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Volumn 1819, Issue 3-4, 2012, Pages 230-237

Chaperoning the histone H3 family

Author keywords

Histone chaperones, chromatin assembly; Histone variants

Indexed keywords

CENTROMERE PROTEIN A; CHAPERONE; CYCLINE; DAXX PROTEIN; EPITOPE; HISTONE H3; HISTONE H4; UNCOUPLING PROTEIN;

EID: 84857122396     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2011.08.009     Document Type: Review
Times cited : (30)

References (102)
  • 1
    • 0035313770 scopus 로고    scopus 로고
    • Higher-order structure of chromatin and chromosomes
    • Woodcock C.L., Dimitrov S. Higher-order structure of chromatin and chromosomes. Curr. Opin. Genet. Dev. 2001, 11:130-135.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 130-135
    • Woodcock, C.L.1    Dimitrov, S.2
  • 2
  • 3
    • 0018221572 scopus 로고
    • Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
    • Laskey R.A., Honda B.M., Mills A.D., Finch J.T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature 1978, 275:416-420.
    • (1978) Nature , vol.275 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 4
    • 77955794751 scopus 로고    scopus 로고
    • The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms
    • Postberg J., Forcob S., Chang W.J., Lipps H.J. The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms. BMC Evol. Biol. 2010, 10:259.
    • (2010) BMC Evol. Biol. , vol.10 , pp. 259
    • Postberg, J.1    Forcob, S.2    Chang, W.J.3    Lipps, H.J.4
  • 6
    • 79959736810 scopus 로고    scopus 로고
    • H3.5 is a novel hominid-specific histone H3 variant that is specifically expressed in the seminiferous tubules of human testes
    • Schenk R., Jenke A., Zilbauer M., Wirth S., Postberg J. H3.5 is a novel hominid-specific histone H3 variant that is specifically expressed in the seminiferous tubules of human testes. Chromosoma 2011, 120:275-285.
    • (2011) Chromosoma , vol.120 , pp. 275-285
    • Schenk, R.1    Jenke, A.2    Zilbauer, M.3    Wirth, S.4    Postberg, J.5
  • 8
    • 0036250827 scopus 로고    scopus 로고
    • Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway
    • Mello J.A., Sillje H.H., Roche D.M., Kirschner D.B., Nigg E.A., Almouzni G. Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway. EMBO Rep. 2002, 3:329-334.
    • (2002) EMBO Rep. , vol.3 , pp. 329-334
    • Mello, J.A.1    Sillje, H.H.2    Roche, D.M.3    Kirschner, D.B.4    Nigg, E.A.5    Almouzni, G.6
  • 9
    • 12344321682 scopus 로고    scopus 로고
    • Human Asf1 regulates the flow of S phase histones during replicational stress
    • Groth A., Ray-Gallet D., Quivy J.P., Lukas J., Bartek J., Almouzni G. Human Asf1 regulates the flow of S phase histones during replicational stress. Mol. Cell 2005, 17:301-311.
    • (2005) Mol. Cell , vol.17 , pp. 301-311
    • Groth, A.1    Ray-Gallet, D.2    Quivy, J.P.3    Lukas, J.4    Bartek, J.5    Almouzni, G.6
  • 11
    • 25144465002 scopus 로고    scopus 로고
    • Functional conservation and specialization among eukaryotic anti-silencing function 1 histone chaperones
    • Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K. Functional conservation and specialization among eukaryotic anti-silencing function 1 histone chaperones. Eukaryot. Cell 2005, 4:1583-1590.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1583-1590
    • Tamburini, B.A.1    Carson, J.J.2    Adkins, M.W.3    Tyler, J.K.4
  • 12
    • 27144453690 scopus 로고    scopus 로고
    • ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA
    • English C.M., Maluf N.K., Tripet B., Churchill M.E., Tyler J.K. ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. Biochemistry 2005, 44:13673-13682.
    • (2005) Biochemistry , vol.44 , pp. 13673-13682
    • English, C.M.1    Maluf, N.K.2    Tripet, B.3    Churchill, M.E.4    Tyler, J.K.5
  • 14
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • Natsume R., Eitoku M., Akai Y., Sano N., Horikoshi M., Senda T. Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4. Nature 2007, 446:338-341.
