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Volumn 41, Issue 5, 2011, Pages 502-514

Histone Chaperones: Modulators of Chromatin Marks

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DOUBLE STRANDED DNA; HISTONE; HISTONE H2A; HISTONE H2AX; HISTONE H2AZ; HISTONE H2B; HISTONE H3; HISTONE H3.3; HISTONE H4; UNCLASSIFIED DRUG;

EID: 79951969175     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2011.02.013     Document Type: Review
Times cited : (168)

References (129)
  • 1
    • 31544446038 scopus 로고    scopus 로고
    • Transcriptional activators are dispensable for transcription in the absence of Spt6-mediated chromatin reassembly of promoter regions
    • Adkins M.W., Tyler J.K. Transcriptional activators are dispensable for transcription in the absence of Spt6-mediated chromatin reassembly of promoter regions. Mol. Cell 2006, 21:405-416.
    • (2006) Mol. Cell , vol.21 , pp. 405-416
    • Adkins, M.W.1    Tyler, J.K.2
  • 2
    • 2942550662 scopus 로고    scopus 로고
    • Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PHO5 and PHO8 genes
    • Adkins M.W., Howar S.R., Tyler J.K. Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PHO5 and PHO8 genes. Mol. Cell 2004, 14:657-666.
    • (2004) Mol. Cell , vol.14 , pp. 657-666
    • Adkins, M.W.1    Howar, S.R.2    Tyler, J.K.3
  • 3
    • 33847398682 scopus 로고    scopus 로고
    • The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase
    • Adkins M.W., Carson J.J., English C.M., Ramey C.J., Tyler J.K. The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase. J. Biol. Chem. 2007, 282:1334-1340.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1334-1340
    • Adkins, M.W.1    Carson, J.J.2    English, C.M.3    Ramey, C.J.4    Tyler, J.K.5
  • 4
    • 33846574739 scopus 로고    scopus 로고
    • Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics
    • Antczak A.J., Tsubota T., Kaufman P.D., Berger J.M. Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics. BMC Struct. Biol. 2006, 6:26.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 26
    • Antczak, A.J.1    Tsubota, T.2    Kaufman, P.D.3    Berger, J.M.4
  • 8
  • 9
    • 76849084692 scopus 로고    scopus 로고
    • A role for Gcn5 in replication-coupled nucleosome assembly
    • Burgess R.J., Zhou H., Han J., Zhang Z. A role for Gcn5 in replication-coupled nucleosome assembly. Mol. Cell 2010, 37:469-480.
    • (2010) Mol. Cell , vol.37 , pp. 469-480
    • Burgess, R.J.1    Zhou, H.2    Han, J.3    Zhang, Z.4
  • 10
    • 77954490394 scopus 로고    scopus 로고
    • New chaps in the histone chaperone arena
    • Campos E.I., Reinberg D. New chaps in the histone chaperone arena. Genes Dev. 2010, 24:1334-1338.
    • (2010) Genes Dev. , vol.24 , pp. 1334-1338
    • Campos, E.I.1    Reinberg, D.2
  • 13
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen C.C., Carson J.J., Feser J., Tamburini B., Zabaronick S., Linger J., Tyler J.K. Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 2008, 134:231-243.
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 15
    • 58149522909 scopus 로고    scopus 로고
    • Making copies of chromatin: the challenge of nucleosomal organization and epigenetic information
    • Corpet A., Almouzni G. Making copies of chromatin: the challenge of nucleosomal organization and epigenetic information. Trends Cell Biol. 2009, 19:29-41.
    • (2009) Trends Cell Biol. , vol.19 , pp. 29-41
    • Corpet, A.1    Almouzni, G.2
  • 17
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C., Lucia M.S., Hansen K.C., Tyler J.K. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 2009, 459:113-117.
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 18
    • 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., Rando O.J. Dynamics of replication-independent histone turnover in budding yeast. Science 2007, 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
  • 19
    • 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
  • 20
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll R., Hudson A., Jackson S.P. Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 2007, 315:649-652.
