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Volumn 1819, Issue 8, 2012, Pages 892-901

Ascending the nucleosome face: Recognition and function of structured domains in the histone H2A-H2B dimer

Author keywords

Acidic patch; Histone H2A and H2B; Nucleosome recognition; Post translational modification; Sir3

Indexed keywords

ADENOSINE KINASE; DIMER; HISTONE H2A; HISTONE H2B; HISTONE H4; LATENCY ASSOCIATED NUCLEAR ANTIGEN; RNA POLYMERASE II; SIRTUIN 3; TRANSCRIPTION FACTOR SAGA;

EID: 84861968365     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2012.04.001     Document Type: Review
Times cited : (20)

References (103)
  • 1
    • 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
  • 2
    • 33847076248 scopus 로고    scopus 로고
    • Chromatin challenges during DNA replication and repair
    • Groth A., Rocha W., Verreault A., Almouzni G. Chromatin challenges during DNA replication and repair. Cell 2007, 128:721-733.
    • (2007) Cell , vol.128 , pp. 721-733
    • Groth, A.1    Rocha, W.2    Verreault, A.3    Almouzni, G.4
  • 3
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007, 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 5
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
    • Taverna S.D., Li H., Ruthenburg A.J., Allis C.D., Patel D.J. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nat. Struct. Mol. Biol. 2007, 14:1025-1040.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 6
    • 82955247642 scopus 로고    scopus 로고
    • Recognition of methylated histones: new twists and variations
    • Khorasanizadeh S. Recognition of methylated histones: new twists and variations. Curr. Opin. Struct. Biol. 2011, 21:744-749.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 744-749
    • Khorasanizadeh, S.1
  • 7
    • 79954416946 scopus 로고    scopus 로고
    • Readers of histone modifications
    • Yun M., Wu J., Workman J.L., Li B. Readers of histone modifications. Cell Res. 2011, 21:564-578.
    • (2011) Cell Res. , vol.21 , pp. 564-578
    • Yun, M.1    Wu, J.2    Workman, J.L.3    Li, B.4
  • 8
    • 82955195929 scopus 로고    scopus 로고
    • Recognition of non-methyl histone marks
    • Bycroft M. Recognition of non-methyl histone marks. Curr. Opin. Struct. Biol. 2011, 21:761-766.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 761-766
    • Bycroft, M.1
  • 10
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • Hansen J.C., Lu X., Ross E.D., Woody R.W. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J. Biol. Chem. 2006, 281:1853-1856.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 12
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6:197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • Mittag T., Kay L.E., Forman-Kay J.D. Protein dynamics and conformational disorder in molecular recognition. J. Mol. Recognit. 2010, 23:105-116.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 15
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 16
    • 0037992395 scopus 로고    scopus 로고
    • The structure of DNA in the nucleosome core
    • Richmond T.J., Davey C.A. The structure of DNA in the nucleosome core. Nature 2003, 423:145-150.
    • (2003) Nature , vol.423 , pp. 145-150
    • Richmond, T.J.1    Davey, C.A.2
  • 17
    • 77957367439 scopus 로고    scopus 로고
    • Structure of RCC1 chromatin factor bound to the nucleosome core particle
    • Makde R.D., England J.R., Yennawar H.P., Tan S. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 2010, 467:562-566.
    • (2010) Nature , vol.467 , pp. 562-566
    • Makde, R.D.1    England, J.R.2    Yennawar, H.P.3    Tan, S.4
  • 21
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution
    • Davey C.A., Sargent D.F., Luger K., Maeder A.W., Richmond T.J. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution. J. Mol. Biol. 2002, 319:1097-1113.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 24
    • 77957369358 scopus 로고    scopus 로고
    • Histone H2B ubiquitination and beyond: regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation
    • Chandrasekharan M.B., Huang F., Sun Z.-W. Histone H2B ubiquitination and beyond: regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation. Epigenetics 2010, 5:460-468.