    • (2007) Nature , vol.446 , pp. 338-341
    • Natsume, R.1    Eitoku, M.2    Akai, Y.3    Sano, N.4    Horikoshi, M.5    Senda, T.6
  • 15
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell 2004, 116:51-61.
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 17
    • 77649268110 scopus 로고    scopus 로고
    • Replication stress interferes with histone recycling and predeposition marking of new histones
    • Jasencakova Z., Scharf A.N., Ask K., Corpet A., Imhof A., Almouzni G., Groth A. Replication stress interferes with histone recycling and predeposition marking of new histones. Mol. Cell 2010, 37:736-743.
    • (2010) Mol. Cell , vol.37 , pp. 736-743
    • Jasencakova, Z.1    Scharf, A.N.2    Ask, K.3    Corpet, A.4    Imhof, A.5    Almouzni, G.6    Groth, A.7
  • 19
    • 1942502859 scopus 로고    scopus 로고
    • The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly
    • Ai X., Parthun M.R. The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly. Mol. Cell 2004, 14:195-205.
    • (2004) Mol. Cell , vol.14 , pp. 195-205
    • Ai, X.1    Parthun, M.R.2
  • 20
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
    • Verreault A., Kaufman P.D., Kobayashi R., Stillman B. Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Curr. Biol. 1998, 8:96-108.
    • (1998) Curr. Biol. , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 24
    • 16844384065 scopus 로고    scopus 로고
    • Split decision: what happens to nucleosomes during DNA replication?
    • Annunziato A.T. Split decision: what happens to nucleosomes during DNA replication?. J. Biol. Chem. 2005, 280:12065-12068.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12065-12068
    • Annunziato, A.T.1
  • 25
    • 74549138158 scopus 로고    scopus 로고
    • Chaperoning histones during DNA replication and repair
    • Ransom M., Dennehey B.K., Tyler J.K. Chaperoning histones during DNA replication and repair. Cell 2010, 140:183-195.
    • (2010) Cell , vol.140 , pp. 183-195
    • Ransom, M.1    Dennehey, B.K.2    Tyler, J.K.3
  • 26
    • 77950462427 scopus 로고    scopus 로고
    • Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly
    • Xu M., Long C., Chen X., Huang C., Chen S., Zhu B. Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly. Science 2010, 328:94-98.
    • (2010) Science , vol.328 , pp. 94-98
    • Xu, M.1    Long, C.2    Chen, X.3    Huang, C.4    Chen, S.5    Zhu, B.6
  • 27
    • 79951992242 scopus 로고    scopus 로고
    • Splitting of H3-H4 tetramers at transcriptionally active genes undergoing dynamic histone exchange
    • Katan-Khaykovich Y., Struhl K. Splitting of H3-H4 tetramers at transcriptionally active genes undergoing dynamic histone exchange. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:1296-1301.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 1296-1301
    • Katan-Khaykovich, Y.1    Struhl, K.2
  • 28
    • 37549049820 scopus 로고    scopus 로고
    • Regulation of replication fork progression through histone supply and demand
    • Groth A., Corpet A., Cook A.J., Roche D., Bartek J., Lukas J., Almouzni G. Regulation of replication fork progression through histone supply and demand. Science 2007, 318:1928-1931.
    • (2007) Science , vol.318 , pp. 1928-1931
    • Groth, A.1    Corpet, A.2    Cook, A.J.3    Roche, D.4    Bartek, J.5    Lukas, J.6    Almouzni, G.7
  • 29
    • 0024372060 scopus 로고
    • Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro
    • Smith S., Stillman B. Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro. Cell 1989, 58:15-25.
    • (1989) Cell , vol.58 , pp. 15-25
    • Smith, S.1    Stillman, B.2
  • 30
    • 0029011919 scopus 로고
    • The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication
    • Kaufman P.D., Kobayashi R., Kessler N., Stillman B. The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication. Cell 1995, 81:1105-1114.
