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Volumn 30, Issue 5, 2010, Pages 1116-1129

Asf1 can promote trimethylation of H3 K36 by Set2

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; FUNGAL PROTEIN; HISTONE H3; HISTONE H4; PROTEIN ASF1; PROTEIN SET2; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 76749150088     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01229-09     Document Type: Article
Times cited : (28)

References (59)
  • 1
    • 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., J. J. Carson, C. M. English, C. J. Ramey, and J. K. Tyler. 2007. The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase. J. Biol. Chem. 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
  • 2
    • 10644222646 scopus 로고    scopus 로고
    • The histone chaperone Asf1p mediates global chromatin disassembly in vivo
    • Adkins, M. W., and J. K. Tyler. 2004. The histone chaperone Asf1p mediates global chromatin disassembly in vivo. J. Biol. Chem. 279:52069-52074.
    • (2004) J. Biol. Chem , vol.279 , pp. 52069-52074
    • Adkins, M.W.1    Tyler, J.K.2
  • 3
    • 40549107989 scopus 로고    scopus 로고
    • Aparicio, O., J. V. Geisberg, and K. Struhl. 2004. Chromatin immunoprecipitation for determining the association of proteins with specific genomic sequences in vivo. In J. S. Bonifacino, M. Dasso, J. B. Harford, J. Lippincott-Schwartz, and K. M. Yamada (ed.), Current protocols in cell biology, chapter 17, unit 17.7. John Wiley and Sons, New York, NY.
    • Aparicio, O., J. V. Geisberg, and K. Struhl. 2004. Chromatin immunoprecipitation for determining the association of proteins with specific genomic sequences in vivo. In J. S. Bonifacino, M. Dasso, J. B. Harford, J. Lippincott-Schwartz, and K. M. Yamada (ed.), Current protocols in cell biology, chapter 17, unit 17.7. John Wiley and Sons, New York, NY.
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., A. Davies, G. J. Cost, E. Caputo, J. Li, P. Hieter, and J. D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14:115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 7
    • 56849114880 scopus 로고    scopus 로고
    • Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genome
    • Cheung, V., G. Chua, N. N. Batada, C. R. Landry, S. W. Michnick, T. R. Hughes, and F. Winston. 2008. Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genome. PLoS Biol. 6:e277.
    • (2008) PLoS Biol , vol.6
    • Cheung, V.1    Chua, G.2    Batada, N.N.3    Landry, C.R.4    Michnick, S.W.5    Hughes, T.R.6    Winston, F.7
  • 8
    • 36248965214 scopus 로고    scopus 로고
    • Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes
    • Chu, Y., R. Simic, M. H. Warner, K. M. Arndt, and G. Prelich. 2007. Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes. EMBO J. 26:4646-4656.
    • (2007) EMBO J , vol.26 , pp. 4646-4656
    • Chu, Y.1    Simic, R.2    Warner, M.H.3    Arndt, K.M.4    Prelich, G.5
  • 9
    • 34147217542 scopus 로고    scopus 로고
    • Collins, S. R., K. M. Miller, N. L. Maas, A. Roguev, J. Fillingham, C. S. Chu, M. Schuldiner, M. Gebbia, J. Recht, M. Shales, H. Ding, H. Xu, J. Han, K. Ingvarsdottir, B. Cheng, B. Andrews, C. Boone, S. L. Berger, P. Hieter, Z. Zhang, G. W. Brown, C. J. Ingles, A. Emili, C. D. Allis, D. P. Toczyski, J. S. Weissman, J. F. Greenblatt, and N. J. Krogan. 2007. Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446:806-810.
    • Collins, S. R., K. M. Miller, N. L. Maas, A. Roguev, J. Fillingham, C. S. Chu, M. Schuldiner, M. Gebbia, J. Recht, M. Shales, H. Ding, H. Xu, J. Han, K. Ingvarsdottir, B. Cheng, B. Andrews, C. Boone, S. L. Berger, P. Hieter, Z. Zhang, G. W. Brown, C. J. Ingles, A. Emili, C. D. Allis, D. P. Toczyski, J. S. Weissman, J. F. Greenblatt, and N. J. Krogan. 2007. Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446:806-810.
