메뉴 건너뛰기




Volumn 49, Issue 19, 2010, Pages 4018-4026

Histone variant H2A.Z inhibits transcription in reconstituted nucleosomes

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL FUNCTIONS; DNA-TEMPLATE; HISTONE VARIANTS; NUCLEOSOMES; RESIDUAL LEVELS; RNA POLYMERASE;

EID: 77952378219     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1001618     Document Type: Article
Times cited : (16)

References (51)
  • 1
    • 37249012276 scopus 로고    scopus 로고
    • Nucleosome destabilization in the epigenetic regulation of gene expression
    • Henikoff, S. (2008) Nucleosome destabilization in the epigenetic regulation of gene expression Nat. Rev. Genet. 9, 15-26
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 15-26
    • Henikoff, S.1
  • 3
    • 0017365534 scopus 로고
    • Non-allelic variants of histones 2a, 2b and 3 in mammals
    • Franklin, S. G. and Zweidler, A. (1977) Non-allelic variants of histones 2a, 2b and 3 in mammals Nature 266, 273-275
    • (1977) Nature , vol.266 , pp. 273-275
    • Franklin, S.G.1    Zweidler, A.2
  • 4
    • 38949091078 scopus 로고    scopus 로고
    • H2A.Z: View from the top
    • Zlatanova, J. and Thakar, A. (2008) H2A.Z: view from the top Structure 16, 166-179
    • (2008) Structure , vol.16 , pp. 166-179
    • Zlatanova, J.1    Thakar, A.2
  • 5
    • 33947098453 scopus 로고    scopus 로고
    • Histone replacement marks the boundaries of cis-regulatory domains
    • Mito, Y., Henikoff, J. G., and Henikoff, S. (2007) Histone replacement marks the boundaries of cis-regulatory domains Science 315, 1408-1411
    • (2007) Science , vol.315 , pp. 1408-1411
    • Mito, Y.1    Henikoff, J.G.2    Henikoff, S.3
  • 6
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication- independent nucleosome assembly
    • Ahmad, K. and Henikoff, S. (2002) The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly Mol. Cell 9, 1191-1200
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 7
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profiling of histone H3.3 replacement patterns
    • Mito, Y., Henikoff, J. G., and Henikoff, S. (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
  • 8
    • 33947137710 scopus 로고    scopus 로고
    • Dynamics of replication-independent histone turnover in budding yeast
    • Dion, M. F., Kaplan, T., Kim, M., Buratowski, S., Friedman, N., and Rando, O. J. (2007) Dynamics of replication-independent histone turnover in budding yeast Science 315, 1405-1408
    • (2007) Science , vol.315 , pp. 1405-1408
    • Dion, M.F.1    Kaplan, T.2    Kim, M.3    Buratowski, S.4    Friedman, N.5    Rando, O.J.6
  • 11
    • 66449128244 scopus 로고    scopus 로고
    • Comparative analysis of H2A.Z nucleosome organization in the human and yeast genomes
    • Tolstorukov, M. Y., Kharchenko, P. V., Goldman, J. A., Kingston, R. E., and Park, P. J. (2009) Comparative analysis of H2A.Z nucleosome organization in the human and yeast genomes Genome Res. 19, 967-977
    • (2009) Genome Res. , vol.19 , pp. 967-977
    • Tolstorukov, M.Y.1    Kharchenko, P.V.2    Goldman, J.A.3    Kingston, R.E.4    Park, P.J.5
  • 12
    • 34250745886 scopus 로고    scopus 로고
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z
    • Jin, C. and Felsenfeld, G. (2007) Nucleosome stability mediated by histone variants H3.3 and H2A.Z Genes Dev. 21, 1519-1529
    • (2007) Genes Dev. , vol.21 , pp. 1519-1529
    • Jin, C.1    Felsenfeld, G.2
  • 13
    • 68149150830 scopus 로고    scopus 로고
    • H3.3/H2A.Z double variant-containing nucleosomes mark "nucleosome-free regions" of active promoters and other regulatory regions
    • Jin, C., Zang, C., Wei, G., Cui, K., Peng, W., Zhao, K., and Felsenfeld, G. (2009) H3.3/H2A.Z double variant-containing nucleosomes mark "nucleosome-free regions" of active promoters and other regulatory regions Nat. Genet. 41, 941-945