    • (2010) Epigenetics , vol.5 , pp. 460-468
    • Chandrasekharan, M.B.1    Huang, F.2    Sun, Z.-W.3
  • 25
    • 33746324216 scopus 로고    scopus 로고
    • Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression
    • Shilatifard A. Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression. Annu. Rev. Biochem. 2006, 75:243-269.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 243-269
    • Shilatifard, A.1
  • 27
    • 75149171523 scopus 로고    scopus 로고
    • Silent information regulator 3: the Goldilocks of the silencing complex
    • Norris A., Boeke J.D. Silent information regulator 3: the Goldilocks of the silencing complex. Genes Dev. 2010, 24:115-122.
    • (2010) Genes Dev. , vol.24 , pp. 115-122
    • Norris, A.1    Boeke, J.D.2
  • 28
    • 0020131558 scopus 로고
    • Participation of core histone "tails" in the stabilization of the chromatin solenoid
    • Allan J., Harborne N., Rau D.C., Gould H. Participation of core histone "tails" in the stabilization of the chromatin solenoid. J. Cell Biol. 1982, 93:285-297.
    • (1982) J. Cell Biol. , vol.93 , pp. 285-297
    • Allan, J.1    Harborne, N.2    Rau, D.C.3    Gould, H.4
  • 29
    • 0030922941 scopus 로고    scopus 로고
    • Hybrid trypsinized nucleosomal arrays: identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction
    • Tse C., Hansen J.C. Hybrid trypsinized nucleosomal arrays: identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction. Biochemistry 1997, 36:11381-11388.
    • (1997) Biochemistry , vol.36 , pp. 11381-11388
    • Tse, C.1    Hansen, J.C.2
  • 30
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: requirement for the histone H4 N-terminal tail
    • Dorigo B., Schalch T., Bystricky K., Richmond T.J. Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J. Mol. Biol. 2003, 327:85-96.
    • (2003) J. Mol. Biol. , vol.327 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.J.4
  • 31
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak M., Ishii H., Sun J.M., Pazin M.J., Davie J.R., Peterson C.L. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 2006, 311:844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 34
    • 53249093714 scopus 로고    scopus 로고
    • Molecular mimicry between IL-33 and KSHV for attachment to chromatin through the H2A-H2B acidic pocket
    • Roussel L., Erard M., Cayrol C., Girard J.-P. Molecular mimicry between IL-33 and KSHV for attachment to chromatin through the H2A-H2B acidic pocket. EMBO Rep. 2008, 9:1006-1012.
    • (2008) EMBO Rep. , vol.9 , pp. 1006-1012
    • Roussel, L.1    Erard, M.2    Cayrol, C.3    Girard, J.-P.4
  • 35
    • 79961085477 scopus 로고    scopus 로고
    • Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR
    • Kato H., van Ingen H., Zhou B.-R., Feng H., Bustin M., Kay L.E., Bai Y. Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:12283-12288.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 12283-12288
    • Kato, H.1    van Ingen, H.2    Zhou, B.-R.3    Feng, H.4    Bustin, M.5    Kay, L.E.6    Bai, Y.7
  • 36
    • 81555212272 scopus 로고    scopus 로고
    • Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution
    • Armache K.-J., Garlick J.D., Canzio D., Narlikar G.J., Kingston R.E. Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution. Science 2011, 334:977-982.
    • (2011) Science , vol.334 , pp. 977-982
    • Armache, K.-J.1    Garlick, J.D.2    Canzio, D.3    Narlikar, G.J.4    Kingston, R.E.5
  • 38
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto R.K., Clarkson M.J., Tremethick D.J., Luger K. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 2000, 7:1121-1124.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 39
    • 79957495040 scopus 로고    scopus 로고
    • Histone H2A.Z acid patch residues required for deposition and function
    • Jensen K., Santisteban M.S., Urekar C., Smith M.M. Histone H2A.Z acid patch residues required for deposition and function. Mol. Genet. Genomics 2011, 285:287-296.
    • (2011) Mol. Genet. Genomics , vol.285 , pp. 287-296
    • Jensen, K.1    Santisteban, M.S.2    Urekar, C.3    Smith, M.M.4
  • 40
    • 0033578004 scopus 로고    scopus 로고
    • Regions of variant histone His2AvD required for Drosophila development
    • Clarkson M.J., Wells J.R.E., Gibson F., Saint R., Tremethick D.J. Regions of variant histone His2AvD required for Drosophila development. Nature 1999, 399:694-697.