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 21
    • 0018267877 scopus 로고
    • The histone core complex: an octamer assembled by two sets of protein-protein interactions
    • Eickbush T.H., Moudrianakis E.N. The histone core complex: an octamer assembled by two sets of protein-protein interactions. Biochemistry 1978, 17:4955-4964.
    • (1978) Biochemistry , vol.17 , pp. 4955-4964
    • Eickbush, T.H.1    Moudrianakis, E.N.2
  • 26
    • 46149091721 scopus 로고    scopus 로고
    • H2B ubiquitylation plays a role in nucleosome dynamics during transcription elongation
    • Fleming A.B., Kao C.F., Hillyer C., Pikaart M., Osley M.A. H2B ubiquitylation plays a role in nucleosome dynamics during transcription elongation. Mol. Cell 2008, 31:57-66.
    • (2008) Mol. Cell , vol.31 , pp. 57-66
    • Fleming, A.B.1    Kao, C.F.2    Hillyer, C.3    Pikaart, M.4    Osley, M.A.5
  • 27
    • 0036964090 scopus 로고    scopus 로고
    • Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure
    • Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y., Rhoades A.R., Kaufman P.D., Stillman D.J. Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure. Genetics 2002, 162:1557-1571.
    • (2002) Genetics , vol.162 , pp. 1557-1571
    • Formosa, T.1    Ruone, S.2    Adams, M.D.3    Olsen, A.E.4    Eriksson, P.5    Yu, Y.6    Rhoades, A.R.7    Kaufman, P.D.8    Stillman, D.J.9
  • 30
    • 8644251883 scopus 로고    scopus 로고
    • Yeast chromatin assembly complex 1 protein excludes nonacetylatable forms of histone H4 from chromatin and the nucleus
    • Glowczewski L., Waterborg J.H., Berman J.G. Yeast chromatin assembly complex 1 protein excludes nonacetylatable forms of histone H4 from chromatin and the nucleus. Mol. Cell. Biol. 2004, 24:10180-10192.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10180-10192
    • Glowczewski, L.1    Waterborg, J.H.2    Berman, J.G.3
  • 31
    • 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
  • 32
    • 29144531244 scopus 로고    scopus 로고
    • Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning
    • Guillemette B., Bataille A.R., Gevry N., Adam M., Blanchette M., Robert F., Gaudreau L. Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning. PLoS Biol. 2005, 3:e384.
    • (2005) PLoS Biol. , vol.3
    • Guillemette, B.1    Bataille, A.R.2    Gevry, N.3    Adam, M.4    Blanchette, M.5    Robert, F.6    Gaudreau, L.7
  • 33
    • 35348970835 scopus 로고    scopus 로고
    • Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity
    • Han J., Zhou H., Li Z., Xu R.M., Zhang Z. Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity. J. Biol. Chem. 2007, 282:28587-28596.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28587-28596
    • Han, J.1    Zhou, H.2    Li, Z.3    Xu, R.M.4    Zhang, Z.5
  • 34
    • 27144544622 scopus 로고    scopus 로고
    • Assembly of variant histones into chromatin
    • Henikoff S., Ahmad K. Assembly of variant histones into chromatin. Annu. Rev. Cell Dev. Biol. 2005, 21:133-153.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 133-153
    • Henikoff, S.1    Ahmad, K.2
  • 35
    • 41549112501 scopus 로고    scopus 로고
    • FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16
    • Heo K., Kim H., Choi S.H., Choi J., Kim K., Gu J., Lieber M.R., Yang A.S., An W. FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16. Mol. Cell 2008, 30:86-97.