    • (2009) Nat. Genet. , vol.41 , pp. 941-945
    • Jin, C.1    Zang, C.2    Wei, G.3    Cui, K.4    Peng, W.5    Zhao, K.6    Felsenfeld, G.7
  • 14
    • 0026512523 scopus 로고
    • Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase
    • O'Neill, T. E., Roberge, M., and Bradbury, E. M. (1992) Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase J. Mol. Biol. 223, 67-78
    • (1992) J. Mol. Biol. , vol.223 , pp. 67-78
    • O'Neill, T.E.1    Roberge, M.2    Bradbury, E.M.3
  • 15
    • 0028125847 scopus 로고
    • A histone octamer can step around a transcribing polymerase without leaving the template
    • Studitsky, V. M., Clark, D. J., and Felsenfeld, G. (1994) A histone octamer can step around a transcribing polymerase without leaving the template Cell 76, 371-382
    • (1994) Cell , vol.76 , pp. 371-382
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 18
    • 0039765281 scopus 로고    scopus 로고
    • In vitro studies on the maintenance of transcription-induced stress by histones and polyamines
    • Peng, H. F. and Jackson, V. (2000) In vitro studies on the maintenance of transcription-induced stress by histones and polyamines J. Biol. Chem. 275, 657-668
    • (2000) J. Biol. Chem. , vol.275 , pp. 657-668
    • Peng, H.F.1    Jackson, V.2
  • 19
    • 0028872728 scopus 로고
    • Binding of disparate transcriptional activators to nucleosomal DNA is inherently cooperative
    • Adams, C. C. and Workman, J. L. (1995) Binding of disparate transcriptional activators to nucleosomal DNA is inherently cooperative Mol. Cell. Biol. 15, 1405-1421
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1405-1421
    • Adams, C.C.1    Workman, J.L.2
  • 20
    • 0032584136 scopus 로고    scopus 로고
    • Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner
    • An, W., Leuba, S. H., van Holde, K., and Zlatanova, J. (1998) Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner Proc. Natl. Acad. Sci. U.S.A. 95, 3396-3401
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3396-3401
    • An, W.1    Leuba, S.H.2    Van Holde, K.3    Zlatanova, J.4
  • 21
    • 33745107476 scopus 로고    scopus 로고
    • The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling
    • Frehlick, L. J., Eirin-Lopez, J. M., Jeffery, E. D., Hunt, D. F., and Ausio, J. (2006) The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling BMC Genomics 7, 99
    • (2006) BMC Genomics , vol.7 , pp. 99
    • Frehlick, L.J.1    Eirin-Lopez, J.M.2    Jeffery, E.D.3    Hunt, D.F.4    Ausio, J.5
  • 22
    • 0033289822 scopus 로고    scopus 로고
    • Expression and purification of recombinant histones and nucleosome reconstitution
    • Luger, K., Rechsteiner, T. J., and Richmond, T. J. (1999) Expression and purification of recombinant histones and nucleosome reconstitution Methods Mol. Biol. 119, 1-16
    • (1999) Methods Mol. Biol. , vol.119 , pp. 1-16
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 23
    • 0017287549 scopus 로고
    • Correlation between structural transformation and cleavage of the major head protein of T4 bacteriophage
    • Laemmli, U. K., Amos, L. A., and Klug, A. (1976) Correlation between structural transformation and cleavage of the major head protein of T4 bacteriophage Cell 7, 191-203
    • (1976) Cell , vol.7 , pp. 191-203
    • Laemmli, U.K.1    Amos, L.A.2    Klug, A.3
  • 24
    • 0025063459 scopus 로고
    • Chromatin reconstitution on small DNA rings. III. Histone H5 dependence of DNA supercoiling in the nucleosome
    • Zivanovic, Y., Duband-Goulet, I., Schultz, P., Stofer, E., Oudet, P., and Prunell, A. (1990) Chromatin reconstitution on small DNA rings. III. Histone H5 dependence of DNA supercoiling in the nucleosome J. Mol. Biol. 214, 479-495