    • (1995) Cell , vol.81 , pp. 1105-1114
    • Kaufman, P.D.1    Kobayashi, R.2    Kessler, N.3    Stillman, B.4
  • 31
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault A., Kaufman P.D., Kobayashi R., Stillman B. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 1996, 87:95-104.
    • (1996) Cell , vol.87 , pp. 95-104
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 32
    • 0033582544 scopus 로고    scopus 로고
    • Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin
    • Shibahara K., Stillman B. Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin. Cell 1999, 96:575-585.
    • (1999) Cell , vol.96 , pp. 575-585
    • Shibahara, K.1    Stillman, B.2
  • 34
    • 0029161152 scopus 로고
    • Chromatin assembly factor 1 (CAF-1) colocalizes with replication foci in HeLa cell nuclei
    • Krude T. Chromatin assembly factor 1 (CAF-1) colocalizes with replication foci in HeLa cell nuclei. Exp. Cell Res. 1995, 220:304-311.
    • (1995) Exp. Cell Res. , vol.220 , pp. 304-311
    • Krude, T.1
  • 35
    • 0032511093 scopus 로고    scopus 로고
    • Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle
    • Marheineke K., Krude T. Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle. J. Biol. Chem. 1998, 273:15279-15286.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15279-15286
    • Marheineke, K.1    Krude, T.2
  • 36
    • 33747792063 scopus 로고    scopus 로고
    • The replication kinase Cdc7-Dbf4 promotes the interaction of the p150 subunit of chromatin assembly factor 1 with proliferating cell nuclear antigen
    • Gerard A., Koundrioukoff S., Ramillon V., Sergere J.C., Mailand N., Quivy J.P., Almouzni G. The replication kinase Cdc7-Dbf4 promotes the interaction of the p150 subunit of chromatin assembly factor 1 with proliferating cell nuclear antigen. EMBO Rep. 2006, 7:817-823.
    • (2006) EMBO Rep. , vol.7 , pp. 817-823
    • Gerard, A.1    Koundrioukoff, S.2    Ramillon, V.3    Sergere, J.C.4    Mailand, N.5    Quivy, J.P.6    Almouzni, G.7
  • 37
    • 1642312883 scopus 로고    scopus 로고
    • Silencing of chromatin assembly factor 1 in human cells leads to cell death and loss of chromatin assembly during DNA synthesis
    • Nabatiyan A., Krude T. Silencing of chromatin assembly factor 1 in human cells leads to cell death and loss of chromatin assembly during DNA synthesis. Mol. Cell. Biol. 2004, 24:2853-2862.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2853-2862
    • Nabatiyan, A.1    Krude, T.2
  • 38
    • 0142091385 scopus 로고    scopus 로고
    • Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication in vivo
    • Hoek M., Stillman B. Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication in vivo. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:12183-12188.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12183-12188
    • Hoek, M.1    Stillman, B.2
  • 39
    • 0037291295 scopus 로고    scopus 로고
    • Defective S phase chromatin assembly causes DNA damage, activation of the S phase checkpoint, and S phase arrest
    • Ye X., Franco A.A., Santos H., Nelson D.M., Kaufman P.D., Adams P.D. Defective S phase chromatin assembly causes DNA damage, activation of the S phase checkpoint, and S phase arrest. Mol. Cell 2003, 11:341-351.
