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Volumn 41, Issue 4, 2013, Pages 2228-2238

Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHROMATIN PROTEIN; GLUTAMINE; HISTONE H4; LYSINE; UNCLASSIFIED DRUG;

EID: 84876404522     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks1451     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 33947098453 scopus 로고    scopus 로고
    • Histone replacement marks the boundaries of cis-regulatory domains
    • Mito, Y., Henikoff, J. 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.2    Henikoff, S.3
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function. Cell, 128, 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 0035815105 scopus 로고    scopus 로고
    • Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites
    • Anderson, J.D., Lowary, P.T. and Widom, J. (2001) Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites. J. Mol. Biol., 307, 977-985.
    • (2001) J. Mol. Biol , vol.307 , pp. 977-985
    • Anderson, J.D.1    Lowary, P.T.2    Widom, J.3
  • 4
    • 0024573304 scopus 로고
    • Use of selectively trypsinized nucleosome core particles to analyze the role of the histone ''tails'' in the stabilization of the nucleosome
    • Ausio, J., Dong, F. and van Holde, K.E. (1989) Use of selectively trypsinized nucleosome core particles to analyze the role of the histone ''tails'' in the stabilization of the nucleosome. J. Mol. Biol., 206, 451-463.
    • (1989) J. Mol. Biol , vol.206 , pp. 451-463
    • Ausio, J.1    Dong, F.2    Van Holde, K.E.3
  • 5
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. (1997) Histone acetylation in chromatin structure and transcription. Nature, 389, 349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 6
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants mechanisms, and functions
    • Hansen, J.C. (2002) Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions. Annu. Rev. Biophys. Biomol. Struct., 31, 361-392.
    • (2002) Annu. Rev. Biophys. Biomol. Struct , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 7
    • 0024286928 scopus 로고
    • Histone acetylation in chicken erythrocytes. Rates of deacetylation in immature and mature red blood cells
    • Zhang, D.E. and Nelson, D.A. (1988) Histone acetylation in chicken erythrocytes. Rates of deacetylation in immature and mature red blood cells. Biochem. J., 250, 241-245.
    • (1988) Biochem. J , vol.250 , pp. 241-245
    • Zhang, D.E.1    Nelson, D.A.2
  • 8
    • 0025720512 scopus 로고
    • Histone deacetylase is a component of the internal nuclear matrix
    • Hendzel, M.J., Delcuve, G.P. and Davie, J.R. (1991) Histone deacetylase is a component of the internal nuclear matrix. J. Biol. Chem., 266, 21936-21942.
    • (1991) J. Biol. Chem , vol.266 , pp. 21936-21942
    • Hendzel, M.J.1    Delcuve, G.P.2    Davie, J.R.3
  • 9
    • 69449102464 scopus 로고    scopus 로고
    • Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
    • Wang, Z., Zang, C., Cui, K., Schones, D.E., Barski, A., Peng, W. and Zhao, K. (2009) Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes. Cell, 138, 1019-1031.
    • (2009) Cell , vol.138 , pp. 1019-1031
    • Wang, Z.1    Zang, C.2    Cui, K.3    Schones, D.E.4    Barski, A.5    Peng, W.6    Zhao, K.7
  • 10
    • 0035957097 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in Saccharomyces cerevisiae
    • Waterborg, J.H. (2001) Dynamics of histone acetylation in Saccharomyces cerevisiae. Biochemistry, 40, 2599-2605.
    • (2001) Biochemistry , vol.40 , pp. 2599-2605
    • Waterborg, J.H.1
  • 11
    • 0035986095 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in vivo A function for acetylation turnover? Biochem
    • Waterborg, J.H. (2002) Dynamics of histone acetylation in vivo A function for acetylation turnover? Biochem. Cell Biol., 80, 363-378.
    • (2002) Cell Biol , vol.80 , pp. 363-378
    • Waterborg, J.H.1
  • 12
    • 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
  • 13
    • 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
  • 14
    • 1242342240 scopus 로고    scopus 로고
    • Histone H3.3 is enriched in covalent modifications associated with active chromatin
    • McKittrick, E., Gafken, P.R., Ahmad, K. and Henikoff, S. (2004) Histone H3.3 is enriched in covalent modifications associated with active chromatin. Proc. Natl Acad. Sci. USA, 101, 1525-1530.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1525-1530
    • McKittrick, E.1    Gafken, P.R.2    Ahmad, K.3    Henikoff, S.4
  • 16
    • 33749599697 scopus 로고    scopus 로고
    • Deposition and function of histone H3 variants in Tetrahymena thermophila
    • Cui, B., Liu, Y. and Gorovsky, M.A. (2006) Deposition and function of histone H3 variants in Tetrahymena thermophila. Mol. Cell Biol., 26, 7719-7730.