    • (1990) J. Mol. Biol. , vol.214 , pp. 479-495
    • Zivanovic, Y.1    Duband-Goulet, I.2    Schultz, P.3    Stofer, E.4    Oudet, P.5    Prunell, A.6
  • 25
    • 0035659506 scopus 로고    scopus 로고
    • The archaeal histone-fold protein HMf organizes DNA into bona fide chromatin fibers
    • Tomschik, M., Karymov, M. A., Zlatanova, J., and Leuba, S. H. (2001) The archaeal histone-fold protein HMf organizes DNA into bona fide chromatin fibers Structure 9, 1201-1211
    • (2001) Structure , vol.9 , pp. 1201-1211
    • Tomschik, M.1    Karymov, M.A.2    Zlatanova, J.3    Leuba, S.H.4
  • 26
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å 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
  • 27
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R. K., Clarkson, M. J., Tremethick, D. J., and Luger, K. (2000) Crystal structure of a nucleosome core particle containing the variant histone H2A.Z Nat. Struct. Biol. 7, 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
  • 28
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: A model system for study of higher order structure
    • Simpson, R. T., Thoma, F., and Brubaker, J. M. (1985) Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: a model system for study of higher order structure Cell 42, 799-808
    • (1985) Cell , vol.42 , pp. 799-808
    • Simpson, R.T.1    Thoma, F.2    Brubaker, J.M.3
  • 29
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription
    • Kireeva, M. L., Walter, W., Tchernajenko, V., Bondarenko, V., Kashlev, M., and Studitsky, V. M. (2002) Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription Mol. Cell 9, 541-552
    • (2002) Mol. Cell , vol.9 , pp. 541-552
    • Kireeva, M.L.1    Walter, W.2    Tchernajenko, V.3    Bondarenko, V.4    Kashlev, M.5    Studitsky, V.M.6
  • 31
    • 0025877255 scopus 로고
    • Transcription on nucleosomal templates by RNA polymerase II in vitro: Inhibition of elongation with enhancement of sequence-specific pausing
    • Izban, M. G. and Luse, D. S. (1991) Transcription on nucleosomal templates by RNA polymerase II in vitro: inhibition of elongation with enhancement of sequence-specific pausing Genes Dev. 5, 683-696
    • (1991) Genes Dev. , vol.5 , pp. 683-696
    • Izban, M.G.1    Luse, D.S.2
  • 32
    • 0025916330 scopus 로고
    • Chromatosome positioning on assembled long chromatin. Linker histones affect nucleosome placement on 5 S rDNA
    • Meersseman, G., Pennings, S., and Bradbury, E. M. (1991) Chromatosome positioning on assembled long chromatin. Linker histones affect nucleosome placement on 5 S rDNA J. Mol. Biol. 220, 89-100
    • (1991) J. Mol. Biol. , vol.220 , pp. 89-100
    • Meersseman, G.1    Pennings, S.2    Bradbury, E.M.3
  • 33
    • 0029151148 scopus 로고
    • DNA at the entry-exit of the nucleosome observed by cryoelectron microscopy
    • Furrer, P., Bednar, J., Dubochet, J., Hamiche, A., and Prunell, A. (1995) DNA at the entry-exit of the nucleosome observed by cryoelectron microscopy J. Struct. Biol. 114, 177-183
    • (1995) J. Struct. Biol. , vol.114 , pp. 177-183
    • Furrer, P.1    Bednar, J.2    Dubochet, J.3    Hamiche, A.4    Prunell, A.5
  • 34
    • 29444454191 scopus 로고    scopus 로고
    • Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling
    • Li, B., Pattenden, S. G., Lee, D., Gutierrez, J., Chen, J., Seidel, C., Gerton, J., and Workman, J. L. (2005) Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling Proc. Natl. Acad. Sci. U.S.A. 102, 18385-18390
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 35
    • 0036183219 scopus 로고    scopus 로고
    • The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states