    • (2003) Mol. Cell , vol.11 , pp. 341-351
    • Ye, X.1    Franco, A.A.2    Santos, H.3    Nelson, D.M.4    Kaufman, P.D.5    Adams, P.D.6
  • 40
    • 33744963245 scopus 로고    scopus 로고
    • Asf1 is required for viability and chromatin assembly during DNA replication in vertebrate cells
    • Sanematsu F., Takami Y., Barman H.K., Fukagawa T., Ono T., Shibahara K., Nakayama T. Asf1 is required for viability and chromatin assembly during DNA replication in vertebrate cells. J. Biol. Chem. 2006, 281:13817-13827.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13817-13827
    • Sanematsu, F.1    Takami, Y.2    Barman, H.K.3    Fukagawa, T.4    Ono, T.5    Shibahara, K.6    Nakayama, T.7
  • 41
    • 44349161775 scopus 로고    scopus 로고
    • In vivo study of the nucleosome assembly functions of ASF1 histone chaperones in human cells
    • Galvani A., Courbeyrette R., Agez M., Ochsenbein F., Mann C., Thuret J.Y. In vivo study of the nucleosome assembly functions of ASF1 histone chaperones in human cells. Mol. Cell. Biol. 2008, 28:3672-3685.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3672-3685
    • Galvani, A.1    Courbeyrette, R.2    Agez, M.3    Ochsenbein, F.4    Mann, C.5    Thuret, J.Y.6
  • 43
    • 0026181844 scopus 로고
    • DNA repair and the role of chromatin structure
    • Smerdon M.J. DNA repair and the role of chromatin structure. Curr. Opin. Cell Biol. 1991, 3:422-428.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 422-428
    • Smerdon, M.J.1
  • 45
    • 0141530885 scopus 로고    scopus 로고
    • Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo
    • Green C.M., Almouzni G. Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo. EMBO J. 2003, 22:5163-5174.
    • (2003) EMBO J. , vol.22 , pp. 5163-5174
    • Green, C.M.1    Almouzni, G.2
  • 46
    • 33750449326 scopus 로고    scopus 로고
    • New histone incorporation marks sites of UV repair in human cells
    • Polo S.E., Roche D., Almouzni G. New histone incorporation marks sites of UV repair in human cells. Cell 2006, 127:481-493.
    • (2006) Cell , vol.127 , pp. 481-493
    • Polo, S.E.1    Roche, D.2    Almouzni, G.3
  • 47
    • 33644543749 scopus 로고    scopus 로고
    • Induction of CAF-1 expression in response to DNA strand breaks in quiescent human cells
    • Nabatiyan A., Szuts D., Krude T. Induction of CAF-1 expression in response to DNA strand breaks in quiescent human cells. Mol. Cell. Biol. 2006, 26:1839-1849.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1839-1849
    • Nabatiyan, A.1    Szuts, D.2    Krude, T.3
  • 48
    • 79953197897 scopus 로고    scopus 로고
    • An analysis of CAF-1-interacting proteins reveals dynamic and direct interactions with the KU complex and 14-3-3 proteins
    • Hoek M., Myers M.P., Stillman B. An analysis of CAF-1-interacting proteins reveals dynamic and direct interactions with the KU complex and 14-3-3 proteins. J. Biol. Chem. 2011, 286:10876-10887.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10876-10887
    • Hoek, M.1    Myers, M.P.2    Stillman, B.3
  • 49
    • 79952580115 scopus 로고    scopus 로고
    • CAF-I-dependent control of degradation of the discontinuous strands during mismatch repair
    • Kadyrova L.Y., Blanko E.R., Kadyrov F.A. CAF-I-dependent control of degradation of the discontinuous strands during mismatch repair. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:2753-2758.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2753-2758
    • Kadyrova, L.Y.1    Blanko, E.R.2    Kadyrov, F.A.3
  • 50
    • 0020358561 scopus 로고
    • Patterns of histone variant synthesis can distinguish G0 from G1 cells
    • Wu R.S., Tsai S., Bonner W.M. Patterns of histone variant synthesis can distinguish G0 from G1 cells. Cell 1982, 31:367-374.
    • (1982) Cell , vol.31 , pp. 367-374
    • Wu, R.S.1    Tsai, S.2    Bonner, W.M.3
  • 51
    • 0022196769 scopus 로고
    • Changes in the levels of three different classes of histone mRNA during murine erythroleukemia cell differentiation
    • Brown D.T., Wellman S.E., Sittman D.B. Changes in the levels of three different classes of histone mRNA during murine erythroleukemia cell differentiation. Mol. Cell. Biol. 1985, 5:2879-2886.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2879-2886
    • Brown, D.T.1    Wellman, S.E.2    Sittman, D.B.3
  • 52
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly
    • Ahmad K., Henikoff S. The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol. Cell 2002, 9:1191-1200.
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 53
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profiling of histone H3.3 replacement patterns
    • Mito Y., Henikoff J.G., Henikoff S. Genome-scale profiling of histone H3.3 replacement patterns. Nat. Genet. 2005, 37:1090-1097.
