메뉴 건너뛰기




Volumn 50, Issue 36, 2011, Pages 7822-7832

Comprehensive structural analysis of mutant nucleosomes containing lysine to glutamine (KQ) substitutions in the H3 and H4 histone-fold domains

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; AMINO ACID SUBSTITUTION; C-TERMINAL REGIONS; CHROMATIN STRUCTURE; HISTONE MODIFICATION; IN-VIVO; LYSINE RESIDUES; N-TERMINALS; NUCLEOSOMES; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN-DNA INTERACTIONS; STRUCTURAL BASIS;

EID: 80052459066     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201021h     Document Type: Article
Times cited : (37)

References (71)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • DOI 10.1038/38444
    • Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution Nature 389, 251-260 (Pubitemid 27406632)
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • Arents, G. and Moudrianakis, E. N. (1995) The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization Proc. Natl. Acad. Sci. U. S. A. 92, 11170-11174
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 4
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • DOI 10.1038/47412
    • Strahl, B. D. and Allis, C. D. (2000) The language of covalent histone modifications Nature 403, 41-45 (Pubitemid 30038513)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 5
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein, T. and Allis, C. D. (2001) Translating the histone code Science 293, 1074-1080 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 6
    • 33749657892 scopus 로고    scopus 로고
    • PTMs on H3 Variants before Chromatin Assembly Potentiate Their Final Epigenetic State
    • DOI 10.1016/j.molcel.2006.08.019, PII S1097276506006009
    • 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 (Pubitemid 44557123)
    • (2006) Molecular Cell , vol.24 , Issue.2 , pp. 309-316
    • Loyola, A.1    Bonaldi, T.2    Roche, D.3    Imhof, A.4    Almouzni, G.5
  • 7
    • 34548433964 scopus 로고    scopus 로고
    • Marking histone H3 variants: How, when and why?
    • DOI 10.1016/j.tibs.2007.08.004, PII S0968000407001922
    • Loyola, A. and Almouzni, G. (2007) Marking histone H3 variants: How, when and why? Trends Biochem. Sci. 32, 425-433 (Pubitemid 47369165)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.9 , pp. 425-433
    • Loyola, A.1    Almouzni, G.2
  • 8
    • 0037099664 scopus 로고    scopus 로고
    • Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization- postsource decay, and nanoelectrospray ionization tandem mass spectrometry
    • DOI 10.1006/abio.2002.5719
    • Zhang, K., Tang, H., Huang, L., Blankenship, J. W., Jones, P. R., Xiang, F., Yau, P. M., and Burlingame, A. L. (2002) Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization-postsource decay, and nanoelectrospray ionization tandem mass spectrometry Anal. Biochem. 306, 259-269 (Pubitemid 34791495)
    • (2002) Analytical Biochemistry , vol.306 , Issue.2 , pp. 259-269
    • Zhang, K.1    Tang, H.2    Huang, L.3    Blankenship, J.W.4    Jones, P.R.5    Xiang, F.6    Yau, P.M.7    Burlingame, A.L.8
  • 9
    • 0041382914 scopus 로고    scopus 로고
    • Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry
    • DOI 10.1023/A:1025334006014
    • Cocklin, R. R. and Wang, M. (2003) Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry J. Protein Chem. 22, 327-334 (Pubitemid 37087793)
    • (2003) Journal of Protein Chemistry , vol.22 , Issue.4 , pp. 327-334
    • Cocklin, R.R.1    Wang, M.2
  • 10
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone post-translational modifications by peptide mass fingerprinting
    • DOI 10.1007/s00412-003-0244-6
    • Zhang, L., Eugeni, E. E., Parthun, M. R., and Freitas, M. A. (2003) Identification of novel histone post-translational modifications by peptide mass fingerprinting Chromosoma 112, 77-86 (Pubitemid 37150565)
    • (2003) Chromosoma , vol.112 , Issue.2 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 11
    • 7544229161 scopus 로고    scopus 로고
    • Application of mass spectrometry to the identification and quantification of histone post-translational modifications
    • DOI 10.1002/jcb.20106