    • (1999) Nature , vol.399 , pp. 694-697
    • Clarkson, M.J.1    Wells, J.R.E.2    Gibson, F.3    Saint, R.4    Tremethick, D.J.5
  • 42
    • 33845880445 scopus 로고    scopus 로고
    • Global analysis of functional surfaces of core histones with comprehensive point mutants
    • Matsubara K., Sano N., Umehara T., Horikoshi M. Global analysis of functional surfaces of core histones with comprehensive point mutants. Genes Cells 2007, 12:13-33.
    • (2007) Genes Cells , vol.12 , pp. 13-33
    • Matsubara, K.1    Sano, N.2    Umehara, T.3    Horikoshi, M.4
  • 43
    • 35848936709 scopus 로고    scopus 로고
    • Cross-regulation of histone modifications
    • Latham J.A., Dent S.Y. Cross-regulation of histone modifications. Nat. Struct. Mol. Biol. 2007, 14:1017-1024.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1017-1024
    • Latham, J.A.1    Dent, S.Y.2
  • 44
    • 34547949573 scopus 로고    scopus 로고
    • A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway
    • Fingerman I.M., Li H.C., Briggs S.D. A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway. Genes Dev. 2007, 21:2018-2029.
    • (2007) Genes Dev. , vol.21 , pp. 2018-2029
    • Fingerman, I.M.1    Li, H.C.2    Briggs, S.D.3
  • 45
    • 37349107849 scopus 로고    scopus 로고
    • Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin
    • Altaf M., Utley R.T., Lacoste N., Tan S., Briggs S.D., Cote J. Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin. Mol. Cell 2007, 28:1002-1014.
    • (2007) Mol. Cell , vol.28 , pp. 1002-1014
    • Altaf, M.1    Utley, R.T.2    Lacoste, N.3    Tan, S.4    Briggs, S.D.5    Cote, J.6
  • 46
    • 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., Briggs S.D. Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4. Genes Dev. 2008, 22:2786-2798.
    • (2008) Genes Dev. , vol.22 , pp. 2786-2798
    • Du, H.N.1    Fingerman, I.M.2    Briggs, S.D.3
  • 47
    • 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., Briggs S.D. 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. 2010, 285:11704-11713.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11704-11713
    • Du, H.-N.1    Briggs, S.D.2
  • 49
    • 71949086318 scopus 로고    scopus 로고
    • Set2-dependent K36 methylation is regulated by novel intratail interactions within H3
    • Psathas J.N., Zheng S., Tan S., Reese J.C. Set2-dependent K36 methylation is regulated by novel intratail interactions within H3. Mol. Cell. Biol. 2009, 29:6413-6426.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6413-6426
    • Psathas, J.N.1    Zheng, S.2    Tan, S.3    Reese, J.C.4
  • 50
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K., Recht J., Osley M.A. Rad6-dependent ubiquitination of histone H2B in yeast. Science 2000, 287:501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 51
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C., Madhani H.D. A conserved RING finger protein required for histone H2B monoubiquitination and cell size control. Mol. Cell 2003, 11:261-266.
    • (2003) Mol. Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1    Venkatasubrahmanyam, S.2    Ianculescu, A.G.3    Tong, A.4    Boone, C.5    Madhani, H.D.6
  • 55
    • 21744433162 scopus 로고    scopus 로고
    • Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: distinct roles in telomeric silencing and general chromatin
    • Gardner R.G., Nelson Z.W., Gottschling D.E. Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: distinct roles in telomeric silencing and general chromatin. Mol. Cell. Biol. 2005, 25:6123-6139.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6123-6139
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 59
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • Ng H.H., Xu R.M., Zhang Y., Struhl K. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J. Biol. Chem. 2002, 277:34655-34657.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 60
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z.W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 2002, 418:104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 61
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: triggering gene activity
    • Weake V.M., Workman J.L. Histone ubiquitination: triggering gene activity. Mol. Cell 2008, 29:653-663.