    • (2008) Mol. Cell , vol.30 , pp. 86-97
    • Heo, K.1    Kim, H.2    Choi, S.H.3    Choi, J.4    Kim, K.5    Gu, J.6    Lieber, M.R.7    Yang, A.S.8    An, W.9
  • 36
    • 77951498531 scopus 로고    scopus 로고
    • High-resolution profiling of gammaH2AX around DNA double strand breaks in the Mamm. Genome
    • Iacovoni J.S., Caron P., Lassadi I., Nicolas E., Massip L., Trouche D., Legube G. High-resolution profiling of gammaH2AX around DNA double strand breaks in the Mamm. Genome. EMBO J. 2010, 29:1446-1457.
    • (2010) EMBO J. , vol.29 , pp. 1446-1457
    • Iacovoni, J.S.1    Caron, P.2    Lassadi, I.3    Nicolas, E.4    Massip, L.5    Trouche, D.6    Legube, G.7
  • 37
    • 78751498728 scopus 로고    scopus 로고
    • Control of chromatin structure by Spt6: different consequences in coding and regulatory regions
    • Ivanovska I., Jacques P.E., Rando O.J., Robert F., Winston F. Control of chromatin structure by Spt6: different consequences in coding and regulatory regions. Mol. Cell. Biol. 2010, 31:531-541.
    • (2010) Mol. Cell. Biol. , vol.31 , pp. 531-541
    • Ivanovska, I.1    Jacques, P.E.2    Rando, O.J.3    Robert, F.4    Winston, F.5
  • 38
    • 33846663256 scopus 로고    scopus 로고
    • Continuous histone H2B and transcription-dependent histone H3 exchange in yeast cells outside of replication
    • Jamai A., Imoberdorf R.M., Strubin M. Continuous histone H2B and transcription-dependent histone H3 exchange in yeast cells outside of replication. Mol. Cell 2007, 25:345-355.
    • (2007) Mol. Cell , vol.25 , pp. 345-355
    • Jamai, A.1    Imoberdorf, R.M.2    Strubin, M.3
  • 39
    • 68349148027 scopus 로고    scopus 로고
    • Histone chaperone spt16 promotes redeposition of the original h3-h4 histones evicted by elongating RNA polymerase
    • Jamai A., Puglisi A., Strubin M. Histone chaperone spt16 promotes redeposition of the original h3-h4 histones evicted by elongating RNA polymerase. Mol. Cell 2009, 35:377-383.
    • (2009) Mol. Cell , vol.35 , pp. 377-383
    • Jamai, A.1    Puglisi, A.2    Strubin, M.3
  • 40
    • 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
  • 41
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • Kaplan C.D., Laprade L., Winston F. Transcription elongation factors repress transcription initiation from cryptic sites. Science 2003, 301:1096-1099.
    • (2003) Science , vol.301 , pp. 1096-1099
    • Kaplan, C.D.1    Laprade, L.2    Winston, F.3
  • 43
    • 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. USA 2011, 108:1296-1301.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1296-1301
    • Katan-Khaykovich, Y.1    Struhl, K.2
  • 44
    • 59049094825 scopus 로고    scopus 로고
    • Chromatin assembly factors Asf1 and CAF-1 have overlapping roles in deactivating the DNA damage checkpoint when DNA repair is complete
    • Kim J.A., Haber J.E. Chromatin assembly factors Asf1 and CAF-1 have overlapping roles in deactivating the DNA damage checkpoint when DNA repair is complete. Proc. Natl. Acad. Sci. USA 2009, 106:1151-1156.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1151-1156
    • Kim, J.A.1    Haber, J.E.2
  • 45
    • 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., Studitsky V.M. Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription. Mol. Cell 2002, 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
  • 48
    • 33646129019 scopus 로고    scopus 로고
    • The histone chaperone Asf1 increases the rate of histone eviction at the yeast PHO5 and PHO8 promoters
    • Korber P., Barbaric S., Luckenbach T., Schmid A., Schermer U.J., Blaschke D., Horz W. The histone chaperone Asf1 increases the rate of histone eviction at the yeast PHO5 and PHO8 promoters. J. Biol. Chem. 2006, 281:5539-5545.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5539-5545
    • Korber, P.1    Barbaric, S.2    Luckenbach, T.3    Schmid, A.4    Schermer, U.J.5    Blaschke, D.6    Horz, W.7
  • 49
    • 44649130038 scopus 로고    scopus 로고
    • Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation
    • Kraus W.L. Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation. Curr. Opin. Cell Biol. 2008, 20:294-302.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 294-302
    • Kraus, W.L.1
  • 51
    • 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., 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
  • 52
    • 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. USA 2010, 107:14075-14080.