    • (2006) Mol. Cell Biol , vol.26 , pp. 7719-7730
    • Cui, B.1    Liu, Y.2    Gorovsky, M.A.3
  • 17
    • 67650960676 scopus 로고    scopus 로고
    • Transcription in the absence of histone H3.3. Curr
    • Hodl, M. and Basler, K. (2009) Transcription in the absence of histone H3.3. Curr. Biol., 19, 1221-1226.
    • (2009) Biol , vol.19 , pp. 1221-1226
    • Hodl, M.1    Basler, K.2
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0032824943 scopus 로고    scopus 로고
    • Histone proteins in vivo: Cell-cycle-dependent physiological effects of exogenous linker histones incorporated into Physarum polycephalum
    • Thiriet, C. and Hayes, J.J. (1999) Histone proteins in vivo: cell-cycle-dependent physiological effects of exogenous linker histones incorporated into Physarum polycephalum. Methods, 17, 140-150.
    • (1999) Methods , vol.17 , pp. 140-150
    • Thiriet, C.1    Hayes, J.J.2
  • 21
    • 1642346956 scopus 로고    scopus 로고
    • Analysis of chromatin assembled in vivo using exogenous histones in Physarum polycephalum
    • Thiriet, C. (2004) Analysis of chromatin assembled in vivo using exogenous histones in Physarum polycephalum. Methods, 33, 86-92.
    • (2004) Methods , vol.33 , pp. 86-92
    • Thiriet, C.1
  • 22
    • 15444376394 scopus 로고    scopus 로고
    • Replication-independent core histone dynamics at transcriptionally active loci in vivo
    • Thiriet, C. and Hayes, J.J. (2005) Replication-independent core histone dynamics at transcriptionally active loci in vivo. Genes Dev., 19, 677-682.
    • (2005) Genes Dev , vol.19 , pp. 677-682
    • Thiriet, C.1    Hayes, J.J.2
  • 23
    • 37549023859 scopus 로고    scopus 로고
    • Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure
    • Wang, X. and Hayes, J.J. (2008) Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure. Mol. Cell Biol., 28, 227-236.
    • (2008) Mol. Cell Biol , vol.28 , pp. 227-236
    • Wang, X.1    Hayes, J.J.2
  • 24
    • 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. and Almouzni, G. (2006) PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state. Mol. Cell, 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
  • 25
    • 84255198348 scopus 로고    scopus 로고
    • A specific function for the histone chaperone NASP to fine-tune a reservoir of soluble H3-H4 in the histone supply chain
    • Cook, A.J., Gurard-Levin, Z.A., Vassias, I. and Almouzni, G. (2011) A specific function for the histone chaperone NASP to fine-tune a reservoir of soluble H3-H4 in the histone supply chain. Mol. Cell, 44, 918-927.
    • (2011) Mol. Cell , vol.44 , pp. 918-927
    • Cook, A.J.1    Gurard-Levin, Z.A.2    Vassias, I.3    Almouzni, G.4
  • 26
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison, C., Bailly, D., Peters, A.H., Quivy, J.P., Roche, D., Taddei, A., Lachner, M., Jenuwein, T. and Almouzni, G. (2002) Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat. Genet., 30, 329-334.
    • (2002) Nat. Genet , vol.30 , pp. 329-334
    • Maison, C.1    Bailly, D.2    Peters, A.H.3    Quivy, J.P.4    Roche, D.5    Taddei, A.6    Lachner, M.7    Jenuwein, T.8    Almouzni, G.9
  • 27
    • 0016337102 scopus 로고
    • Molecular basis of control of mitotic cell division in eukaryotes
    • Bradbury, E.M., Inglis, R.J., Matthews, H.R. and Langan, T.A. (1974) Molecular basis of control of mitotic cell division in eukaryotes. Nature, 249, 553-556.
    • (1974) Nature , vol.249 , pp. 553-556
    • Bradbury, E.M.1    Inglis, R.J.2    Matthews, H.R.3    Langan, T.A.4
  • 28
    • 0018891793 scopus 로고
    • Incorporation of exogenous pyrene-labeled histone into Physarum chromatin: A system for studying changes in nucleosomes assembled in vivo
    • Prior, C.P., Cantor, C.R., Johnson, E.M. and Allfrey, V.G. (1980) Incorporation of exogenous pyrene-labeled histone into Physarum chromatin: a system for studying changes in nucleosomes assembled in vivo. Cell, 20, 597-608.
