메뉴 건너뛰기




Volumn 16, Issue 2, 2006, Pages 119-124

Patterning chromatin: Form and function for H2A.Z variant nucleosomes

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2A; PROTEIN HISTONE H2A Z; UNCLASSIFIED DRUG;

EID: 33644850957     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2006.02.005     Document Type: Review
Times cited : (90)

References (38)
  • 1
    • 0028231021 scopus 로고
    • Phylogenetic analysis of the core histones H2A, H2B, H3, and H4
    • T.H. Thatcher, and M.A. Gorovsky Phylogenetic analysis of the core histones H2A, H2B, H3, and H4 Nucleic Acids Res 22 1994 174 179
    • (1994) Nucleic Acids Res , vol.22 , pp. 174-179
    • Thatcher, T.H.1    Gorovsky, M.A.2
  • 2
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • C. Costanzi, and J.R. Pehrson Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals Nature 393 1998 599 601
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 4
    • 0043066728 scopus 로고    scopus 로고
    • Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage
    • C. Redon, D.R. Pilch, E.P. Rogakou, A.H. Orr, N.F. Lowndes, and W.M. Bonner Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage EMBO Rep 4 2003 678 684
    • (2003) EMBO Rep , vol.4 , pp. 678-684
    • Redon, C.1    Pilch, D.R.2    Rogakou, E.P.3    Orr, A.H.4    Lowndes, N.F.5    Bonner, W.M.6
  • 5
    • 0034307468 scopus 로고    scopus 로고
    • Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants
    • J.D. Jackson, and M.A. Gorovsky Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants Nucleic Acids Res 28 2000 3811 3816
    • (2000) Nucleic Acids Res , vol.28 , pp. 3811-3816
    • Jackson, J.D.1    Gorovsky, M.A.2
  • 6
    • 0028139274 scopus 로고
    • Analysis of a histone H2A variant from fission yeast: Evidence for a role in chromosome stability
    • A.M. Carr, S.M. Dorrington, J. Hindley, G.A. Phear, S.J. Aves, and P. Nurse Analysis of a histone H2A variant from fission yeast: evidence for a role in chromosome stability Mol Gen Genet 245 1994 628 635
    • (1994) Mol Gen Genet , vol.245 , pp. 628-635
    • Carr, A.M.1    Dorrington, S.M.2    Hindley, J.3    Phear, G.A.4    Aves, S.J.5    Nurse, P.6
  • 7
    • 0034725587 scopus 로고    scopus 로고
    • Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster
    • T.J. Leach, M. Mazzeo, H.L. Chotkowski, J.P. Madigan, M.G. Wotring, and R.L. Glaser Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster J Biol Chem 275 2000 23267 23272
    • (2000) J Biol Chem , vol.275 , pp. 23267-23272
    • Leach, T.J.1    Mazzeo, M.2    Chotkowski, H.L.3    Madigan, J.P.4    Wotring, M.G.5    Glaser, R.L.6
  • 11
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • R.K. Suto, M.J. Clarkson, D.J. Tremethick, and K. Luger Crystal structure of a nucleosome core particle containing the variant histone H2A.Z 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
  • 12
    • 0035834777 scopus 로고    scopus 로고
    • Characterization of the stability and folding of H2A.Z chromatin particles: Implications for transcriptional activation
    • D.W. Abbott, V.S. Ivanova, X. Wang, W.M. Bonner, and J. Ausio Characterization of the stability and folding of H2A.Z chromatin particles: implications for transcriptional activation J Biol Chem 276 2001 41945 41949
    • (2001) J Biol Chem , vol.276 , pp. 41945-41949
    • Abbott, D.W.1    Ivanova, V.S.2    Wang, X.3    Bonner, W.M.4    Ausio, J.5
  • 13
    • 2642515598 scopus 로고    scopus 로고
    • A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome
    • Y.J. Park, P.N. Dyer, D.J. Tremethick, and K. Luger A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome J Biol Chem 279 2004 24274 24282
    • (2004) J Biol Chem , vol.279 , pp. 24274-24282
    • Park, Y.J.1    Dyer, P.N.2    Tremethick, D.J.3    Luger, K.4
  • 15
    • 26844489856 scopus 로고    scopus 로고
    • Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss
    • H. Zhang, D.N. Roberts, and B.R. Cairns Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss Cell 123 2005 219 231 The authors localize H2A.Z across the yeast genome at the resolution of intergenic regions and open reading frames. A selective enrichment of promoter segments with H2A.Z was found, and this negatively correlated with transcription. On the basis of this observation and the sensitivity of H2A.Z to salt extraction in isolated yeast chromatin, the authors propose that H2A.Z facilitates nucleosome loss during gene induction.
    • (2005) Cell , vol.123 , pp. 219-231
    • Zhang, H.1    Roberts, D.N.2    Cairns, B.R.3
  • 16
    • 0027759372 scopus 로고
    • Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila
    • L.A. Stargell, J. Bowen, C.A. Dadd, P.C. Dedon, M. Davis, R.G. Cook, C.D. Allis, and M.A. Gorovsky Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila Genes Dev 7 1993 2641 2651
    • (1993) Genes Dev , vol.7 , pp. 2641-2651