    • (2010) Proc. Natl. Acad. Sci. USA , 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
  • 53
    • 66149127693 scopus 로고    scopus 로고
    • The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes
    • Li S., Shogren-Knaak M.A. The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes. J. Biol. Chem. 2009, 284:9411-9417.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9411-9417
    • Li, S.1    Shogren-Knaak, M.A.2
  • 54
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li B., Carey M., Workman J.L. The role of chromatin during transcription. Cell 2007, 128:707-719.
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 55
    • 34249099730 scopus 로고    scopus 로고
    • Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin
    • Li B., Gogol M., Carey M., Lee D., Seidel C., Workman J.L. Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin. Science 2007, 316:1050-1054.
    • (2007) Science , vol.316 , pp. 1050-1054
    • Li, B.1    Gogol, M.2    Carey, M.3    Lee, D.4    Seidel, C.5    Workman, J.L.6
  • 56
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    • Li Q., Zhou H., Wurtele H., Davies B., Horazdovsky B., Verreault A., Zhang Z. Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 2008, 134:244-255.
    • (2008) Cell , vol.134 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5    Verreault, A.6    Zhang, Z.7
  • 58
    • 67649518325 scopus 로고    scopus 로고
    • Molecular and reverse genetic characterization of NUCLEOSOME ASSEMBLY PROTEIN1 (NAP1) genes unravels their function in transcription and nucleotide excision repair in Arabidopsis thaliana
    • Liu Z., Zhu Y., Gao J., Yu F., Dong A., Shen W.H. Molecular and reverse genetic characterization of NUCLEOSOME ASSEMBLY PROTEIN1 (NAP1) genes unravels their function in transcription and nucleotide excision repair in Arabidopsis thaliana. Plant J. 2009, 59:27-38.
    • (2009) Plant J. , vol.59 , pp. 27-38
    • Liu, Z.1    Zhu, Y.2    Gao, J.3    Yu, F.4    Dong, A.5    Shen, W.H.6
  • 59
    • 33749657892 scopus 로고    scopus 로고
    • PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state
    • Loyola A., Bonaldi T., Roche D., Imhof A., Almouzni G. PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state. Mol. Cell 2006, 24:309-316.
    • (2006) Mol. Cell , vol.24 , pp. 309-316
    • Loyola, A.1    Bonaldi, T.2    Roche, D.3    Imhof, A.4    Almouzni, G.5
  • 61
    • 46649121282 scopus 로고    scopus 로고
    • Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus
    • Malay A.D., Umehara T., Matsubara-Malay K., Padmanabhan B., Yokoyama S. Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus. J. Biol. Chem. 2008, 283:14022-14031.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14022-14031
    • Malay, A.D.1    Umehara, T.2    Matsubara-Malay, K.3    Padmanabhan, B.4    Yokoyama, S.5
  • 63
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto H., Hawke D., Kobayashi R., Verreault A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 2005, 436:294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 64
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi G., Shen X., Landry J., Wu W.H., Sen S., 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    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 68
    • 0033212963 scopus 로고    scopus 로고
    • Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins
    • Murzina N., Verreault A., Laue E., Stillman B. Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. Mol. Cell 1999, 4:529-540.