  • 10
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll, R., A. Hudson, and S. P. Jackson. 2007. Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315:649-652.
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 11
    • 54349105157 scopus 로고    scopus 로고
    • Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4
    • Du, H. N., I. M. Fingerman, and S. D. Briggs. 2008. Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4. Genes Dev. 22:2786-2798.
    • (2008) Genes Dev , vol.22 , pp. 2786-2798
    • Du, H.N.1    Fingerman, I.M.2    Briggs, S.D.3
  • 12
    • 0035101733 scopus 로고    scopus 로고
    • Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1
    • Emili, A., D. M. Schieltz, J. R. Yates III, and L. H. Hartwell. 2001. Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1. Mol. Cell 7:13-20.
    • (2001) Mol. Cell , vol.7 , pp. 13-20
    • Emili, A.1    Schieltz, D.M.2    Yates III, J.R.3    Hartwell, L.H.4
  • 13
    • 33750477650 scopus 로고    scopus 로고
    • Structural basis for the histone chaperone activity of Asf1
    • English, C. M., M. W. Adkins, J. J. Carson, M. E. Churchill, and J. K. Tyler. 2006. Structural basis for the histone chaperone activity of Asf1. Cell 127: 495-508.
    • (2006) Cell , vol.127 , pp. 495-508
    • English, C.M.1    Adkins, M.W.2    Carson, J.J.3    Churchill, M.E.4    Tyler, J.K.5
  • 14
    • 67651183861 scopus 로고    scopus 로고
    • A glycolytic burst drives glucose induction of global histone acetylation by picNuA4 and SAGA
    • Friis, R. M. N., B. P. Wu, S. N. Reinke, D. J. Hockman, B. D. Sykes, and M. C. Schultz. 2009. A glycolytic burst drives glucose induction of global histone acetylation by picNuA4 and SAGA. Nucleic Acids Res. 37:3969-3980.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3969-3980
    • Friis, R.M.N.1    Wu, B.P.2    Reinke, S.N.3    Hockman, D.J.4    Sykes, B.D.5    Schultz, M.C.6
  • 15
  • 18
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • Goldstein, A. L., and J. H. McCusker. 1999. Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 15:1541-1553.
    • (1999) Yeast , vol.15 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 20
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han, J., H. Zhou, B. Horazdovsky, K. Zhang, R. M. Xu, and Z. Zhang. 2007. Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315:653-655.
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1    Zhou, H.2    Horazdovsky, B.3    Zhang, K.4    Xu, R.M.5    Zhang, Z.6
  • 21
    • 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., H. Zhou, Z. Li, R. M. Xu, and Z. Zhang. 2007. Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity. J. Biol. Chem. 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
  • 22
    • 0035336971 scopus 로고    scopus 로고
    • Asf1 links Rad53 to control of chromatin assembly
    • Hu, F., A. A. Alcasabas, and S. J. Elledge. 2001. Asf1 links Rad53 to control of chromatin assembly. Genes Dev. 15:1061-1066.
    • (2001) Genes Dev , vol.15 , pp. 1061-1066
    • Hu, F.1    Alcasabas, A.A.2    Elledge, S.J.3
  • 23
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • Kaplan, C. D., L. Laprade, and F. Winston. 2003. Transcription elongation factors repress transcription initiation from cryptic sites. Science 301:1096-1099.
    • (2003) Science , vol.301 , pp. 1096-1099
    • Kaplan, C.D.1    Laprade, L.2    Winston, F.3
  • 25
    • 64249111489 scopus 로고    scopus 로고
    • Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5′ transcribed regions
    • Kim, T., and S. Buratowski. 2009. Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5′ transcribed regions. Cell 137:259-272.
    • (2009) Cell , vol.137 , pp. 259-272
    • Kim, T.1    Buratowski, S.2
  • 26
    • 16244384503 scopus 로고    scopus 로고
    • A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation
    • Kizer, K. O., H. P. Phatnani, Y. Shibata, H. Hall, A. L. Greenleaf, and B. D. Strahl. 2005. A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol. Cell. Biol. 25:3305-3316.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 3305-3316
    • Kizer, K.O.1    Phatnani, H.P.2    Shibata, Y.3    Hall, H.4    Greenleaf, A.L.5    Strahl, B.D.6
  • 29
    • 0030862060 scopus 로고    scopus 로고
    • Two new S-phase-specific genes from Saccharomyces cerevisiae
    • Le, S., C. Davis, J. B. Konopka, and R. Sternglanz. 1997. Two new S-phase-specific genes from Saccharomyces cerevisiae. Yeast 13:1029-1042.