    • Freitas, M. A., Sklenar, A. R., and Parthun, M. R. (2004) Application of mass spectrometry to the identification and quantification of histone post-translational modifications J. Cell. Biochem. 92, 691-700 (Pubitemid 44264260)
    • (2004) Journal of Cellular Biochemistry , vol.92 , Issue.4 , pp. 691-700
    • Freitas, M.A.1    Sklenar, A.R.2    Parthun, M.R.3
  • 13
    • 33646900510 scopus 로고    scopus 로고
    • The tale beyond the tail: Histone core domain modifications and the regulation of chromatin structure
    • DOI 10.1093/nar/gkl338
    • Mersfelder, E. L. and Parthun, M. R. (2006) The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure Nucleic Acids Res. 34, 2653-2662 (Pubitemid 43985628)
    • (2006) Nucleic Acids Research , vol.34 , Issue.9 , pp. 2653-2662
    • Mersfelder, E.L.1    Parthun, M.R.2
  • 14
    • 40949099577 scopus 로고    scopus 로고
    • ε-acetyllysine in recombinant proteins
    • DOI 10.1038/nchembio.73, PII NCHEMBIO73
    • Neumann, H., Peak-Chew, S. Y., and Chin, J. W. (2008) Genetically encoding N(epsilon)-acetyllysine in recombinant proteins Nat. Chem. Biol. 4, 232-234 (Pubitemid 351414829)
    • (2008) Nature Chemical Biology , vol.4 , Issue.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 16
    • 79953719035 scopus 로고    scopus 로고
    • Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes
    • Shimko, J. C., North, J. A., Bruns, A. N., Poirier, M. G., and Ottesen, J. J. (2011) Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes J. Mol. Biol. 408, 187-204
    • (2011) J. Mol. Biol. , vol.408 , pp. 187-204
    • Shimko, J.C.1    North, J.A.2    Bruns, A.N.3    Poirier, M.G.4    Ottesen, J.J.5
  • 17
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: Essential role of lysines subject to reversible acetylation
    • Megee, P. C., Morgan, B. A., Mittman, B. A., and Smith, M. M. (1990) Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation Science 247, 841-845
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Mittman, B.A.3    Smith, M.M.4
  • 18
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • DOI 10.1093/emboj/17.11.3155
    • Zhang, W., Bone, J. R., Edmondson, D. G., Turner, B. M., and Roth, S. Y. (1998) Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase EMBO J. 17, 3155-3167 (Pubitemid 28254387)
    • (1998) EMBO Journal , vol.17 , Issue.11 , pp. 3155-3167
    • Zhang, W.1    Bone, J.R.2    Edmondson, D.G.3    Turner, B.M.4    Roth, S.Y.5
  • 19
    • 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
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4.
    • Collaborative Computational Project Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 24
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin, A. and Teplyakov, A. (1997) MOLREP: an Automated Program for Molecular Replacement J. Appl. Crystallogr. 30, 1022-1025 (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • DOI 10.1016/S0076-6879(99)04003-3
    • Luger, K., Rechsteiner, T. J., and Richmond, T. J. (1999) Preparation of nucleosome core particle from recombinant histones Methods Enzymol. 304, 3-19 (Pubitemid 29268874)
    • (1999) Methods in Enzymology , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 31
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 A resolution
    • DOI 10.1016/S0022-2836(02)00386-8
    • Davey, C. A., Sargent, D. F., Luger, K., Maeder, A. W., and Richmond, T. J. (2002) Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution J. Mol. Biol. 319, 1097-1113 (Pubitemid 34729421)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.5 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 32
    • 20444462007 scopus 로고    scopus 로고
    • Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle
    • DOI 10.1093/nar/gki663
    • Tsunaka, Y., Kajimura, N., Tate, S., and Morikawa, K. (2005) Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle Nucleic Acids Res. 33, 3424-3434 (Pubitemid 41194485)
    • (2005) Nucleic Acids Research , vol.33 , Issue.10 , pp. 3424-3434
    • Tsunaka, Y.1    Kajimura, N.2    Tate, S.-I.3    Morikawa, K.4
  • 33
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • DOI 10.1038/nature03714
    • Masumoto, H., Hawke, D., Kobayashi, R., and Verreault, A. (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response Nature 436, 294-298 (Pubitemid 41021284)