    • (2005) Nat. Genet. , vol.37 , pp. 1090-1097
    • Mito, Y.1    Henikoff, J.G.2    Henikoff, S.3
  • 55
    • 17044394787 scopus 로고    scopus 로고
    • Transcriptional activation triggers deposition and removal of the histone variant H3.3
    • Schwartz B.E., Ahmad K. Transcriptional activation triggers deposition and removal of the histone variant H3.3. Genes Dev. 2005, 19:804-814.
    • (2005) Genes Dev. , vol.19 , pp. 804-814
    • Schwartz, B.E.1    Ahmad, K.2
  • 57
    • 66449111160 scopus 로고    scopus 로고
    • Inducible deposition of the histone variant H3.3 in interferon-stimulated genes
    • Tamura T., Smith M., Kanno T., Dasenbrock H., Nishiyama A., Ozato K. Inducible deposition of the histone variant H3.3 in interferon-stimulated genes. J. Biol. Chem. 2009, 284:12217-12225.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12217-12225
    • Tamura, T.1    Smith, M.2    Kanno, T.3    Dasenbrock, H.4    Nishiyama, A.5    Ozato, K.6
  • 58
    • 31444437043 scopus 로고    scopus 로고
    • Distribution of histone H3.3 in hematopoietic cell lineages
    • Jin C., Felsenfeld G. Distribution of histone H3.3 in hematopoietic cell lineages. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:574-579.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 574-579
    • Jin, C.1    Felsenfeld, G.2
  • 60
    • 27644515513 scopus 로고    scopus 로고
    • The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus
    • Loppin B., Bonnefoy E., Anselme C., Laurencon A., Karr T.L., Couble P. The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus. Nature 2005, 437:1386-1390.
    • (2005) Nature , vol.437 , pp. 1386-1390
    • Loppin, B.1    Bonnefoy, E.2    Anselme, C.3    Laurencon, A.4    Karr, T.L.5    Couble, P.6
  • 61
    • 33744923452 scopus 로고    scopus 로고
    • Dynamic distribution of the replacement histone variant H3.3 in the mouse oocyte and preimplantation embryos
    • Torres-Padilla M.E., Bannister A.J., Hurd P.J., Kouzarides T., Zernicka-Goetz M. Dynamic distribution of the replacement histone variant H3.3 in the mouse oocyte and preimplantation embryos. Int. J. Dev. Biol. 2006, 50:455-461.
    • (2006) Int. J. Dev. Biol. , vol.50 , pp. 455-461
    • Torres-Padilla, M.E.1    Bannister, A.J.2    Hurd, P.J.3    Kouzarides, T.4    Zernicka-Goetz, M.5
  • 63
    • 77953955724 scopus 로고    scopus 로고
    • The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3
    • Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 2010, 24:1253-1265.
    • (2010) Genes Dev. , vol.24 , pp. 1253-1265
    • Drane, P.1    Ouararhni, K.2    Depaux, A.3    Shuaib, M.4    Hamiche, A.5
  • 66
    • 34250745886 scopus 로고    scopus 로고
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z
    • Jin C., Felsenfeld G. Nucleosome stability mediated by histone variants H3.3 and H2A.Z. Genes Dev. 2007, 21:1519-1529.
    • (2007) Genes Dev. , vol.21 , pp. 1519-1529
    • Jin, C.1    Felsenfeld, G.2
  • 69
    • 60649119364 scopus 로고    scopus 로고
    • HPC2 and ubinuclein define a novel family of histone chaperones conserved throughout eukaryotes
    • Balaji S., Iyer L.M., Aravind L. HPC2 and ubinuclein define a novel family of histone chaperones conserved throughout eukaryotes. Mol. Biosyst. 2009, 5:269-275.
    • (2009) Mol. Biosyst. , vol.5 , pp. 269-275
    • Balaji, S.1    Iyer, L.M.2    Aravind, L.3
  • 70
    • 35948990898 scopus 로고    scopus 로고
    • The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization
    • Bonnefoy E., Orsi G.A., Couble P., Loppin B. The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization. PLoS Genet. 2007, 3:1991-2006.