    • (1999) Mol. Cell , vol.4 , pp. 529-540
    • Murzina, N.1    Verreault, A.2    Laue, E.3    Stillman, B.4
  • 69
    • 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
  • 71
    • 0036205048 scopus 로고    scopus 로고
    • Genome-wide location and regulated recruitment of the RSC nucleosome-remodeling complex
    • Ng H.H., Robert F., Young R.A., Struhl K. Genome-wide location and regulated recruitment of the RSC nucleosome-remodeling complex. Genes Dev. 2002, 16:806-819.
    • (2002) Genes Dev. , vol.16 , pp. 806-819
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 72
    • 32044445075 scopus 로고    scopus 로고
    • Evidence that Spt2/Sin1, an HMG-like factor, plays roles in transcription elongation, chromatin structure, and genome stability in Saccharomyces cerevisiae
    • Nourani A., Robert F., Winston F. Evidence that Spt2/Sin1, an HMG-like factor, plays roles in transcription elongation, chromatin structure, and genome stability in Saccharomyces cerevisiae. Mol. Cell. Biol. 2006, 26:1496-1509.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1496-1509
    • Nourani, A.1    Robert, F.2    Winston, F.3
  • 73
    • 77957814604 scopus 로고    scopus 로고
    • Reduced histone biosynthesis and chromatin changes arising from a damage signal at telomeres
    • O'Sullivan R.J., Kubicek S., Schreiber S.L., Karlseder J. Reduced histone biosynthesis and chromatin changes arising from a damage signal at telomeres. Nat. Struct. Mol. Biol. 2010, 17:1218-1225.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1218-1225
    • O'Sullivan, R.J.1    Kubicek, S.2    Schreiber, S.L.3    Karlseder, J.4
  • 74
    • 77956500253 scopus 로고    scopus 로고
    • Epigenetic inheritance of an inducibly nucleosome-depleted promoter and its associated transcriptional state in the apparent absence of transcriptional activators
    • Ohsawa R., Adkins M., Tyler J.K. Epigenetic inheritance of an inducibly nucleosome-depleted promoter and its associated transcriptional state in the apparent absence of transcriptional activators. Epigenetics Chromatin 2009, 2:11.
    • (2009) Epigenetics Chromatin , vol.2 , pp. 11
    • Ohsawa, R.1    Adkins, M.2    Tyler, J.K.3
  • 75
    • 0032498273 scopus 로고    scopus 로고
    • FACT, a factor that facilitates transcript elongation through nucleosomes
    • Orphanides G., LeRoy G., Chang C.H., Luse D.S., Reinberg D. FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 1998, 92:105-116.
    • (1998) Cell , vol.92 , pp. 105-116
    • Orphanides, G.1    LeRoy, G.2    Chang, C.H.3    Luse, D.S.4    Reinberg, D.5
  • 76
    • 0033566129 scopus 로고    scopus 로고
    • The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins
    • Orphanides G., Wu W.H., Lane W.S., Hampsey M., Reinberg D. The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature 1999, 400:284-288.
    • (1999) Nature , vol.400 , pp. 284-288
    • Orphanides, G.1    Wu, W.H.2    Lane, W.S.3    Hampsey, M.4    Reinberg, D.5
  • 78
    • 33646691283 scopus 로고    scopus 로고
    • Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II
    • Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D. Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Cell 2006, 125:703-717.
    • (2006) Cell , vol.125 , pp. 703-717
    • Pavri, R.1    Zhu, B.2    Li, G.3    Trojer, P.4    Mandal, S.5    Shilatifard, A.6    Reinberg, D.7
  • 79
    • 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
  • 80
    • 27644559475 scopus 로고    scopus 로고
    • Identification and characterization of Elf1, a conserved transcription elongation factor in Saccharomyces cerevisiae
    • Prather D., Krogan N.J., Emili A., Greenblatt J.F., Winston F. Identification and characterization of Elf1, a conserved transcription elongation factor in Saccharomyces cerevisiae. Mol. Cell. Biol. 2005, 25:10122-10135.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10122-10135
    • Prather, D.1    Krogan, N.J.2    Emili, A.3    Greenblatt, J.F.4    Winston, F.5
  • 81
    • 27644470214 scopus 로고    scopus 로고
    • The HIR corepressor complex binds to nucleosomes generating a distinct protein/DNA complex resistant to remodeling by SWI/SNF
    • Prochasson P., Florens L., Swanson S.K., Washburn M.P., Workman J.L. The HIR corepressor complex binds to nucleosomes generating a distinct protein/DNA complex resistant to remodeling by SWI/SNF. Genes Dev. 2005, 19:2534-2539.
