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Volumn 30, Issue 12, 2005, Pages 680-687

In and out: Histone variant exchange in chromatin

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE;

EID: 27944442030     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2005.10.003     Document Type: Review
Times cited : (128)

References (70)
  • 1
    • 0037311294 scopus 로고    scopus 로고
    • Histone chaperones and nucleosome assembly
    • C.W. Akey, and K. Luger Histone chaperones and nucleosome assembly Curr. Opin. Struct. Biol. 13 2003 6 14
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 6-14
    • Akey, C.W.1    Luger, K.2
  • 3
    • 21844465956 scopus 로고    scopus 로고
    • Histone dynamics in living cells revealed by photobleaching
    • H. Kimura Histone dynamics in living cells revealed by photobleaching DNA Repair 4 2005 939 950
    • (2005) DNA Repair , vol.4 , pp. 939-950
    • Kimura, H.1
  • 4
    • 3042522654 scopus 로고    scopus 로고
    • Chromatin dynamics at DNA replication, transcription and repair
    • A.E. Ehrenhofer-Murray Chromatin dynamics at DNA replication, transcription and repair Eur. J. Biochem. 271 2004 2335 2349
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2335-2349
    • Ehrenhofer-Murray, A.E.1
  • 5
    • 15744397041 scopus 로고    scopus 로고
    • Chromatin remodeling complexes: Strength in diversity, precision through specialization
    • B.R. Cairns Chromatin remodeling complexes: strength in diversity, precision through specialization Curr. Opin. Genet. Dev. 15 2005 185 190
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 185-190
    • Cairns, B.R.1
  • 6
    • 20444500543 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling complexes and their role in nuclear receptor-dependent transcription in vivo
    • S. Aoyagi ATP-dependent chromatin remodeling complexes and their role in nuclear receptor-dependent transcription in vivo Vitam. Horm. 70 2005 281 307
    • (2005) Vitam. Horm. , vol.70 , pp. 281-307
    • Aoyagi, S.1
  • 7
    • 2942746179 scopus 로고    scopus 로고
    • Histone variants, nucleosome assembly and epigenetic inheritance
    • S. Henikoff Histone variants, nucleosome assembly and epigenetic inheritance Trends Genet. 20 2004 320 326
    • (2004) Trends Genet. , vol.20 , pp. 320-326
    • Henikoff, S.1
  • 8
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • H.S. Malik, and S. Henikoff Phylogenomics of the nucleosome Nat. Struct. Biol. 10 2003 882 891
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 9
    • 0036531895 scopus 로고    scopus 로고
    • Histone H2A variants H2AX and H2AZ
    • C. Redon Histone H2A variants H2AX and H2AZ Curr. Opin. Genet. Dev. 12 2002 162 169
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 162-169
    • Redon, C.1
  • 10
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • M.D. Meneghini 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
  • 11
    • 4644311959 scopus 로고    scopus 로고
    • New twists on H2A.Z: A histone variant with a controversial structural and functional past
    • D. Dryhurst New twists on H2A.Z: a histone variant with a controversial structural and functional past Biochem. Cell Biol. 82 2004 490 497
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 490-497
    • Dryhurst, D.1
  • 12
    • 3042642001 scopus 로고    scopus 로고
    • RNA interference demonstrates a novel role for H2A.Z in chromosome segregation
    • D. Rangasamy RNA interference demonstrates a novel role for H2A.Z in chromosome segregation Nat. Struct. Mol. Biol. 11 2004 650 655
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 650-655
    • Rangasamy, D.1
  • 13
    • 11844295965 scopus 로고    scopus 로고
    • The role of histone H2Av variant replacement and histone H4 acetylation in the establishment of Drosophila heterochromatin
    • J. Swaminathan The role of histone H2Av variant replacement and histone H4 acetylation in the establishment of Drosophila heterochromatin Genes Dev. 19 2005 65 76
    • (2005) Genes Dev. , vol.19 , pp. 65-76
    • Swaminathan, J.1
  • 14
    • 0033578004 scopus 로고    scopus 로고
    • Regions of variant histone His2AvD required for Drosophila development
    • M.J. Clarkson Regions of variant histone His2AvD required for Drosophila development Nature 399 1999 694 697
    • (1999) Nature , vol.399 , pp. 694-697
    • Clarkson, M.J.1
  • 15
    • 23844485933 scopus 로고    scopus 로고
    • Structural characterization of the histone variant macroH2A