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 62
    • 63049135667 scopus 로고    scopus 로고
    • The role of RAD6 in recombinational repair, checkpoints and meiosis via histone modification
    • Game J.C., Chernikova S.B. The role of RAD6 in recombinational repair, checkpoints and meiosis via histone modification. DNA Repair (Amst) 2009, 8:470-482.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 470-482
    • Game, J.C.1    Chernikova, S.B.2
  • 64
    • 77953400995 scopus 로고    scopus 로고
    • Histone H2B C-terminal helix mediates trans-histone H3K4 methylation independent of H2B ubiquitination
    • Chandrasekharan M.B., Huang F., Chen Y.-C., Sun Z.-W. Histone H2B C-terminal helix mediates trans-histone H3K4 methylation independent of H2B ubiquitination. Mol. Cell. Biol. 2010, 30:3216-3232.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3216-3232
    • Chandrasekharan, M.B.1    Huang, F.2    Chen, Y.-C.3    Sun, Z.-W.4
  • 68
    • 77954382325 scopus 로고    scopus 로고
    • Novel Functional Residues in the Core Domain of Histone H2B Regulate Yeast Gene Expression and Silencing and Affect the Response to DNA Damage
    • Kyriss M.N.M., Jin Y., Gallegos I.J., Sanford J.A., Wyrick J.J. Novel Functional Residues in the Core Domain of Histone H2B Regulate Yeast Gene Expression and Silencing and Affect the Response to DNA Damage. Mol. Cell. Biol. 2010, 30:3503-3518.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3503-3518
    • Kyriss, M.N.M.1    Jin, Y.2    Gallegos, I.J.3    Sanford, J.A.4    Wyrick, J.J.5
  • 69
    • 78951489353 scopus 로고    scopus 로고
    • Yin and Yang of histone H2B roles in silencing and longevity: a tale of two arginines
    • Dai J., Hyland E.M., Norris A., Boeke J.D. Yin and Yang of histone H2B roles in silencing and longevity: a tale of two arginines. Genetics 2010, 186:813-828.
    • (2010) Genetics , vol.186 , pp. 813-828
    • Dai, J.1    Hyland, E.M.2    Norris, A.3    Boeke, J.D.4
  • 70
    • 79953312638 scopus 로고    scopus 로고
    • A common telomeric gene silencing assay is affected by nucleotide metabolism
    • Rossmann M.P., Luo W., Tsaponina O., Chabes A., Stillman B. A common telomeric gene silencing assay is affected by nucleotide metabolism. Mol. Cell 2011, 42:127-136.
    • (2011) Mol. Cell , vol.42 , pp. 127-136
    • Rossmann, M.P.1    Luo, W.2    Tsaponina, O.3    Chabes, A.4    Stillman, B.5
  • 72
    • 58149165025 scopus 로고    scopus 로고
    • Compensatory interactions between Sir3p and the nucleosomal LRS surface imply their direct interaction
    • Norris A., Bianchet M.A., Boeke J.D. Compensatory interactions between Sir3p and the nucleosomal LRS surface imply their direct interaction. PLoS Genet. 2008, 4:e1000301.
    • (2008) PLoS Genet. , vol.4
    • Norris, A.1    Bianchet, M.A.2    Boeke, J.D.3
  • 73
    • 66349093144 scopus 로고    scopus 로고
    • Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes
    • Sampath V., Yuan P., Wang I.X., Prugar E., van Leeuwen F., Sternglanz R. Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes. Mol. Cell. Biol. 2009, 29:2532-2545.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2532-2545
    • Sampath, V.1    Yuan, P.2    Wang, I.X.3    Prugar, E.4    van Leeuwen, F.5    Sternglanz, R.6
  • 74
    • 37349033583 scopus 로고    scopus 로고
    • Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly
    • Onishi M., Liou G.G., Buchberger J.R., Walz T., Moazed D. Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly. Mol. Cell 2007, 28:1015-1028.