    • (2005) Nature , vol.436 , Issue.7048 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 34
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • DOI 10.1016/j.cell.2005.03.011, PII S0092867405002837
    • Xu, F., Zhang, K., and Grunstein, M. (2005) Acetylation in histone H3 globular domain regulates gene expression in yeast Cell 121, 375-385 (Pubitemid 40692298)
    • (2005) Cell , vol.121 , Issue.3 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 35
    • 34547277498 scopus 로고    scopus 로고
    • Genome-Wide Replication-Independent Histone H3 Exchange Occurs Predominantly at Promoters and Implicates H3 K56 Acetylation and Asf1
    • DOI 10.1016/j.molcel.2007.07.011, PII S1097276507004844
    • Rufiange, A., Jacques, P. E., Bhat, W., Robert, F., and Nourani, A. (2007) Genome-wide replication-independent histone H3 exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1 Mol. Cell 27, 393-405 (Pubitemid 47135636)
    • (2007) Molecular Cell , vol.27 , Issue.3 , pp. 393-405
    • Rufiange, A.1    Jacques, P.-E.2    Bhat, W.3    Robert, F.4    Nourani, A.5
  • 36
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated Lysine 56 on Histone H3 Drives Chromatin Assembly after Repair and Signals for the Completion of Repair
    • DOI 10.1016/j.cell.2008.06.035, PII S0092867408008222
    • Chen, C. C., Carson, J. J., Feser, J., Tamburini, B., Zabaronick, S., Linger, J., and Tyler, J. K. (2008) Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair Cell 134, 231-243 (Pubitemid 352010334)
    • (2008) Cell , vol.134 , Issue.2 , 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
  • 37
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
    • DOI 10.1016/j.cell.2008.06.018, PII S0092867408007708
    • Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., and Zhang, Z. (2008) Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly Cell 134, 244-255 (Pubitemid 352010333)
    • (2008) Cell , vol.134 , Issue.2 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5    Verreault, A.6    Zhang, Z.7
  • 40
    • 78650475567 scopus 로고    scopus 로고
    • Coordinated allele-specific histone acetylation at the differentially methylated regions of imprinted genes
    • Singh, P., Cho, J., Tsai, S. Y., Rivas, G. E., Larson, G. P., and Szabó, P. E. (2010) Coordinated allele-specific histone acetylation at the differentially methylated regions of imprinted genes Nucleic Acids Res. 38, 7974-7990
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7974-7990
    • Singh, P.1    Cho, J.2    Tsai, S.Y.3    Rivas, G.E.4    Larson, G.P.5    Szabó, P.E.6
  • 42
    • 0028801404 scopus 로고
    • Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription
    • Kruger, W., Peterson, C. L., Sil, A., Coburn, C., Arents, G., Moudrianakis, E. N., and Herskowitz, I. (1995) Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription Genes Dev. 9, 2770-2779
    • (1995) Genes Dev. , vol.9 , pp. 2770-2779
    • Kruger, W.1    Peterson, C.L.2    Sil, A.3    Coburn, C.4    Arents, G.5    Moudrianakis, E.N.6    Herskowitz, I.7
  • 43
    • 0030699092 scopus 로고    scopus 로고
    • Sin mutations of histone H3: Influence on nucleosome core structure and function
    • Kurumizaka, H. and Wolffe, A. P. (1997) Sin mutations of histone H3: influence on nucleosome core structure and function Mol. Cell. Biol. 17, 6953-6969 (Pubitemid 27505926)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 6953-6969
    • Kurumizaka, H.1    Wolffe, A.P.2
  • 44
    • 0030893061 scopus 로고    scopus 로고
    • - versions of histone H4 on yeast chromatin structure and function
    • DOI 10.1093/emboj/16.8.2086
    • Wechser, M. A., Kladde, M. P., Alfieri, J. A., and Peterson, C. L. (1997) Effects of Sin- versions of histone H4 on yeast chromatin structure and function EMBO J. 16, 2086-2095 (Pubitemid 27170969)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 2086-2095
    • Wechser, M.A.1    Kladde, M.P.2    Alfieri, J.A.3    Peterson, C.L.4
  • 45
    • 1542320757 scopus 로고    scopus 로고
    • Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions
    • DOI 10.1038/sj.emboj.7600046
    • Muthurajan, U. M., Bao, Y., Forsberg, L. J., Edayathumangalam, R. S., Dyer, P. N., White, C. L., and Luger, K. (2004) Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions EMBO J. 23, 260-271 (Pubitemid 38294491)