    • (2005) Genes Dev. , vol.19 , pp. 2534-2539
    • Prochasson, P.1    Florens, L.2    Swanson, S.K.3    Washburn, M.P.4    Workman, J.L.5
  • 83
    • 51349099238 scopus 로고    scopus 로고
    • The HP1-p150/CAF-1 interaction is required for pericentric heterochromatin replication and S-phase progression in mouse cells
    • Quivy J.P., Gerard A., Cook A.J., Roche D., Almouzni G. The HP1-p150/CAF-1 interaction is required for pericentric heterochromatin replication and S-phase progression in mouse cells. Nat. Struct. Mol. Biol. 2008, 15:972-979.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 972-979
    • Quivy, J.P.1    Gerard, A.2    Cook, A.J.3    Roche, D.4    Almouzni, G.5
  • 86
    • 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
  • 88
    • 1542328277 scopus 로고    scopus 로고
    • Anatomy of a hypersensitive site
    • Reinke H., Horz W. Anatomy of a hypersensitive site. Biochim. Biophys. Acta 2004, 1677:24-29.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 24-29
    • Reinke, H.1    Horz, W.2
  • 89
    • 44449104927 scopus 로고    scopus 로고
    • Clothing up DNA for all seasons: Histone chaperones and nucleosome assembly pathways
    • Rocha W., Verreault A. Clothing up DNA for all seasons: Histone chaperones and nucleosome assembly pathways. FEBS Lett. 2008, 582:1938-1949.
    • (2008) FEBS Lett. , vol.582 , pp. 1938-1949
    • Rocha, W.1    Verreault, A.2
  • 90
    • 0032861343 scopus 로고    scopus 로고
    • Megabase chromatin domains involved in DNA double-strand breaks in vivo
    • Rogakou E.P., Boon C., Redon C., Bonner W.M. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol. 1999, 146:905-916.
    • (1999) J. Cell Biol. , vol.146 , pp. 905-916
    • Rogakou, E.P.1    Boon, C.2    Redon, C.3    Bonner, W.M.4
  • 92
    • 77956673574 scopus 로고    scopus 로고
    • Epigenetic modifications in double-strand break DNA damage signaling and repair
    • Rossetto D., Truman A.W., Kron S.J., Cote J. Epigenetic modifications in double-strand break DNA damage signaling and repair. Clin. Cancer Res. 2010, 16:4543-4552.
    • (2010) Clin. Cancer Res. , vol.16 , pp. 4543-4552
    • Rossetto, D.1    Truman, A.W.2    Kron, S.J.3    Cote, J.4
  • 93
    • 34547277498 scopus 로고    scopus 로고
    • Genome-wide replication-independent histone H3 exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1
    • Rufiange A., Jacques P.E., Bhat W., Robert F., Nourani A. Genome-wide replication-independent histone H3 exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1. Mol. Cell 2007, 27:393-405.
    • (2007) Mol. Cell , vol.27 , pp. 393-405
    • Rufiange, A.1    Jacques, P.E.2    Bhat, W.3    Robert, F.4    Nourani, A.5
  • 94
    • 22544450837 scopus 로고    scopus 로고
    • Histones are incorporated in trans during reassembly of the yeast PHO5 promoter
    • Schermer U.J., Korber P., Horz W. Histones are incorporated in trans during reassembly of the yeast PHO5 promoter. Mol. Cell 2005, 19:279-285.