    • (1980) Cell , vol.20 , pp. 597-608
    • Prior, C.P.1    Cantor, C.R.2    Johnson, E.M.3    Allfrey, V.G.4
  • 29
    • 0020554124 scopus 로고
    • Reversible changes in nucleosome structure and histone H3 accessibility in transcriptionally active and inactive states of rDNA chromatin
    • Prior, C.P., Cantor, C.R., Johnson, E.M., Littau, V.C. and Allfrey, V.G. (1983) Reversible changes in nucleosome structure and histone H3 accessibility in transcriptionally active and inactive states of rDNA chromatin. Cell, 34, 1033-1042.
    • (1983) Cell , vol.34 , pp. 1033-1042
    • Prior, C.P.1    Cantor, C.R.2    Johnson, E.M.3    Littau, V.C.4    Allfrey, V.G.5
  • 30
    • 0035881855 scopus 로고    scopus 로고
    • A novel labeling technique reveals a function for histone H2A/H2B dimer tail domains in chromatin assembly in vivo
    • Thiriet, C. and Hayes, J.J. (2001) A novel labeling technique reveals a function for histone H2A/H2B dimer tail domains in chromatin assembly in vivo. Genes Dev., 15, 2048-2053.
    • (2001) Genes Dev , vol.15 , pp. 2048-2053
    • Thiriet, C.1    Hayes, J.J.2
  • 31
    • 0023664692 scopus 로고
    • Histone synthesis during the cell cycle of Physarum polycephalum. Synthesis of different histone species is not under a common regulatory control
    • Loidl, P. and Grobner, P. (1987) Histone synthesis during the cell cycle of Physarum polycephalum. Synthesis of different histone species is not under a common regulatory control. J. Biol. Chem., 262, 10195-10199.
    • (1987) J. Biol. Chem , vol.262 , pp. 10195-10199
    • Loidl, P.1    Grobner, P.2
  • 32
    • 0033710367 scopus 로고    scopus 로고
    • Role of histone acetylation in the assembly and modulation of chromatin structures
    • Annunziato, A.T. and Hansen, J.C. (2000) Role of histone acetylation in the assembly and modulation of chromatin structures. Gene Expr., 9, 37-61.
    • (2000) Gene Expr , vol.9 , pp. 37-61
    • Annunziato, A.T.1    Hansen, J.C.2
  • 33
    • 78751531687 scopus 로고    scopus 로고
    • H4 replication-dependent diacetylation and Hat1 promote S-phase chromatin assembly in vivo
    • Ejlassi-Lassallette, A., Mocquard, E., Arnaud, M.C. and Thiriet, C. (2011) H4 replication-dependent diacetylation and Hat1 promote S-phase chromatin assembly in vivo. Mol. Biol. Cell, 22, 245-255.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 245-255
    • Ejlassi-Lassallette, A.1    Mocquard, E.2    Arnaud, M.C.3    Thiriet, C.4
  • 34
    • 0344688414 scopus 로고    scopus 로고
    • A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae
    • Gunjan, A. and Verreault, A. (2003) A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae. Cell, 115, 537-549.
    • (2003) Cell , vol.115 , pp. 537-549
    • Gunjan, A.1    Verreault, A.2
  • 35
  • 36
    • 0038449280 scopus 로고    scopus 로고
    • Developmentally regulated usage of Physarum DNA replication origins
    • Maric, C., Benard, M. and Pierron, G. (2003) Developmentally regulated usage of Physarum DNA replication origins. EMBO Rep., 4, 474-478.
    • (2003) EMBO Rep , vol.4 , pp. 474-478
    • Maric, C.1    Benard, M.2    Pierron, G.3
  • 37
    • 0024544492 scopus 로고
    • Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
    • Lin, R., Leone, J.W., Cook, R.G. and Allis, C.D. (1989) Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena. J. Cell Biol., 108, 1577-1588.
