 로고
    • Evidence for nucleosome depletion at active regulatory regions genome-wide
    • C.K. Lee, Y. Shibata, B. Rao, B.D. Strahl, and J.D. Lieb Evidence for nucleosome depletion at active regulatory regions genome-wide Nat. Genet. 36 2004 900 905
    • (2004) Nat. Genet. , vol.36 , pp. 900-905
    • Lee, C.K.1    Shibata, Y.2    Rao, B.3    Strahl, B.D.4    Lieb, J.D.5
  • 26
    • 0028359822 scopus 로고
    • Defining the sequence specificity of the Saccharomyces cerevisiae DNA binding protein REB1p by selecting binding sites from random-sequence oligonucleotides
    • P.C. Liaw, and C.J. Brandl Defining the sequence specificity of the Saccharomyces cerevisiae DNA binding protein REB1p by selecting binding sites from random-sequence oligonucleotides Yeast 10 1994 771 787
    • (1994) Yeast , vol.10 , pp. 771-787
    • Liaw, P.C.1    Brandl, C.J.2
  • 27
    • 0029878216 scopus 로고    scopus 로고
    • Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: Redundant and position-independent functions in assembly but not in gene regulation
    • X. Ling, T.A. Harkness, M.C. Schultz, G. Fisher-Adams, and M. Grunstein Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation Genes Dev. 10 1996 686 699
    • (1996) Genes Dev. , vol.10 , pp. 686-699
    • Ling, X.1    Harkness, T.A.2    Schultz, M.C.3    Fisher-Adams, G.4    Grunstein, M.5
  • 28
  • 29
    • 0037291695 scopus 로고    scopus 로고
    • Different sensitivities of bromodomain factors 1 and 2 to histone H4 acetylation
    • O. Matangkasombut, and S. Buratowski Different sensitivities of bromodomain factors 1 and 2 to histone H4 acetylation Mol. Cell 11 2003 353 363
    • (2003) Mol. Cell , vol.11 , pp. 353-363
    • Matangkasombut, O.1    Buratowski, S.2
  • 30
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • M.D. Meneghini, M. Wu, and H.D. Madhani Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin Cell 112 2003 725 736
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 31
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • G. Mizuguchi, X. Shen, J. Landry, W.H. Wu, S. Sen, and C. Wu ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex Science 303 2004 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
  • 32
    • 0037452770 scopus 로고    scopus 로고
    • Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: A potential mechanism for position-effect variegation
    • H.H. Ng, D.N. Ciccone, K.B. Morshead, M.A. Oettinger, and K. Struhl Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation Proc. Natl. Acad. Sci. USA 100 2003 1820 1825
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1820-1825
    • Ng, H.H.1    Ciccone, D.N.2    Morshead, K.B.3    Oettinger, M.A.4    Struhl, K.5
  • 33
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • H.H. Ng, F. Robert, R.A. Young, and K. Struhl Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity Mol. Cell 11 2003 709 719
    • (2003) Mol. Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 35
    • 0034721645 scopus 로고    scopus 로고
    • Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes
    • M.S. Santisteban, T. Kalashnikova, and M.M. Smith Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes Cell 103 2000 411 422
    • (2000) Cell , vol.103 , pp. 411-422
    • Santisteban, M.S.1    Kalashnikova, T.2    Smith, M.M.3
  • 36
    • 9144253287 scopus 로고    scopus 로고
    • Methylation of H3 lysine 4 at euchromatin promotes Sir3p association with heterochromatin
    • H. Santos-Rosa, A.J. Bannister, P.M. Dehe, V. Geli, and T. Kouzarides Methylation of H3 lysine 4 at euchromatin promotes Sir3p association with heterochromatin J. Biol. Chem. 279 2004 47506 47512
    • (2004) J. Biol. Chem. , vol.279 , pp. 47506-47512
    • Santos-Rosa, H.1    Bannister, A.J.2    Dehe, P.M.3    Geli, V.4    Kouzarides, T.5
  • 38
    • 20444403749 scopus 로고    scopus 로고
    • Intrinsic histone-DNA interactions and low nucleosome density are important for preferential accessibility of promoter regions in yeast
    • E.A. Sekinger, Z. Moqtaderi, and K. Struhl Intrinsic histone-DNA interactions and low nucleosome density are important for preferential accessibility of promoter regions in yeast Mol. Cell 18 2005 735 748
    • (2005) Mol. Cell , vol.18 , pp. 735-748
    • Sekinger, E.A.1    Moqtaderi, Z.2    Struhl, K.3
  • 39
    • 0345166826 scopus 로고    scopus 로고
    • Chromosomal site-specific double-strand breaks are efficiently targeted for repair by oligonucleotides in yeast
    • F. Storici, C.L. Durham, D.A. Gordenin, and M.A. Resnick Chromosomal site-specific double-strand breaks are efficiently targeted for repair by oligonucleotides in yeast Proc. Natl. Acad. Sci. USA 100 2003 14994 14999
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14994-14999
    • Storici, F.1    Durham, C.L.2    Gordenin, D.A.3    Resnick, M.A.4
  • 40
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
    • N. Suka, K. Luo, and M. Grunstein Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin Nat. Genet. 32 2002 378 383
    • (2002) Nat. Genet. , vol.32 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 41
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2AZ
    • R.K. Suto, M.J. Clarkson, D.J. Tremethick, and K. Luger Crystal structure of a nucleosome core particle containing the variant histone H2AZ Nat. Struct. Biol. 7 2000 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
  • 42
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • F. van Leeuwen, P.R. Gafken, and D.E. Gottschling Dot1p modulates silencing in yeast by methylation of the nucleosome core Cell 109 2002 745 756
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3


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