    • Stargell, L.A.1    Bowen, J.2    Dadd, C.A.3    Dedon, P.C.4    Davis, M.5    Cook, R.G.6    Allis, C.D.7    Gorovsky, M.A.8
  • 17
    • 26844511498 scopus 로고    scopus 로고
    • Histone variant H2A.Z marks the 5′ ends of both active and inactive genes in euchromatin
    • R.M. Raisner, P.D. Hartley, M.D. Meneghini, M.Z. Bao, C.L. Liu, S.L. Schreiber, O.J. Rando, and H.D. Madhani Histone variant H2A.Z marks the 5′ ends of both active and inactive genes in euchromatin Cell 123 2005 233 248 Using chromatin immunoprecipitation and high-density tiling microarrays, the authors demonstrate that two H2A.Z nucleosomes flank a nucleosome-free region at the transcription start site of most genes in yeast euchromatin. This localization is dependent upon histone acetylation and Bdf1 but does not require gene transcription. A 22 bp segment containing a binding site for the Myb-related protein Reb1 and an adjacent dA:dT tract was shown to be sufficient to induce a nucleosome-free region flanked by two H2A.Z nucleosomes.
    • (2005) Cell , vol.123 , pp. 233-248
    • Raisner, R.M.1    Hartley, P.D.2    Meneghini, M.D.3    Bao, M.Z.4    Liu, C.L.5    Schreiber, S.L.6    Rando, O.J.7    Madhani, H.D.8
  • 18
    • 29144531244 scopus 로고    scopus 로고
    • Variant histone H2A.Z Is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning
    • B. Guillemette, A.R. Bataille, N. Gevry, M. Adam, M. Blanchette, F. Robert, and L. Gaudreau Variant histone H2A.Z Is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning PLoS Biol 3 2005 e384 To demonstrate promoter enrichment with H2A.Z, the authors immunoprecipated sonicated S. cerevisiae chromatin with anti-Myc-H2A.Z antibodies and hybridized probes derived from this material to microarrays that contain an oligonucleotide approximately every 300 bp across the genome. Additionally, they used indirect end-labeled micrococcal nuclease-digested DNA to show that there is a small shift in the position of nucleosomes at the GAL1 promoter in an htz1Δ strain.
    • (2005) PLoS Biol , vol.3 , pp. 384
    • Guillemette, B.1    Bataille, A.R.2    Gevry, N.3    Adam, M.4    Blanchette, M.5    Robert, F.6    Gaudreau, L.7
  • 19
    • 0036712095 scopus 로고    scopus 로고
    • DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis
    • J.P. Madigan, H.L. Chotkowski, and R.L. Glaser 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    Chotkowski, H.L.2    Glaser, R.L.3
  • 20
    • 26944498687 scopus 로고    scopus 로고
    • The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken
    • K. Bruce, F.A. Myers, E. Mantouvalou, P. Lefevre, I. Greaves, C. Bonifer, D.J. Tremethick, A.W. Thorne, and C. Crane-Robinson The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken Nucleic Acids Res 33 2005 5633 5639 The authors use chromatin immunoprecipitation for both acetylated and unacetylated forms of H2A.Z in chicken to show that the 5′ ends of both tissue-specific and housekeeping genes are selectively enriched with the acetylated form. Notably, the β-globin insulator element is highly enriched with acetylated H2A.Z.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5633-5639
    • Bruce, K.1    Myers, F.A.2    Mantouvalou, E.3    Lefevre, P.4    Greaves, I.5    Bonifer, C.6    Tremethick, D.J.7    Thorne, A.W.8    Crane-Robinson, C.9
  • 21
    • 0037390327 scopus 로고    scopus 로고
    • Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development
    • D. Rangasamy, L. Berven, P. Ridgway, and D.J. Tremethick Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development EMBO J 22 2003 1599 1607
    • (2003) EMBO J , vol.22 , pp. 1599-1607
    • Rangasamy, D.1    Berven, L.2    Ridgway, P.3    Tremethick, D.J.4
  • 22
    • 3042642001 scopus 로고    scopus 로고
    • RNA interference demonstrates a novel role for H2A.Z in chromosome segregation
    • D. Rangasamy, I. Greaves, and D.J. Tremethick RNA interference demonstrates a novel role for H2A.Z in chromosome segregation Nat Struct Mol Biol 11 2004 650 655 The authors use an inducible RNAi system to demonstrate that H2A.Z is required for proper segregation of chromosomes in mammalian cells.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 650-655
    • Rangasamy, D.1    Greaves, I.2    Tremethick, D.J.3
  • 23
    • 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 The authors demonstrate using in vitro and in vivo assays that a complex containing the Swi2/Snf2-related ATPase Swr1 is responsible for H2A.Z deposition in yeast.
    • (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
  • 25
    • 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, S. Venkatasubrahmanyam, M.D. Meneghini, J.W. Gin, J.L. 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 The authors purify the 13-subunit Swr1-C in yeast and demonstrate that it is required for in vivo deposition of H2A.Z.