    • (1989) J. Cell Biol , vol.108 , pp. 1577-1588
    • Lin, R.1    Leone, J.W.2    Cook, R.G.3    Allis, C.D.4
  • 38
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • Sobel, R.E., Cook, R.G., Perry, C.A., Annunziato, A.T. and Allis, C.D. (1995) Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Proc. Natl Acad. Sci. USA, 92, 1237-1241.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1237-1241
    • Sobel, R.E.1    Cook, R.G.2    Perry, C.A.3    Annunziato, A.T.4    Allis, C.D.5
  • 39
    • 0035941198 scopus 로고    scopus 로고
    • Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase
    • Makowski, A.M., Dutnall, R.N. and Annunziato, A.T. (2001) Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase. J. Biol. Chem., 276, 43499-43502.
    • (2001) J. Biol. Chem , vol.276 , pp. 43499-43502
    • Makowski, A.M.1    Dutnall, R.N.2    Annunziato, A.T.3
  • 40
  • 41
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura, H. and Cook, P.R. (2001) Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B. J. Cell. Biol., 153, 1341-1353.
    • (2001) J. Cell. Biol , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 42
    • 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. and Nakatani, Y. (2004) Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell, 116, 51-61.
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 43
    • 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. and Allis, C.D. (2010) Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl Acad. Sci. USA, 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
  • 44
    • 21244491441 scopus 로고    scopus 로고
    • Regulation of histone synthesis and nucleosome assembly
    • Gunjan, A., Paik, J. and Verreault, A. (2005) Regulation of histone synthesis and nucleosome assembly. Biochimie, 87, 625-635.
    • (2005) Biochimie , vol.87 , pp. 625-635
    • Gunjan, A.1    Paik, J.2    Verreault, A.3
  • 45
    • 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. and Almouzni, G. (2007) Regulation of replication fork progression through histone supply and demand. Science, 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
  • 46
    • 0021093461 scopus 로고
    • Structure of chromatin at deoxyribonucleic acid replication forks: Nuclease hypersensitivity results from both prenucleosomal deoxyribonucleic acid and an immature chromatin structure
    • Cusick, M.E., Lee, K.S., DePamphilis, M.L. and Wassarman, P.M. (1983) Structure of chromatin at deoxyribonucleic acid replication forks: nuclease hypersensitivity results from both prenucleosomal deoxyribonucleic acid and an immature chromatin structure. Biochemistry, 22, 3873-3884.
    • (1983) Biochemistry , vol.22 , pp. 3873-3884
    • Cusick, M.E.1    Lee, K.S.2    Depamphilis, M.L.3    Wassarman, P.M.4
  • 47
    • 0020491951 scopus 로고
    • Maturation of nucleosomal and nonnucleosomal components of nascent chromatin: Differential requirements for concurrent protein synthesis
    • Annunziato, A.T. and Seale, R.L. (1982) Maturation of nucleosomal and nonnucleosomal components of nascent chromatin: differential requirements for concurrent protein synthesis. Biochemistry, 21, 5431-5438.
    • (1982) Biochemistry , vol.21 , pp. 5431-5438
    • Annunziato, A.T.1    Seale, R.L.2
  • 48
    • 17244368913 scopus 로고    scopus 로고
    • Genomic characterization reveals a simple histone H4 acetylation code
    • Dion, M.F., Altschuler, S.J., Wu, L.F. and Rando, O.J. (2005) Genomic characterization reveals a simple histone H4 acetylation code. Proc. Natl Acad. Sci. USA, 102, 5501-5506.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5501-5506
    • Dion, M.F.1    Altschuler, S.J.2    Wu, L.F.3    Rando, O.J.4
  • 49
    • 84864837861 scopus 로고    scopus 로고
    • Drosophila dosage compensation involves enhanced Pol II recruitment to male X-linked promoters
    • Conrad, T., Cavalli, F.M., Vaquerizas, J.M., Luscombe, N.M. and Akhtar, A. (2012) Drosophila dosage compensation involves enhanced Pol II recruitment to male X-linked promoters. Science, 337, 742-746.
    • (2012) Science , vol.337 , pp. 742-746
    • Conrad, T.1    Cavalli, F.M.2    Vaquerizas, J.M.3    Luscombe, N.M.4    Akhtar, A.5
  • 51
    • 84866497062 scopus 로고    scopus 로고
    • Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes
    • Venkatesh, S., Smolle, M., Li, H., Gogol, M.M., Saint, M., Kumar, S., Natarajan, K. and Workman, J.L. (2012) Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes. Nature, 489, 452-455.
    • (2012) Nature , vol.489 , pp. 452-455
    • Venkatesh, S.1    Smolle, M.2    Li, H.3    Gogol, M.M.4    Saint, M.5    Kumar, S.6    Natarajan, K.7    Workman, J.L.8


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