    • (2005) Mol. Cell , vol.19 , pp. 279-285
    • Schermer, U.J.1    Korber, P.2    Horz, W.3
  • 95
    • 33846023720 scopus 로고    scopus 로고
    • Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II
    • Schneider J., Bajwa P., Johnson F.C., Bhaumik S.R., Shilatifard A. Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II. J. Biol. Chem. 2006, 281:37270-37274.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37270-37274
    • Schneider, J.1    Bajwa, P.2    Johnson, F.C.3    Bhaumik, S.R.4    Shilatifard, A.5
  • 96
    • 33646141366 scopus 로고    scopus 로고
    • Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II
    • Schwabish M.A., Struhl K. Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II. Mol. Cell 2006, 22:415-422.
    • (2006) Mol. Cell , vol.22 , pp. 415-422
    • Schwabish, M.A.1    Struhl, K.2
  • 97
    • 34250309212 scopus 로고    scopus 로고
    • Vps75, a new yeast member of the NAP histone chaperone family
    • Selth L., Svejstrup J.Q. Vps75, a new yeast member of the NAP histone chaperone family. J. Biol. Chem. 2007, 282:12358-12362.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12358-12362
    • Selth, L.1    Svejstrup, J.Q.2
  • 99
    • 45849153073 scopus 로고    scopus 로고
    • The coactivators CBP/p300 and the histone chaperone NAP1 promote transcription-independent nucleosome eviction at the HTLV-1 promoter
    • Sharma N., Nyborg J.K. The coactivators CBP/p300 and the histone chaperone NAP1 promote transcription-independent nucleosome eviction at the HTLV-1 promoter. Proc. Natl. Acad. Sci. USA 2008, 105:7959-7963.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7959-7963
    • Sharma, N.1    Nyborg, J.K.2
  • 101
    • 5444225805 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: the short and long of it
    • Sims R.J., Belotserkovskaya R., Reinberg D. Elongation by RNA polymerase II: the short and long of it. Genes Dev. 2004, 18:2437-2468.
    • (2004) Genes Dev. , vol.18 , pp. 2437-2468
    • Sims, R.J.1    Belotserkovskaya, R.2    Reinberg, D.3
  • 102
    • 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
  • 104
    • 23844472662 scopus 로고    scopus 로고
    • Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription
    • Swaminathan V., Kishore A.H., Febitha K.K., Kundu T.K. Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription. Mol. Cell. Biol. 2005, 25:7534-7545.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7534-7545
    • Swaminathan, V.1    Kishore, A.H.2    Febitha, K.K.3    Kundu, T.K.4
  • 106
    • 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
  • 107
    • 65649153311 scopus 로고    scopus 로고
    • FACT and Asf1 regulate nucleosome dynamics and coactivator binding at the HO promoter
    • Takahata S., Yu Y., Stillman D.J. FACT and Asf1 regulate nucleosome dynamics and coactivator binding at the HO promoter. Mol. Cell 2009, 34:405-415.
    • (2009) Mol. Cell , vol.34 , pp. 405-415
    • Takahata, S.1    Yu, Y.2    Stillman, D.J.3
  • 108
    • 70350761680 scopus 로고    scopus 로고
    • The E2F functional analogue SBF recruits the Rpd3(L) HDAC, via Whi5 and Stb1, and the FACT chromatin reorganizer, to yeast G1 cyclin promoters
    • Takahata S., Yu Y., Stillman D.J. The E2F functional analogue SBF recruits the Rpd3(L) HDAC, via Whi5 and Stb1, and the FACT chromatin reorganizer, to yeast G1 cyclin promoters. EMBO J. 2009, 28:3378-3389.