    • Fan, J. Y., Gordon, F., Luger, K., Hansen, J. C., and Tremethick, D. J. (2002) The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states Nat. Struct. Biol. 9, 172-176
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 172-176
    • Fan, J.Y.1    Gordon, F.2    Luger, K.3    Hansen, J.C.4    Tremethick, D.J.5
  • 36
    • 0026546508 scopus 로고
    • Chromatin reconstitution on small DNA rings. IV. DNA supercoiling and nucleosome sequence preference
    • Duband-Goulet, I., Carot, V., Ulyanov, A. V., Douc-Rasy, S., and Prunell, A. (1992) Chromatin reconstitution on small DNA rings. IV. DNA supercoiling and nucleosome sequence preference J. Mol. Biol. 224, 981-1001
    • (1992) J. Mol. Biol. , vol.224 , pp. 981-1001
    • Duband-Goulet, I.1    Carot, V.2    Ulyanov, A.V.3    Douc-Rasy, S.4    Prunell, A.5
  • 39
    • 70349292569 scopus 로고    scopus 로고
    • Histone H2A.Z cooperates with RNAi and heterochromatin factors to suppress antisense RNAs
    • Zofall, M., Fischer, T., Zhang, K., Zhou, M., Cui, B., Veenstra, T. D., and Grewal, S. I. (2009) Histone H2A.Z cooperates with RNAi and heterochromatin factors to suppress antisense RNAs Nature 461, 419-422
    • (2009) Nature , vol.461 , pp. 419-422
    • Zofall, M.1    Fischer, T.2    Zhang, K.3    Zhou, M.4    Cui, B.5    Veenstra, T.D.6    Grewal, S.I.7
  • 41
    • 73149085055 scopus 로고    scopus 로고
    • H2A.Z-containing nucleosomes mediate the thermosensory response in Arabidopsis
    • Kumar, S. V. and Wiggle, P. A. (2010) H2A.Z-containing nucleosomes mediate the thermosensory response in Arabidopsis Cell 140, 136-147
    • (2010) Cell , vol.140 , pp. 136-147
    • Kumar, S.V.1    Wiggle, P.A.2
  • 42
    • 66649092628 scopus 로고    scopus 로고
    • Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome
    • Ishibashi, T., Dryhurst, D., Rose, K. L., Shabanowitz, J., Hunt, D. F., and Ausio, J. (2009) Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome Biochemistry 48, 5007-5017
    • (2009) Biochemistry , vol.48 , pp. 5007-5017
    • Ishibashi, T.1    Dryhurst, D.2    Rose, K.L.3    Shabanowitz, J.4    Hunt, D.F.5    Ausio, J.6
  • 45
    • 0021718495 scopus 로고
    • 2. Solubility and binding studies, transition to and characterization of the higher-order structure
    • 2. Solubility and binding studies, transition to and characterization of the higher-order structure J. Mol. Biol. 177, 373-398
    • (1984) J. Mol. Biol. , vol.177 , pp. 373-398
    • Ausio, J.1    Borochov, N.2    Seger, D.3    Eisenberg, H.4
  • 46
    • 0034734277 scopus 로고    scopus 로고
    • Analytical ultracentrifugation and the characterization of chromatin structure
    • Ausio, J. (2000) Analytical ultracentrifugation and the characterization of chromatin structure Biophys. Chem. 86, 141-153
    • (2000) Biophys. Chem. , vol.86 , pp. 141-153
    • Ausio, J.1
  • 47
    • 33747351584 scopus 로고    scopus 로고
    • Full and partial genome-wide assembly and disassembly of the yeast transcription machinery in response to heat shock
    • Zanton, S. J. and Pugh, B. F. (2006) Full and partial genome-wide assembly and disassembly of the yeast transcription machinery in response to heat shock Genes Dev. 20, 2250-2265
    • (2006) Genes Dev. , vol.20 , pp. 2250-2265
    • Zanton, S.J.1    Pugh, B.F.2
  • 51
    • 0035659506 scopus 로고    scopus 로고
    • The archaeal histone-fold protein HMf organizes DNA into bona fide chromatin fibers
    • Tomschik, M., Karymov, M. A., Zlatanova, J., and Leuba, S. H. (2001) The archaeal histone-fold protein HMf organizes DNA into bona fide chromatin fibers Structure 9, 1201-1211
    • (2001) Structure , vol.9 , pp. 1201-1211
    • Tomschik, M.1    Karymov, M.A.2    Zlatanova, J.3    Leuba, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.