    • (2004) EMBO Journal , vol.23 , Issue.2 , pp. 260-271
    • Muthurajan, U.M.1    Bao, Y.2    Forsberg, L.J.3    Edayathumangalam, R.S.4    Dyer, P.N.5    White, C.L.6    Luger, K.7
  • 47
    • 27644467857 scopus 로고    scopus 로고
    • Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae
    • DOI 10.1128/MCB.25.22.10060-10070.2005
    • Hyland, E. M., Cosgrove, M. S., Molina, H., Wang, D., Pandey, A., Cottee, R. J., and Boeke, J. D. (2005) Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae Mol. Cell. Biol. 25, 10060-10070 (Pubitemid 41572751)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.22 , pp. 10060-10070
    • Hyland, E.M.1    Cosgrove, M.S.2    Molina, H.3    Wang, D.4    Pandey, A.5    Cottee, R.J.6    Boeke, J.D.7
  • 48
    • 29144491494 scopus 로고    scopus 로고
    • Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition
    • DOI 10.1021/pr050188r
    • Garcia, B. A., Busby, S. A., Shabanowitz, J., Hunt, D. F., and Mishra, N. (2005) Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition J. Proteome Res. 4, 2032-2042 (Pubitemid 41814269)
    • (2005) Journal of Proteome Research , vol.4 , Issue.6 , pp. 2032-2042
    • Garcia, B.A.1    Busby, S.A.2    Shabanowitz, J.3    Hunt, D.F.4    Mishra, N.5
  • 49
    • 15944416371 scopus 로고    scopus 로고
    • Histone H4 lysine 91 acetylation: A core domain modificationassociated with chromatin assembly
    • DOI 10.1016/j.molcel.2005.02.031
    • Ye, J., Ai, X., Eugeni, E. E., Zhang, L., Carpenter, L. R., Jelinek, M. A., Freitas, M. A., and Parthun, M. R. (2005) Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly Mol. Cell 18, 123-130 (Pubitemid 40444653)
    • (2005) Molecular Cell , vol.18 , Issue.1 , pp. 123-130
    • Ye, J.1    Ai, X.2    Eugeni, E.E.3    Zhang, L.4    Carpenter, L.R.5    Jelinek, M.A.6    Freitas, M.A.7    Parthun, M.R.8
  • 50
    • 1942502859 scopus 로고    scopus 로고
    • The nuclear Hat1p/Hat2p complex: A molecular link between type B histone acetyltransferases and chromatin assembly
    • DOI 10.1016/S1097-2765(04)00184-4, PII S1097276504001844
    • Ai, X. and Parthun, M. R. (2004) The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly Mol. Cell 14, 195-205 (Pubitemid 38515647)
    • (2004) Molecular Cell , vol.14 , Issue.2 , pp. 195-205
    • Ai, X.1    Parthun, M.R.2
  • 51
    • 70349759491 scopus 로고    scopus 로고
    • BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response
    • Yan, Q., Dutt, S., Xu, R., Graves, K., Juszczynski, P., Manis, J. P., and Shipp, M. A. (2009) BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response Mol. Cell 36, 110-120
    • (2009) Mol. Cell , vol.36 , pp. 110-120
    • Yan, Q.1    Dutt, S.2    Xu, R.3    Graves, K.4    Juszczynski, P.5    Manis, J.P.6    Shipp, M.A.7
  • 52
    • 33745950498 scopus 로고    scopus 로고
    • Chromatin Assembly with H3 Histones: Full Throttle Down Multiple Pathways
    • DOI 10.1016/S0070-2153(06)74002-9, PII S0070215306740029
    • Schwartz, B. E. and Ahmad, K. (2006) Chromatin Assembly with H3 Histones: Full Throttle Down Multiple Pathways Curr. Top. Dev. Biol. 74, 31-55 (Pubitemid 44062703)
    • (2006) Current Topics in Developmental Biology , vol.74 , pp. 31-55
    • Schwartz, B.E.1    Ahmad, K.2
  • 53
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • DOI 10.1016/S0960-9822(02)00901-6, PII S0960982202009016
    • Feng, Q., Wang, H., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Struhl, K., and Zhang, Y. (2002) Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain Curr. Biol. 12, 1052-1058 (Pubitemid 34703339)
    • (2002) Current Biology , vol.12 , Issue.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3    Erdjument-Bromage, H.4    Tempst, P.5    Struhl, K.6    Zhang, Y.7
  • 56
    • 53549124960 scopus 로고    scopus 로고
    • The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure
    • Lu, X., Simon, M. D., Chodaparambil, J. V., Hansen, J. C., Shokat, K. M., and Luger, K. (2008) The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure Nat. Struct. Mol. Biol. 15, 1122-1124
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1122-1124
    • Lu, X.1    Simon, M.D.2    Chodaparambil, J.V.3    Hansen, J.C.4    Shokat, K.M.5    Luger, K.6