    • S. Chakravarthy Structural characterization of the histone variant macroH2A Mol. Cell. Biol. 25 2005 7616 7624
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7616-7624
    • Chakravarthy, S.1
  • 16
    • 0020660260 scopus 로고
    • Eukaryotic RNA polymerase II binds to nucleosome cores from transcribed genes
    • B.W. Baer, and D. Rhodes Eukaryotic RNA polymerase II binds to nucleosome cores from transcribed genes Nature 301 1983 482 488
    • (1983) Nature , vol.301 , pp. 482-488
    • Baer, B.W.1    Rhodes, D.2
  • 17
    • 0025134076 scopus 로고
    • In vivo studies on the dynamics of histone-DNA interaction: Evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both
    • V. Jackson In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both Biochemistry 29 1990 719 731
    • (1990) Biochemistry , vol.29 , pp. 719-731
    • Jackson, V.1
  • 18
    • 1542267778 scopus 로고    scopus 로고
    • Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome
    • V. Levchenko, and V. Jackson Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome Biochemistry 43 2004 2359 2372
    • (2004) Biochemistry , vol.43 , pp. 2359-2372
    • Levchenko, V.1    Jackson, V.2
  • 19
    • 16844366808 scopus 로고    scopus 로고
    • Histone release during transcription: Displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress
    • V. Levchenko Histone release during transcription: displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress Biochemistry 44 2005 5357 5372
    • (2005) Biochemistry , vol.44 , pp. 5357-5372
    • Levchenko, V.1
  • 20
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription
    • M.L. Kireeva Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription Mol. Cell 9 2002 541 552
    • (2002) Mol. Cell , vol.9 , pp. 541-552
    • Kireeva, M.L.1
  • 21
    • 0041828954 scopus 로고    scopus 로고
    • FACT facilitates transcription-dependent nucleosome alteration
    • R. Belotserkovskaya FACT facilitates transcription-dependent nucleosome alteration Science 301 2003 1090 1093
    • (2003) Science , vol.301 , pp. 1090-1093
    • Belotserkovskaya, R.1
  • 22
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • C.D. Kaplan Transcription elongation factors repress transcription initiation from cryptic sites Science 301 2003 1096 1099
    • (2003) Science , vol.301 , pp. 1096-1099
    • Kaplan, C.D.1
  • 23
    • 0242579933 scopus 로고    scopus 로고
    • The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo
    • P.B. Mason, and K. Struhl The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo Mol. Cell. Biol. 23 2003 8323 8333
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8323-8333
    • Mason, P.B.1    Struhl, K.2
  • 24
    • 0043239320 scopus 로고    scopus 로고
    • H2A.Z has a function reminiscent of an activator required for preferential binding to intergenic DNA
    • M. Larochelle, and L. Gaudreau H2A.Z has a function reminiscent of an activator required for preferential binding to intergenic DNA EMBO J. 22 2003 4512 4522
    • (2003) EMBO J. , vol.22 , pp. 4512-4522
    • Larochelle, M.1    Gaudreau, L.2
  • 25
    • 21644468242 scopus 로고    scopus 로고
    • Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z
    • S.D. Farris Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z J. Biol. Chem. 280 2005 25298 25303
    • (2005) J. Biol. Chem. , vol.280 , pp. 25298-25303
    • Farris, S.D.1
  • 26
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • H. Tagami Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis Cell 116 2004 51 61
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1
  • 27
    • 12544258222 scopus 로고    scopus 로고
    • Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
    • Y.J. Park Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding J. Biol. Chem. 280 2005 1817 1825
    • (2005) J. Biol. Chem. , vol.280 , pp. 1817-1825
    • Park, Y.J.1
  • 28
    • 0028799432 scopus 로고
    • Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer
    • P.P. Walter Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer Mol. Cell. Biol. 15 1995 6178 6187
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6178-6187
    • Walter, P.P.1
  • 29
    • 0347539781 scopus 로고    scopus 로고
    • Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities
    • M. Bruno Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities Mol. Cell 12 2003 1599 1606
    • (2003) Mol. Cell , vol.12 , pp. 1599-1606
    • Bruno, M.1
  • 30
    • 0033898468 scopus 로고    scopus 로고
    • P300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone
    • T. Ito p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone Genes Dev. 14 2000 1899 1907
    • (2000) Genes Dev. , vol.14 , pp. 1899-1907
    • Ito, T.1
  • 31
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • G. Mizuguchi 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
  • 32
    • 19944427674 scopus 로고    scopus 로고
    • Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA
    • R. Zhang Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA Dev. Cell 8 2005 19 30
    • (2005) Dev. Cell , vol.8 , pp. 19-30
    • Zhang, R.1
  • 33
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
    • M.S. Kobor A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin PLoS Biol. 2 2004 E131
    • (2004) PLoS Biol. , vol.2 , pp. 131
    • Kobor, M.S.1
  • 34
    • 4544262211 scopus 로고    scopus 로고
    • Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4
    • N.J. Krogan Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4 Proc. Natl. Acad. Sci. U. S. A. 101 2004 13513 13518
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13513-13518
    • Krogan, N.J.1
  • 35
    • 11144355550 scopus 로고    scopus 로고
    • SWRred not shaken; Mixing the histones
    • P. Korber, and W. Horz SWRred not shaken; mixing the histones Cell 117 2004 5 7
    • (2004) Cell , vol.117 , pp. 5-7
    • Korber, P.1    Horz, W.2
  • 36
    • 20244385811 scopus 로고    scopus 로고
    • The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes
    • Y. Cai The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes J. Biol. Chem. 280 2005 13665 13670
    • (2005) J. Biol. Chem. , vol.280 , pp. 13665-13670
    • Cai, Y.1
  • 37
    • 10844233155 scopus 로고    scopus 로고
    • Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions
    • T. Kusch Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions Science 306 2004 2084 2087
    • (2004) Science , vol.306 , pp. 2084-2087
    • Kusch, T.1
  • 38
    • 10944233962 scopus 로고    scopus 로고
    • Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair
    • H. van Attikum Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair Cell 119 2004 777 788
    • (2004) Cell , vol.119 , pp. 777-788
    • Van Attikum, H.1
  • 39
    • 10944224673 scopus 로고    scopus 로고
    • INO80 and γ-H2AX interaction links ATP-dependent chromatin remodeling to DNA damage repair
    • A.J. Morrison INO80 and γ-H2AX interaction links ATP-dependent chromatin remodeling to DNA damage repair Cell 119 2004 767 775
    • (2004) Cell , vol.119 , pp. 767-775
    • Morrison, A.J.1
  • 40
    • 10944267160 scopus 로고    scopus 로고
    • Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites
    • J.A. Downs Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites Mol. Cell 16 2004 979 990
    • (2004) Mol. Cell , vol.16 , pp. 979-990
    • Downs, J.A.1
  • 41
    • 0037179692 scopus 로고    scopus 로고
    • Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair
    • A.W. Bird Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair Nature 419 2002 411 415
    • (2002) Nature , vol.419 , pp. 411-415
    • Bird, A.W.1
  • 42
    • 0036889332 scopus 로고    scopus 로고
    • NuA4 subunit Yng2 function in intra-S-phase DNA damage response
    • J.S. Choy, and S.J. Kron NuA4 subunit Yng2 function in intra-S-phase DNA damage response Mol. Cell. Biol. 22 2002 8215 8225
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8215-8225
    • Choy, J.S.1    Kron, S.J.2
  • 43
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • T. Ikura Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis Cell 102 2000 463 473
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1
  • 44
    • 0036712095 scopus 로고    scopus 로고
    • DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis
    • J.P. Madigan DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis Nucleic Acids Res. 30 2002 3698 3705
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3698-3705
    • Madigan, J.P.1
  • 45
    • 9144269660 scopus 로고    scopus 로고
    • A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1
    • N.J. Krogan A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1 Mol. Cell 12 2003 1565 1576
    • (2003) Mol. Cell , vol.12 , pp. 1565-1576
    • Krogan, N.J.1
  • 46
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • H.S. Malik, and S. Henikoff Phylogenomics of the nucleosome Nat. Struct. Biol. 10 2003 882 891
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 47
    • 0036591877 scopus 로고    scopus 로고
    • Centromeres and variant histones: What, where, when and why?