    • (1997) Yeast , vol.13 , pp. 1029-1042
    • Le, S.1    Davis, C.2    Konopka, J.B.3    Sternglanz, R.4
  • 30
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • Lee, K. K., and J. L. Workman. 2007. Histone acetyltransferase complexes: one size doesn't fit all. Nat. Rev. Mol. Cell Biol. 8:284-295.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 31
    • 34249099730 scopus 로고    scopus 로고
    • Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin
    • Li, B., M. Gogol, M. Carey, D. Lee, C. Seidel, and J. L. Workman. 2007. Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin. Science 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
  • 32
    • 65549095078 scopus 로고    scopus 로고
    • Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription
    • Li, B., J. Jackson, M. D. Simon, B. Fleharty, M. Gogol, C. Seidel, J. L. Workman, and A. Shilatifard. 2009. Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription. J. Biol. Chem. 284:7970-7976.
    • (2009) J. Biol. Chem , vol.284 , pp. 7970-7976
    • Li, B.1    Jackson, J.2    Simon, M.D.3    Fleharty, B.4    Gogol, M.5    Seidel, C.6    Workman, J.L.7    Shilatifard, A.8
  • 33
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., A. McKenzie III, D. J. Demarini, N. G. Shah, A. Wach, A. Brachat, P. Philippsen, and J. R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 35
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • Natsume, R., M. Eitoku, Y. Akai, N. Sano, M. Horikoshi, and T. Senda. 2007. Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4. Nature 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
  • 36
    • 33748163064 scopus 로고    scopus 로고
    • Proline isomerization of histone H3 regulates lysine methylation and gene expression
    • Nelson, C. J., H. Santos-Rosa, and T. Kouzarides. 2006. Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 126:905-916.
    • (2006) Cell , vol.126 , pp. 905-916
    • Nelson, C.J.1    Santos-Rosa, H.2    Kouzarides, T.3
  • 38
    • 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., L. Florens, S. K. Swanson, M. P. Washburn, and J. L. Workman. 2005. The HIR corepressor complex binds to nucleosomes generating a distinct protein/DNA complex resistant to remodeling by SWI/ SNF. Genes Dev. 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
  • 40
    • 1342269199 scopus 로고    scopus 로고
    • Large-scale screening of yeast mutants for sensitivity to the IMP dehydrogenase inhibitor 6-azauracil
    • Riles, L., R. J. Shaw, M. Johnston, and D. Reines. 2004. Large-scale screening of yeast mutants for sensitivity to the IMP dehydrogenase inhibitor 6-azauracil. Yeast 21:241-248.
    • (2004) Yeast , vol.21 , pp. 241-248
    • Riles, L.1    Shaw, R.J.2    Johnston, M.3    Reines, D.4
  • 41
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • Rusche, L. N., A. L. Kirchmaier, and J. Rine. 2003. The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae. Annu. Rev. Biochem. 72:481-516.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 42
    • 33646141366 scopus 로고    scopus 로고
    • Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II
    • Schwabish, M. A., and K. Struhl. 2006. Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II. Mol. Cell 22:415-422.
    • (2006) Mol. Cell , vol.22 , pp. 415-422
    • Schwabish, M.A.1    Struhl, K.2
  • 43
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • Shahbazian, M. D., and M. Grunstein. 2007. Functions of site-specific histone acetylation and deacetylation. Annu. Rev. Biochem. 76:75-100.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 44
    • 0035799281 scopus 로고    scopus 로고
    • Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing
    • Sharp, J. A., E. T. Fouts, D. C. Krawitz, and P. D. Kaufman. 2001. Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing. Curr. Biol. 11:463-473.