    • (2007) PLoS Genet. , vol.3 , pp. 1991-2006
    • Bonnefoy, E.1    Orsi, G.A.2    Couble, P.3    Loppin, B.4
  • 73
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang X., Khosravi-Far R., Chang H.Y., Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 1997, 89:1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 75
    • 4444317361 scopus 로고    scopus 로고
    • Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX
    • Ishov A.M., Vladimirova O.V., Maul G.G. Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J. Cell Sci. 2004, 117:3807-3820.
    • (2004) J. Cell Sci. , vol.117 , pp. 3807-3820
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 76
    • 77956282773 scopus 로고    scopus 로고
    • Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
    • Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D. Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:14075-14080.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14075-14080
    • Lewis, P.W.1    Elsaesser, S.J.2    Noh, K.M.3    Stadler, S.C.4    Allis, C.D.5
  • 77
    • 33947274529 scopus 로고    scopus 로고
    • Propagation of centromeric chromatin requires exit from mitosis
    • Jansen L.E., Black B.E., Foltz D.R., Cleveland D.W. Propagation of centromeric chromatin requires exit from mitosis. J. Cell Biol. 2007, 176:795-805.
    • (2007) J. Cell Biol. , vol.176 , pp. 795-805
    • Jansen, L.E.1    Black, B.E.2    Foltz, D.R.3    Cleveland, D.W.4
  • 79
    • 0034722340 scopus 로고    scopus 로고
    • Chromatin assembly at kinetochores is uncoupled from DNA replication
    • Shelby R.D., Monier K., Sullivan K.F. Chromatin assembly at kinetochores is uncoupled from DNA replication. J. Cell Biol. 2000, 151:1113-1118.
    • (2000) J. Cell Biol. , vol.151 , pp. 1113-1118
    • Shelby, R.D.1    Monier, K.2    Sullivan, K.F.3
  • 80
    • 34548267126 scopus 로고    scopus 로고
    • Tetrameric structure of centromeric nucleosomes in interphase Drosophila cells
    • Dalal Y., Wang H., Lindsay S., Henikoff S. Tetrameric structure of centromeric nucleosomes in interphase Drosophila cells. PLoS Biol. 2007, 5:e218.
    • (2007) PLoS Biol. , vol.5
    • Dalal, Y.1    Wang, H.2    Lindsay, S.3    Henikoff, S.4
  • 83
    • 33846199534 scopus 로고    scopus 로고
    • Centromere identity maintained by nucleosomes assembled with histone H3 containing the CENP-A targeting domain
    • Black B.E., Jansen L.E., Maddox P.S., Foltz D.R., Desai A.B., Shah J.V., Cleveland D.W. Centromere identity maintained by nucleosomes assembled with histone H3 containing the CENP-A targeting domain. Mol. Cell 2007, 25:309-322.
    • (2007) Mol. Cell , vol.25 , pp. 309-322
    • Black, B.E.1    Jansen, L.E.2    Maddox, P.S.3    Foltz, D.R.4    Desai, A.B.5    Shah, J.V.6    Cleveland, D.W.7
  • 84
    • 4544275776 scopus 로고    scopus 로고
    • Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres
    • Hayashi T., Fujita Y., Iwasaki O., Adachi Y., Takahashi K., Yanagida M. Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres. Cell 2004, 118:715-729.
    • (2004) Cell , vol.118 , pp. 715-729
    • Hayashi, T.1    Fujita, Y.2    Iwasaki, O.3    Adachi, Y.4    Takahashi, K.5    Yanagida, M.6
  • 85
  • 86
    • 65649124957 scopus 로고    scopus 로고
    • Active establishment of centromeric CENP-A chromatin by RSF complex
    • Perpelescu M., Nozaki N., Obuse C., Yang H., Yoda K. Active establishment of centromeric CENP-A chromatin by RSF complex. J. Cell Biol. 2009, 185:397-407.