  • 57
    • 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., Fingerman, I. M., and Briggs, S. D. (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
  • 58
    • 27744577727 scopus 로고    scopus 로고
    • Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription
    • DOI 10.1016/j.cell.2005.10.023, PII S0092867405011566
    • Carrozza, M. J., Li, B., Florens, L., Suganuma, T., Swanson, S. K., Lee, K. K., Shia, W. J., Anderson, S., Yates, J., Washburn, M. P., and Workman, J. L. (2005) Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription Cell 123, 581-592 (Pubitemid 41608462)
    • (2005) Cell , vol.123 , Issue.4 , pp. 581-592
    • Carrozza, M.J.1    Li, B.2    Florens, L.3    Suganuma, T.4    Swanson, S.K.5    Lee, K.K.6    Shia, W.-J.7    Anderson, S.8    Yates, J.9    Washburn, M.P.10    Workman, J.L.11
  • 59
    • 29144468972 scopus 로고    scopus 로고
    • Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to pol II elongation
    • DOI 10.1016/j.molcel.2005.11.021, PII S1097276505018083
    • Joshi, A. A. and Struhl, K. (2005) Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation Mol. Cell 20, 971-978 (Pubitemid 41814885)
    • (2005) Molecular Cell , vol.20 , Issue.6 , pp. 971-978
    • Joshi, A.A.1    Struhl, K.2
  • 61
    • 34249099730 scopus 로고    scopus 로고
    • Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin
    • DOI 10.1126/science.1139004
    • Li, B., Gogol, M., Carey, M., Lee, D., Seidel, C., and Workman, J. L. (2007) Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin Science 316, 1050-1054 (Pubitemid 46799495)
    • (2007) Science , vol.316 , Issue.5827 , pp. 1050-1054
    • Li, B.1    Gogol, M.2    Carey, M.3    Lee, D.4    Seidel, C.5    Workman, J.L.6
  • 63
    • 77951249838 scopus 로고    scopus 로고
    • A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 Lys36 methylation, histone acetylation, and repression of cryptic transcription
    • Du, H. N. and Briggs, S. D. (2010) A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 Lys36 methylation, histone acetylation, and repression of cryptic transcription J. Biol. Chem. 285, 11704-11713
    • (2010) J. Biol. Chem. , vol.285 , pp. 11704-11713
    • Du, H.N.1    Briggs, S.D.2
  • 64
    • 4444378379 scopus 로고    scopus 로고
    • Histone variant H2ABbd confers lower stability to the nucleosome
    • DOI 10.1038/sj.embor.7400182
    • Gautier, T., Abbott, D. W., Molla, A., Verdel, A., Ausio, J., and Dimitrov, S. (2004) Histone variant H2ABbd confers lower stability to the nucleosome EMBO Rep. 5, 715-720 (Pubitemid 39173008)
    • (2004) EMBO Reports , vol.5 , Issue.7 , pp. 715-720
    • Gautier, T.1    Abbott, D.W.2    Molla, A.3    Verdel, A.4    Ausio, J.5    Dimitrov, S.6
  • 68
    • 33750477650 scopus 로고    scopus 로고
    • Structural Basis for the Histone Chaperone Activity of Asf1
    • DOI 10.1016/j.cell.2006.08.047, PII S0092867406012736
    • English, C. M., Adkins, M. W., Carson, J. J., Churchill, M. E. A., and Tyler, J. K. (2006) Structural basis for the histone chaperone activity of Asf1 Cell 127, 495-508 (Pubitemid 44647420)
    • (2006) Cell , vol.127 , Issue.3 , pp. 495-508
    • English, C.M.1    Adkins, M.W.2    Carson, J.J.3    Churchill, M.E.A.4    Tyler, J.K.5
  • 69
    • 33846574739 scopus 로고    scopus 로고
    • Structure of the yeast histone H3-ASFI interaction: Implications for chaperone mechanism, species-specific interactions, and epigenetics
    • Antczak, A. J., Tsubota, T., Kaufman, P. D., and Berger, J. M. (2006) Structure of the yeast histone H3-ASFI interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics. BMC Struct. Biol. 6:26.
    • (2006) BMC Struct. Biol. , vol.626
    • Antczak, A.J.1    Tsubota, T.2    Kaufman, P.D.3    Berger, J.M.4
  • 70
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • DOI 10.1038/nature05613, PII NATURE05613
    • Natsume, R., Eitoku, M., Akai, Y., Sano, N., Horikoshi, M., and Senda, T. (2007) Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4 Nature 446, 338-341 (Pubitemid 46437114)
    • (2007) Nature , vol.446 , Issue.7133 , pp. 338-341
    • Natsume, R.1    Eitoku, M.2    Akai, Y.3    Sano, N.4    Horikoshi, M.5    Senda, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.