    • (2007) Mol. Cell , vol.28 , pp. 1015-1028
    • Onishi, M.1    Liou, G.G.2    Buchberger, J.R.3    Walz, T.4    Moazed, D.5
  • 76
    • 0034046081 scopus 로고    scopus 로고
    • Two classes of sir3 mutants enhance the sir1 mutant mating defect and abolish telomeric silencing in Saccharomyces cerevisiae
    • Stone E.M., Reifsnyder C., McVey M., Gazo B., Pillus L. Two classes of sir3 mutants enhance the sir1 mutant mating defect and abolish telomeric silencing in Saccharomyces cerevisiae. Genetics 2000, 155:509-522.
    • (2000) Genetics , vol.155 , pp. 509-522
    • Stone, E.M.1    Reifsnyder, C.2    McVey, M.3    Gazo, B.4    Pillus, L.5
  • 78
    • 33646123085 scopus 로고    scopus 로고
    • Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S cerevisiae at 1.95 A resolution
    • Hou Z., Danzer J.R., Fox C.A., Keck J.L. Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S cerevisiae at 1.95 A resolution. Protein Sci. 2006, 15:1182-1186.
    • (2006) Protein Sci. , vol.15 , pp. 1182-1186
    • Hou, Z.1    Danzer, J.R.2    Fox, C.A.3    Keck, J.L.4
  • 80
    • 35649016107 scopus 로고    scopus 로고
    • Regulation of gene transcription by the histone H2A N-terminal domain
    • Parra M.A., Wyrick J.J. Regulation of gene transcription by the histone H2A N-terminal domain. Mol. Cell. Biol. 2007, 27:7641-7648.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7641-7648
    • Parra, M.A.1    Wyrick, J.J.2
  • 81
    • 59349107969 scopus 로고    scopus 로고
    • The role of histone H2A and H2B post-translational modifications in transcription: a genomic perspective
    • Wyrick J.J., Parra M.A. The role of histone H2A and H2B post-translational modifications in transcription: a genomic perspective. Biochim. Biophys. Acta 2009, 1789:37-44.
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 37-44
    • Wyrick, J.J.1    Parra, M.A.2
  • 82
    • 77954371390 scopus 로고    scopus 로고
    • Novel trans-tail regulation of H2B ubiquitylation and H3K4 methylation by the N terminus of histone H2A
    • Zheng S., Wyrick J.J., Reese J.C. Novel trans-tail regulation of H2B ubiquitylation and H3K4 methylation by the N terminus of histone H2A. Mol. Cell. Biol. 2010, 30:3635-3645.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3635-3645
    • Zheng, S.1    Wyrick, J.J.2    Reese, J.C.3
  • 83
    • 0042818412 scopus 로고    scopus 로고
    • The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p
    • Wood A., Schneider J., Dover J., Johnston M., Shilatifard A. The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J. Biol. Chem. 2003, 278:34739-34742.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34739-34742
    • Wood, A.1    Schneider, J.2    Dover, J.3    Johnston, M.4    Shilatifard, A.5
  • 84
    • 0942290540 scopus 로고    scopus 로고
    • Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B
    • Kao C.F., Hillyer C., Tsukuda T., Henry K., Berger S., Osley M.A. Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B. Genes Dev. 2004, 18:184-195.
    • (2004) Genes Dev. , vol.18 , pp. 184-195
    • Kao, C.F.1    Hillyer, C.2    Tsukuda, T.3    Henry, K.4    Berger, S.5    Osley, M.A.6
  • 86
    • 79959549133 scopus 로고    scopus 로고
    • Condensin association with histone H2A shapes mitotic chromosomes
    • Tada K., Susumu H., Sakuno T., Watanabe Y. Condensin association with histone H2A shapes mitotic chromosomes. Nature 2011, 474:477-483.
    • (2011) Nature , vol.474 , pp. 477-483
    • Tada, K.1    Susumu, H.2    Sakuno, T.3    Watanabe, Y.4
  • 87
    • 22244481613 scopus 로고    scopus 로고
    • The structure and function of SMC and kleisin complexes
    • Nasmyth K., Haering C.H. The structure and function of SMC and kleisin complexes. Annu. Rev. Biochem. 2005, 74:595-648.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 595-648
    • Nasmyth, K.1    Haering, C.H.2
  • 89
    • 0029739422 scopus 로고    scopus 로고
    • All four core histone N-termini contain sequences required for the repression of basal transcription in yeast
    • Lenfant F., Mann R.K., Thomsen B., Ling X., Grunstein M. All four core histone N-termini contain sequences required for the repression of basal transcription in yeast. EMBO J. 1996, 15:3974-3985.