    • (2009) J. Cell Biol. , vol.185 , pp. 397-407
    • Perpelescu, M.1    Nozaki, N.2    Obuse, C.3    Yang, H.4    Yoda, K.5
  • 89
    • 76549131870 scopus 로고    scopus 로고
    • HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres
    • Shuaib M., Ouararhni K., Dimitrov S., Hamiche A. HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:1349-1354.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1349-1354
    • Shuaib, M.1    Ouararhni, K.2    Dimitrov, S.3    Hamiche, A.4
  • 90
    • 67549104312 scopus 로고    scopus 로고
    • Common ancestry of the CENP-A chaperones Scm3 and HJURP
    • Sanchez-Pulido L., Pidoux A.L., Ponting C.P., Allshire R.C. Common ancestry of the CENP-A chaperones Scm3 and HJURP. Cell 2009, 137:1173-1174.
    • (2009) Cell , vol.137 , pp. 1173-1174
    • Sanchez-Pulido, L.1    Pidoux, A.L.2    Ponting, C.P.3    Allshire, R.C.4
  • 91
    • 33646589676 scopus 로고    scopus 로고
    • Chaperone-mediated assembly of centromeric chromatin in vitro
    • Furuyama T., Dalal Y., Henikoff S. Chaperone-mediated assembly of centromeric chromatin in vitro. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:6172-6177.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6172-6177
    • Furuyama, T.1    Dalal, Y.2    Henikoff, S.3
  • 95
    • 34250316190 scopus 로고    scopus 로고
    • Scm3 is essential to recruit the histone h3 variant cse4 to centromeres and to maintain a functional kinetochore
    • Camahort R., Li B., Florens L., Swanson S.K., Washburn M.P., Gerton J.L. Scm3 is essential to recruit the histone h3 variant cse4 to centromeres and to maintain a functional kinetochore. Mol. Cell 2007, 26:853-865.
    • (2007) Mol. Cell , vol.26 , pp. 853-865
    • Camahort, R.1    Li, B.2    Florens, L.3    Swanson, S.K.4    Washburn, M.P.5    Gerton, J.L.6
  • 96
    • 34250173486 scopus 로고    scopus 로고
    • Nonhistone Scm3 and histones CenH3-H4 assemble the core of centromere-specific nucleosomes
    • Mizuguchi G., Xiao H., Wisniewski J., Smith M.M., Wu C. Nonhistone Scm3 and histones CenH3-H4 assemble the core of centromere-specific nucleosomes. Cell 2007, 129:1153-1164.
    • (2007) Cell , vol.129 , pp. 1153-1164
    • Mizuguchi, G.1    Xiao, H.2    Wisniewski, J.3    Smith, M.M.4    Wu, C.5
  • 97
    • 34547112848 scopus 로고    scopus 로고
    • Scm3, an essential Saccharomyces cerevisiae centromere protein required for G2/M progression and Cse4 localization
    • Stoler S., Rogers K., Weitze S., Morey L., Fitzgerald-Hayes M., Baker R.E. Scm3, an essential Saccharomyces cerevisiae centromere protein required for G2/M progression and Cse4 localization. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:10571-10576.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 10571-10576
    • Stoler, S.1    Rogers, K.2    Weitze, S.3    Morey, L.4    Fitzgerald-Hayes, M.5    Baker, R.E.6
  • 99
    • 59649107021 scopus 로고    scopus 로고
    • Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin
    • Williams J.S., Hayashi T., Yanagida M., Russell P. Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin. Mol. Cell 2009, 33:287-298.
    • (2009) Mol. Cell , vol.33 , pp. 287-298
    • Williams, J.S.1    Hayashi, T.2    Yanagida, M.3    Russell, P.4
  • 101
    • 78149424194 scopus 로고    scopus 로고
    • An E3 ubiquitin ligase prevents ectopic localization of the centromeric histone H3 variant via the centromere targeting domain
    • Ranjitkar P., Press M.O., Yi X., Baker R., MacCoss M.J., Biggins S. An E3 ubiquitin ligase prevents ectopic localization of the centromeric histone H3 variant via the centromere targeting domain. Mol. Cell 2010, 40:455-464.
    • (2010) Mol. Cell , vol.40 , pp. 455-464
    • Ranjitkar, P.1    Press, M.O.2    Yi, X.3    Baker, R.4    MacCoss, M.J.5    Biggins, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.