    • M.M. Smith Centromeres and variant histones: what, where, when and why? Curr. Opin. Cell Biol. 14 2002 279 285
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 279-285
    • Smith, M.M.1
  • 48
    • 17044394787 scopus 로고    scopus 로고
    • Transcriptional activation triggers deposition and removal of the histone variant H3.3
    • B.E. Schwartz, and K. Ahmad Transcriptional activation triggers deposition and removal of the histone variant H3.3 Genes Dev. 19 2005 804 814
    • (2005) Genes Dev. , vol.19 , pp. 804-814
    • Schwartz, B.E.1    Ahmad, K.2
  • 49
    • 23744460663 scopus 로고    scopus 로고
    • Variant histone H3.3 is deposited at sites of nucleosomal displacement throughout transcribed genes while active histone modifications show a promoter-proximal bias
    • C. Wirbelauer Variant histone H3.3 is deposited at sites of nucleosomal displacement throughout transcribed genes while active histone modifications show a promoter-proximal bias Genes Dev. 19 2005 1761 1766
    • (2005) Genes Dev. , vol.19 , pp. 1761-1766
    • Wirbelauer, C.1
  • 50
    • 8644287437 scopus 로고    scopus 로고
    • Evidence for eviction and rapid deposition of histones upon transcriptional elongation by RNA polymerase II
    • M.A. Schwabish, and K. Struhl Evidence for eviction and rapid deposition of histones upon transcriptional elongation by RNA polymerase II Mol. Cell. Biol. 24 2004 10111 10117
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10111-10117
    • Schwabish, M.A.1    Struhl, K.2
  • 51
    • 22544450837 scopus 로고    scopus 로고
    • Histones are incorporated in trans during reassembly of the yeast PHO5 promoter
    • U.J. Schermer Histones are incorporated in trans during reassembly of the yeast PHO5 promoter Mol. Cell 19 2005 279 285
    • (2005) Mol. Cell , vol.19 , pp. 279-285
    • Schermer, U.J.1
  • 52
    • 15444376394 scopus 로고    scopus 로고
    • Replication-independent core histone dynamics at transcriptionally active loci in vivo
    • C. Thiriet, and J.J. Hayes Replication-independent core histone dynamics at transcriptionally active loci in vivo Genes Dev. 19 2005 677 682
    • (2005) Genes Dev. , vol.19 , pp. 677-682
    • Thiriet, C.1    Hayes, J.J.2
  • 53
    • 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
    • H. Kimura, and P.R. Cook Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B J. Cell Biol. 153 2001 1341 1353
    • (2001) J. Cell Biol. , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 54
    • 1242342240 scopus 로고    scopus 로고
    • Histone H3.3 is enriched in covalent modifications associated with active chromatin
    • E. McKittrick Histone H3.3 is enriched in covalent modifications associated with active chromatin Proc. Natl. Acad. Sci. U. S. A. 101 2004 1525 1530
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1525-1530
    • McKittrick, E.1
  • 55
    • 1542298307 scopus 로고    scopus 로고
    • Histone chaperones, a supporting role in the limelight
    • A. Loyola, and G. Almouzni Histone chaperones, a supporting role in the limelight Biochim. Biophys. Acta 1677 2004 3 11
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 3-11
    • Loyola, A.1    Almouzni, G.2
  • 56
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution
    • C.A. Davey Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution J. Mol. Biol. 319 2002 1097 1113
    • (2002) J. Mol. Biol. , vol.319 , pp. 1097-1113
    • Davey, C.A.1
  • 57
    • 18144370095 scopus 로고    scopus 로고
    • Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes
    • S.B. Hake Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes Proc. Natl. Acad. Sci. U. S. A. 102 2005 6344 6349
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6344-6349
    • Hake, S.B.1
  • 58
    • 3042794631 scopus 로고    scopus 로고
    • Building the centromere: From foundation proteins to 3D organization
    • D.J. Amor Building the centromere: from foundation proteins to 3D organization Trends Cell Biol. 14 2004 359 368