    • (2001) Curr. Biol , vol.11 , pp. 463-473
    • Sharp, J.A.1    Fouts, E.T.2    Krawitz, D.C.3    Kaufman, P.D.4
  • 45
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 46
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D., and C. D. Allis. 2000. The language of covalent histone modifications. Nature 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 48
    • 0034977802 scopus 로고    scopus 로고
    • Yeast ASF1 protein is required for cell cycle regulation of histone gene transcription
    • Sutton, A., J. Bucaria, M. A. Osley, and R. Sternglanz. 2001. Yeast ASF1 protein is required for cell cycle regulation of histone gene transcription. Genetics 158:587-596.
    • (2001) Genetics , vol.158 , pp. 587-596
    • Sutton, A.1    Bucaria, J.2    Osley, M.A.3    Sternglanz, R.4
  • 49
    • 0037930802 scopus 로고    scopus 로고
    • Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex
    • Sutton, A., W. J. Shia, D. Band, P. D. Kaufman, S. Osada, J. L. Workman, and R. Sternglanz. 2003. Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex. J. Biol. Chem. 278:16887-16892.
    • (2003) J. Biol. Chem , vol.278 , pp. 16887-16892
    • Sutton, A.1    Shia, W.J.2    Band, D.3    Kaufman, P.D.4    Osada, S.5    Workman, J.L.6    Sternglanz, R.7
  • 50
    • 33745418946 scopus 로고    scopus 로고
    • Dominant mutants of the Saccharomyces cerevisiae ASF1 histone chaperone bypass the need for CAF-1 in transcriptional silencing by altering histone and Sir protein recruitment
    • Tamburini, B. A., J. J. Carson, J. G. Linger, and J. K. Tyler. 2006. Dominant mutants of the Saccharomyces cerevisiae ASF1 histone chaperone bypass the need for CAF-1 in transcriptional silencing by altering histone and Sir protein recruitment. Genetics 173:599-610.
    • (2006) Genetics , vol.173 , pp. 599-610
    • Tamburini, B.A.1    Carson, J.J.2    Linger, J.G.3    Tyler, J.K.4
  • 51
    • 34247842881 scopus 로고    scopus 로고
    • Histone H3 lysine 36 methylation antagonizes silencing in Saccharomyces cerevisiae independently of the Rpd3S histone deacetylase complex
    • Tompa, R., and H. D. Madhani. 2007. Histone H3 lysine 36 methylation antagonizes silencing in Saccharomyces cerevisiae independently of the Rpd3S histone deacetylase complex. Genetics 175:585-593.
    • (2007) Genetics , vol.175 , pp. 585-593
    • Tompa, R.1    Madhani, H.D.2
  • 53
    • 76749121101 scopus 로고    scopus 로고
    • Treco, D. A., and V. Lundblad. 1993. Basic techniques of yeast genetics, p.13.1.1-13.1.7. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, 2. John Wiley and Sons, New York, NY.
    • Treco, D. A., and V. Lundblad. 1993. Basic techniques of yeast genetics, p.13.1.1-13.1.7. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 2. John Wiley and Sons, New York, NY.
  • 54
    • 0033518179 scopus 로고    scopus 로고
    • The RCAF complex mediates chromatin assembly during DNA replication and repair
    • Tyler, J. K., C. R. Adams, S. R. Chen, R. Kobayashi, R. T. Kamakaka, and J. T. Kadonaga. 1999. The RCAF complex mediates chromatin assembly during DNA replication and repair. Nature 402:555-560.
    • (1999) Nature , vol.402 , pp. 555-560
    • Tyler, J.K.1    Adams, C.R.2    Chen, S.R.3    Kobayashi, R.4    Kamakaka, R.T.5    Kadonaga, J.T.6
  • 55
    • 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., D. Truong, and J. K. Tyler. 2008. Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc. Natl. Acad. Sci. U. S. A. 105:9000-9005.
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 9000-9005
    • Williams, S.K.1    Truong, D.2    Tyler, J.K.3
  • 58
    • 68349131435 scopus 로고    scopus 로고
    • yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement
    • Xin, H., S. Takahata, M. Blanksma, L. McCullough, D. J. Stillman, and T. Formosa. 2009. yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement. Mol. Cell 35:365-376.
    • (2009) Mol. Cell , vol.35 , pp. 365-376
    • Xin, H.1    Takahata, S.2    Blanksma, M.3    McCullough, L.4    Stillman, D.J.5    Formosa, T.6


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