    • (2004) PLoS Biol , vol.2 , pp. 131
    • 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
  • 26
    • 10844233155 scopus 로고    scopus 로고
    • Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions
    • T. Kusch, L. Florens, W.H. Macdonald, S.K. Swanson, R.L. Glaser, J.R. Yates III, S.M. Abmayr, M.P. Washburn, and J.L. Workman Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions Science 306 2004 2084 2087 The authors demonstrate that the Drosophila Tip60 complex is responsible for acetylation and exchange of the phosphorylated H2Av histone variant with unphosphorylated H2Av at sites of DNA lesions.
    • (2004) Science , vol.306 , pp. 2084-2087
    • Kusch, T.1    Florens, L.2    MacDonald, W.H.3    Swanson, S.K.4    Glaser, R.L.5    Yates III, J.R.6    Abmayr, S.M.7    Washburn, M.P.8    Workman, J.L.9
  • 27
    • 20244385811 scopus 로고    scopus 로고
    • The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes
    • Y. Cai, J. Jin, L. Florens, S.K. Swanson, T. Kusch, B. Li, J.L. Workman, M.P. Washburn, R.C. Conaway, and J.W. Conaway The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes J Biol Chem 280 2005 13665 13670 The authors purify a mammalian presumptive H2A.Z deposition complex and show that it has subunits homologous to those in the yeast Swr1-C and Drosophila Tip60 complexes.
    • (2005) J Biol Chem , vol.280 , pp. 13665-13670
    • Cai, Y.1    Jin, J.2    Florens, L.3    Swanson, S.K.4    Kusch, T.5    Li, B.6    Workman, J.L.7    Washburn, M.P.8    Conaway, R.C.9    Conaway, J.W.10
  • 28
    • 0034721645 scopus 로고    scopus 로고
    • Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes
    • M.S. Santisteban, T. Kalashnikova, and M.M. Smith Histone H2A.Z regulats 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
  • 29
    • 0035725036 scopus 로고    scopus 로고
    • H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions
    • M. Adam, F. Robert, M. Larochelle, and L. Gaudreau H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions Mol Cell Biol 21 2001 6270 6279
    • (2001) Mol Cell Biol , vol.21 , pp. 6270-6279
    • Adam, M.1    Robert, F.2    Larochelle, M.3    Gaudreau, L.4
  • 31
    • 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
  • 32
    • 0027058961 scopus 로고
    • A histone variant, H2AvD, is essential in Drosophila melanogaster
    • A. van Daal, and S.C. Elgin A histone variant, H2AvD, is essential in Drosophila melanogaster Mol Biol Cell 3 1992 593 602
    • (1992) Mol Biol Cell , vol.3 , pp. 593-602
    • Van Daal, A.1    Elgin, S.C.2
  • 34
    • 11844295965 scopus 로고    scopus 로고
    • The role of histone H2Av variant replacement and histone H4 acetylation in the establishment of Drosophila heterochromatin
    • J. Swaminathan, E.M. Baxter, and V.G. Corces 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    Baxter, E.M.2    Corces, V.G.3
  • 35
    • 6344277345 scopus 로고    scopus 로고
    • Unique residues on the H2A.Z containing nucleosome surface are important for Xenopus laevis development
    • P. Ridgway, K.D. Brown, D. Rangasamy, U. Svensson, and D.J. Tremethick Unique residues on the H2A.Z containing nucleosome surface are important for Xenopus laevis development J Biol Chem 279 2004 43815 43820 Using immunofluorescence, RNAi and mutant alleles, the authors show that H2A.Z is localized in a tissue-specific manner and is required for proper Xenopus laevis development.
    • (2004) J Biol Chem , vol.279 , pp. 43815-43820
    • Ridgway, P.1    Brown, K.D.2    Rangasamy, D.3    Svensson, U.4    Tremethick, D.J.5
  • 36
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • L.N. Rusche, A.L. Kirchmaier, and J. Rine The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae Annu Rev Biochem 72 2003 481 516
    • (2003) Annu Rev Biochem , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 37
    • 28544442465 scopus 로고    scopus 로고
    • Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
    • W.H. Wu, S. Alami, E. Luk, C.H. Wu, S. Sen, G. Mizuguchi, D. Wei, and C. Wu Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange Nat Struct Mol Biol 12 2005 1064 1071
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1064-1071
    • Wu, W.H.1    Alami, S.2    Luk, E.3    Wu, C.H.4    Sen, S.5    Mizuguchi, G.6    Wei, D.7    Wu, C.8
  • 38
    • 29444454191 scopus 로고    scopus 로고
    • Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling
    • B. Li, S.G. Pattenden, D. Lee, J. Gutierrez, J. Chen, C. Seidel, J. Gerton, and J.L. Workman Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling Proc Natl Acad Sci USA 102 2005 18385 18390
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18385-18390
    • Li, B.1    Pattenden, S.G.2    Lee, D.3    Gutierrez, J.4    Chen, J.5    Seidel, C.6    Gerton, J.7    Workman, J.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.