    • (2009) EMBO J. , vol.28 , pp. 3378-3389
    • Takahata, S.1    Yu, Y.2    Stillman, D.J.3
  • 109
    • 33748357745 scopus 로고    scopus 로고
    • Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication
    • Tan B.C., Chien C.T., Hirose S., Lee S.C. Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication. EMBO J. 2006, 25:3975-3985.
    • (2006) EMBO J. , vol.25 , pp. 3975-3985
    • Tan, B.C.1    Chien, C.T.2    Hirose, S.3    Lee, S.C.4
  • 114
    • 34250831538 scopus 로고    scopus 로고
    • A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly
    • Walfridsson J., Khorosjutina O., Matikainen P., Gustafsson C.M., Ekwall K. A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly. EMBO J. 2007, 26:2868-2879.
    • (2007) EMBO J. , vol.26 , pp. 2868-2879
    • Walfridsson, J.1    Khorosjutina, O.2    Matikainen, P.3    Gustafsson, C.M.4    Ekwall, K.5
  • 117
    • 34047262671 scopus 로고    scopus 로고
    • Transcriptional regulation by chromatin disassembly and reassembly
    • Williams S.K., Tyler J.K. Transcriptional regulation by chromatin disassembly and reassembly. Curr. Opin. Genet. Dev. 2007, 17:88-93.
    • (2007) Curr. Opin. Genet. Dev. , vol.17 , pp. 88-93
    • Williams, S.K.1    Tyler, J.K.2
  • 118
    • 48249148195 scopus 로고    scopus 로고
    • Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation
    • Williams S.K., Truong D., Tyler J.K. Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc. Natl. Acad. Sci. USA 2008, 105:9000-9005.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9000-9005
    • Williams, S.K.1    Truong, D.2    Tyler, J.K.3
  • 120
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu F., Zhang K., Grunstein M. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 2005, 121:375-385.
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 121
    • 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
  • 122
    • 78650754693 scopus 로고    scopus 로고
    • Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci
    • Yamane K., Mizuguchi T., Cui B., Zofall M., Noma K., Grewal S.I. Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci. Mol. Cell 2011, 41:56-66.
    • (2011) Mol. Cell , vol.41 , pp. 56-66
    • Yamane, K.1    Mizuguchi, T.2    Cui, B.3    Zofall, M.4    Noma, K.5    Grewal, S.I.6
  • 123
    • 58049206591 scopus 로고    scopus 로고
    • The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation
    • Yoh S.M., Lucas J.S., Jones K.A. The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation. Genes Dev. 2008, 22:3422-3434.
    • (2008) Genes Dev. , vol.22 , pp. 3422-3434
    • Yoh, S.M.1    Lucas, J.S.2    Jones, K.A.3
  • 126
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan J., Pu M., Zhang Z., Lou Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 2009, 8:1747-1753.
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 127
    • 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., 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
  • 128
    • 38149098408 scopus 로고    scopus 로고
    • Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation
    • Zhou W., Zhu P., Wang J., Pascual G., Ohgi K.A., Lozach J., Glass C.K., Rosenfeld M.G. Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation. Mol. Cell 2008, 29:69-80.
    • (2008) Mol. Cell , vol.29 , pp. 69-80
    • Zhou, W.1    Zhu, P.2    Wang, J.3    Pascual, G.4    Ohgi, K.A.5    Lozach, J.6    Glass, C.K.7    Rosenfeld, M.G.8
  • 129
    • 58149159543 scopus 로고    scopus 로고
    • Chromatin restoration following nucleotide excision repair involves the incorporation of ubiquitinated H2A at damaged genomic sites
    • Zhu Q., Wani G., Arab H.H., El-Mahdy M.A., Ray A., Wani A.A. Chromatin restoration following nucleotide excision repair involves the incorporation of ubiquitinated H2A at damaged genomic sites. DNA Repair (Amst.) 2009, 8:262-273.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 262-273
    • Zhu, Q.1    Wani, G.2    Arab, H.H.3    El-Mahdy, M.A.4    Ray, A.5    Wani, A.A.6


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