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Volumn 8, Issue 1, 2007, Pages 59-66

H2A.Z-mediated genome-wide chromatin specialization

Author keywords

Acetylation; Gene activity; Genome wide distribution; H2A.Z; Heterochromatin; Promoter regions

Indexed keywords

DNA DIRECTED RNA POLYMERASE; DNA DIRECTED RNA POLYMERASE III; HISTONE ACETYLTRANSFERASE GCN5; HISTONE DEACETYLASE; HISTONE H2A; HISTONE H2AX; HISTONE H2AZ; HISTONE H4; NUCLEAR PROTEIN; UNCLASSIFIED DRUG;

EID: 33947650501     PISSN: 13892029     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920207780076965     Document Type: Review
Times cited : (15)

References (39)
  • 1
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • Malik, H.S. and Henikoff, S. Phylogenomics of the nucleosome. Nat. Struct. Biol., 2003, 10: 882-891.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. and Allis, C.D. Translating the histone code. Science, 2001, 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 0142184470 scopus 로고    scopus 로고
    • Colworth memorial lecture. Pathways for remodelling chromatin
    • Owen-Hughes, T. Colworth memorial lecture. Pathways for remodelling chromatin. Biochem. Soc. Trans., 2003, 31: 893-905.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 893-905
    • Owen-Hughes, T.1
  • 4
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Meneghini, M.D., Wu, M. and Madhani, H.D. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell, 2003, 112: 725-736.
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 5
    • 4644311959 scopus 로고    scopus 로고
    • New twists on H2A.Z: A histone variant with a controversial structural and functional past
    • Dryhurst, D.D., Thambirajah, A.A. and Ausió, J. New twists on H2A.Z: a histone variant with a controversial structural and functional past. Biochem. Cell Biol., 2004, 82: 490-497.
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 490-497
    • Dryhurst, D.D.1    Thambirajah, A.A.2    Ausió, J.3
  • 6
    • 33750732646 scopus 로고    scopus 로고
    • Long-range histone acetylation: Biological significance, structural implications, and mechanisms
    • Calestagne-Morelli, A. and Ausio, J. Long-range histone acetylation: biological significance, structural implications, and mechanisms. Biochem. Cell Biol., 2006, 84: 518-527.
    • (2006) Biochem. Cell Biol. , vol.84 , pp. 518-527
    • Calestagne-Morelli, A.1    Ausio, J.2
  • 7
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • Kimura, A., Umehara, T. and Horikoshi, M. Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing. Nat. Genet., 2002, 32: 370-377.
    • (2002) Nat. Genet. , vol.32 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 8
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin
    • Suka, N., Luo, K. and Grunstein, M. Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin. Nat. Genet., 2002, 32: 378-383.
    • (2002) Nat. Genet. , vol.32 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 9
    • 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
    • Ng, H.H., Ciccione, D.N., Morshead, K.B., Oettinger, M.A. and Struhl, K. 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. U.S.A., 2003, 100: 1820-1825.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 1820-1825
    • Ng, H.H.1    Ciccione, D.N.2    Morshead, K.B.3    Oettinger, M.A.4    Struhl, K.5
  • 10
    • 9144253287 scopus 로고    scopus 로고
    • Methylation of H3 lysine 4 at euchromatin promotes Sir3p association with heterochromatin
    • Santos-Rosa, H., Bannister, A.J., Dehe, P.M., Geli, V. and Kouzarides, T. Methylation of H3 lysine 4 at euchromatin promotes Sir3p association with heterochromatin. J. Biol. Chem., 2004, 279: 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
  • 12
    • 0043239320 scopus 로고    scopus 로고
    • H2A.Z has a function reminiscent of an activator required for preferential binding to intergenic DNA
    • Larochelle, M. and Gaudreau, L. H2A.Z has a function reminiscent of an activator required for preferential binding to intergenic DNA. EMBO J., 2003, 22: 4512-4522.
    • (2003) EMBO J. , vol.22 , pp. 4512-4522
    • Larochelle, M.1    Gaudreau, L.2
  • 13
    • 0034721645 scopus 로고    scopus 로고
    • Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes
    • Santisteban, M.S., Kalashnikova, T. and Smith, M.M. Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes. Cell, 2000, 103: 411-422.
    • (2000) Cell , vol.103 , pp. 411-422
    • Santisteban, M.S.1    Kalashnikova, T.2    Smith, M.M.3
  • 17
    • 26844489856 scopus 로고    scopus 로고
    • Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss
    • Zhang, H., Roberts, D.N. and Cairns, B.R. Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss. Cell, 2005, 123: 219-231.
    • (2005) Cell , vol.123 , pp. 219-231
    • Zhang, H.1    Roberts, D.N.2    Cairns, B.R.3
  • 20
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi, G., Shen, X., Landry, J., Hu, W.-H., Sen, S. and Wu, C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science, 2004, 303: 343-348.
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Hu, W.-H.4    Sen, S.5    Wu, C.6
  • 22
    • 33645002813 scopus 로고    scopus 로고
    • Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast
    • Millar, C.B., Xu, F., Zhang, K. and Grunstein, M. Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast. Genes Dev., 2006, 20: 711-722.