    • (2004) Trends Cell Biol. , vol.14 , pp. 359-368
    • Amor, D.J.1
  • 59
    • 4544275776 scopus 로고    scopus 로고
    • Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres
    • T. Hayashi Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres Cell 118 2004 715 729
    • (2004) Cell , vol.118 , pp. 715-729
    • Hayashi, T.1
  • 60
    • 20144376151 scopus 로고    scopus 로고
    • The CHD remodeling factor Hrp1 stimulates CENP-A loading to centromeres
    • J. Walfridsson The CHD remodeling factor Hrp1 stimulates CENP-A loading to centromeres Nucleic Acids Res. 33 2005 2868 2879
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2868-2879
    • Walfridsson, J.1
  • 61
    • 7944224836 scopus 로고    scopus 로고
    • Proteolysis contributes to the exclusive centromere localization of the yeast Cse4/CENP-A histone H3 variant
    • K.A. Collins Proteolysis contributes to the exclusive centromere localization of the yeast Cse4/CENP-A histone H3 variant Curr. Biol. 14 2004 1968 1972
    • (2004) Curr. Biol. , vol.14 , pp. 1968-1972
    • Collins, K.A.1
  • 62
    • 1942439646 scopus 로고    scopus 로고
    • The highly conserved and multifunctional NuA4 HAT complex
    • Y. Doyon, and J. Cote The highly conserved and multifunctional NuA4 HAT complex Curr. Opin. Genet. Dev. 14 2004 147 154
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 147-154
    • Doyon, Y.1    Cote, J.2
  • 63
    • 1342327654 scopus 로고    scopus 로고
    • Fission yeast Arp6 is required for telomere silencing, but functions independently of Swi6
    • M. Ueno Fission yeast Arp6 is required for telomere silencing, but functions independently of Swi6 Nucleic Acids Res. 32 2004 736 741
    • (2004) Nucleic Acids Res. , vol.32 , pp. 736-741
    • Ueno, M.1
  • 64
    • 4143093789 scopus 로고    scopus 로고
    • Actin and ARPs: Action in the nucleus
    • C.A. Blessing Actin and ARPs: action in the nucleus Trends Cell Biol. 14 2004 435 442
    • (2004) Trends Cell Biol. , vol.14 , pp. 435-442
    • Blessing, C.A.1
  • 65
    • 8644257491 scopus 로고    scopus 로고
    • Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex
    • Z.O. Jonsson Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex Mol. Cell 16 2004 465 477
    • (2004) Mol. Cell , vol.16 , pp. 465-477
    • Jonsson, Z.O.1
  • 66
    • 0033945861 scopus 로고    scopus 로고
    • DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci
    • M.R. Rountree DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci Nat. Genet. 25 2000 269 277
    • (2000) Nat. Genet. , vol.25 , pp. 269-277
    • Rountree, M.R.1
  • 67
    • 6344279816 scopus 로고    scopus 로고
    • The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres
    • H. Zhang The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres Mol. Cell. Biol. 24 2004 9424 9436
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9424-9436
    • Zhang, H.1
  • 68
    • 0242322038 scopus 로고    scopus 로고
    • Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex
    • Y. Cai Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex J. Biol. Chem. 278 2003 42733 42736
    • (2003) J. Biol. Chem. , vol.278 , pp. 42733-42736
    • Cai, Y.1
  • 69
    • 19944431321 scopus 로고    scopus 로고
    • A novel repressive E2F6 complex containing the polycomb group protein, EPC1, that interacts with EZH2 in a proliferation-specific manner
    • C. Attwooll A novel repressive E2F6 complex containing the polycomb group protein, EPC1, that interacts with EZH2 in a proliferation-specific manner J. Biol. Chem. 280 2005 1199 1208
    • (2005) J. Biol. Chem. , vol.280 , pp. 1199-1208
    • Attwooll, C.1
  • 70
    • 1342346531 scopus 로고    scopus 로고
    • Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans
    • Y. Doyon Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans Mol. Cell. Biol. 24 2004 1884 1896
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1884-1896
    • Doyon, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.