    • (2006) Genes Dev. , vol.20 , pp. 711-722
    • Millar, C.B.1    Xu, F.2    Zhang, K.3    Grunstein, M.4
  • 23
    • 33746015346 scopus 로고    scopus 로고
    • H2A.Z sabilizes chromatin in a way that is dependent on core histone acetylation
    • Thambirajah, A.A., Dryhurst, D.D., Ishibashi, T., Li, A., Maffey, A.H. and Ausio, J. H2A.Z sabilizes chromatin in a way that is dependent on core histone acetylation. J. Biol. Chem., 2005, 281: 20036-20044.
    • (2005) J. Biol. Chem. , vol.281 , pp. 20036-20044
    • Thambirajah, A.A.1    Dryhurst, D.D.2    Ishibashi, T.3    Li, A.4    Maffey, A.H.5    Ausio, J.6
  • 24
    • 21644468242 scopus 로고    scopus 로고
    • Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z
    • Farris, S.D., Rubio, E.D., Moon, J.J., Gombert, W.M., Nelson, B.H. and Krumm, A. Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z. J. Biol. Chem., 2005, 280: 25298-25303.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25298-25303
    • Farris, S.D.1    Rubio, E.D.2    Moon, J.J.3    Gombert, W.M.4    Nelson, B.H.5    Krumm, A.6
  • 26
    • 3543023310 scopus 로고    scopus 로고
    • Evidence for nucleosome depletion at active regulatory regions genome-wide
    • Lee, C.K., Shibata, Y., Rao, B., Strahl, B.D. and Lieb, J.D. Evidence for nucleosome depletion at active regulatory regions genome-wide. Nat. Genet., 2004, 36: 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
  • 27
    • 33644999042 scopus 로고    scopus 로고
    • Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae
    • Babiarz, J.E., Halley, J.E. and Rine, J. Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae. Genes Dev., 2006, 20: 700-710.
    • (2006) Genes Dev. , vol.20 , pp. 700-710
    • Babiarz, J.E.1    Halley, J.E.2    Rine, J.3
  • 30
    • 0034307468 scopus 로고    scopus 로고
    • Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants
    • Jackson, J.D. and Gorovsky, M.A. Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucl. Acids Res., 2000, 28: 3811-3816.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 3811-3816
    • Jackson, J.D.1    Gorovsky, M.A.2
  • 31
    • 28544442465 scopus 로고    scopus 로고
    • Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
    • Wu, W.H., Alami, S., Luk, E., Wu, C.H., Sen, S., Mizuguchi, G., Wei, D. and Wu, C. Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat. Struct. Mol. Biol., 2005, 12: 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
  • 32
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global hisone acetylation patterns to gene expression
    • Kurdistani, S.K., Tavazoie, S. and Grunstein, M. Mapping global hisone acetylation patterns to gene expression. Cell, 2004, 117: 721-733.
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 34
    • 22344437987 scopus 로고    scopus 로고
    • Fast and sysematic genome-wide discovery of conserved regulatory elements using a non-aligment based approach
    • Elemento, O. and Tavazoie, S. Fast and sysematic genome-wide discovery of conserved regulatory elements using a non-aligment based approach. Genome Biol., 2005, 6: R18.
    • (2005) Genome Biol. , vol.6
    • Elemento, O.1    Tavazoie, S.2
  • 35
    • 0242322038 scopus 로고    scopus 로고
    • Identification of new subunits of the multprotein mammalian TRRAP /TIP60-containing histone acetyltransferase complex
    • Cai, Y., Jin, J., Tomomori-Sato, C., Sato, S., Sorokina, I., Parmely, T.J., Conaway, R.C. and Conaway, J.W. Identification of new subunits of the multprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. J. Biol. Chem., 2003, 278: 42733-42736.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42733-42736
    • Cai, Y.1    Jin, J.2    Tomomori-Sato, C.3    Sato, S.4    Sorokina, I.5    Parmely, T.J.6    Conaway, R.C.7    Conaway, J.W.8
  • 36
    • 1342346531 scopus 로고    scopus 로고
    • Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans
    • Doyon, Y., Selleck, W., Lane, W.S., Tan, S. and Cote, J. Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol. Cell. Biol., 2004, 24: 1884-1896.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1884-1896
    • Doyon, Y.1    Selleck, W.2    Lane, W.S.3    Tan, S.4    Cote, J.5
  • 37
    • 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
    • Zhang, H., Richardson, D.O., Roberts, D.N., Utley, R., Erdjument-Bromage, H., Tempst, P., Cote, J. and Cairns, B.R. 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., 2004, 24: 9424-9436.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9424-9436
    • Zhang, H.1    Richardson, D.O.2    Roberts, D.N.3    Utley, R.4    Erdjument-Bromage, H.5    Tempst, P.6    Cote, J.7    Cairns, B.R.8
  • 38
    • 33947524604 scopus 로고    scopus 로고
    • Histone variants: The structure behind the function
    • Ausió, J. Histone variants: the structure behind the function. Brief. Funct. Genomic. Proteomic., 2006, 5: 228-243.
    • (2006) Brief. Funct. Genomic. Proteomic. , vol.5 , pp. 228-243
    • Ausió, J.1
  • 39
    • 0030990291 scopus 로고    scopus 로고
    • Molecular model for telomeric heterochromatin in yeast
    • Grunstein, M. Molecular model for telomeric heterochromatin in yeast. Curr. Opin. Cell Biol., 1997, 9: 383-387.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 383-387
    • Grunstein, M.1


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