    • (1996) EMBO J. , vol.15 , pp. 3974-3985
    • Lenfant, F.1    Mann, R.K.2    Thomsen, B.3    Ling, X.4    Grunstein, M.5
  • 90
    • 33646580356 scopus 로고    scopus 로고
    • Deciphering the roles of the histone H2B N-terminal domain in genome-wide transcription
    • Parra M.A., Kerr D., Fahy D., Pouchnik D.J., Wyrick J.J. Deciphering the roles of the histone H2B N-terminal domain in genome-wide transcription. Mol. Cell. Biol. 2006, 26:3842-3852.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3842-3852
    • Parra, M.A.1    Kerr, D.2    Fahy, D.3    Pouchnik, D.J.4    Wyrick, J.J.5
  • 91
    • 77950513764 scopus 로고    scopus 로고
    • A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast
    • Nag R., Kyriss M., Smerdon J.W., Wyrick J.J., Smerdon M.J. A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast. Nucleic Acids Res. 2010, 38:1450-1460.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1450-1460
    • Nag, R.1    Kyriss, M.2    Smerdon, J.W.3    Wyrick, J.J.4    Smerdon, M.J.5
  • 92
    • 79959864524 scopus 로고    scopus 로고
    • The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation
    • Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y. The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation. Mol. Cell 2011, 43:132-144.
    • (2011) Mol. Cell , vol.43 , pp. 132-144
    • Wu, L.1    Zee, B.M.2    Wang, Y.3    Garcia, B.A.4    Dou, Y.5
  • 93
    • 70449426592 scopus 로고    scopus 로고
    • Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain
    • Tweedie-Cullen R.Y., Reck J.M., Mansuy I.M. Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain. J. Proteome Res. 2009, 8:4966-4982.
    • (2009) J. Proteome Res. , vol.8 , pp. 4966-4982
    • Tweedie-Cullen, R.Y.1    Reck, J.M.2    Mansuy, I.M.3
  • 94
    • 79251551440 scopus 로고    scopus 로고
    • Identification of lysine 37 of histone H2B as a novel site of methylation
    • Gardner K.E., Zhou L., Parra M.A., Chen X., Strahl B.D. Identification of lysine 37 of histone H2B as a novel site of methylation. PLoS One 2011, 6:e16244.
    • (2011) PLoS One , vol.6
    • Gardner, K.E.1    Zhou, L.2    Parra, M.A.3    Chen, X.4    Strahl, B.D.5
  • 97
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
    • Hardie D.G. AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nat. Rev. Mol. Cell Biol. 2007, 8:774-785.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 774-785
    • Hardie, D.G.1
  • 98
    • 77956269315 scopus 로고    scopus 로고
    • Targeting the Core of Transcription
    • Hardie D.G. Targeting the Core of Transcription. Science 2010, 329:1158-1159.
    • (2010) Science , vol.329 , pp. 1158-1159
    • Hardie, D.G.1
  • 99
    • 78650447665 scopus 로고    scopus 로고
    • β-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • Sakabe K., Wang Z., Hart G.W. β-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:19915-19920.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 100
    • 77951884380 scopus 로고    scopus 로고
    • RCC1 uses a conformationally diverse loop region to interact with the nucleosome: a model for the RCC1-nucleosome complex
    • England J.R., Huang J., Jennings M.J., Makde R.D., Tan S. RCC1 uses a conformationally diverse loop region to interact with the nucleosome: a model for the RCC1-nucleosome complex. J. Mol. Biol. 2010, 398:518-529.
    • (2010) J. Mol. Biol. , vol.398 , pp. 518-529
    • England, J.R.1    Huang, J.2    Jennings, M.J.3    Makde, R.D.4    Tan, S.5
  • 101
    • 59649087503 scopus 로고    scopus 로고
    • Intrinsic disorder explains diverse nuclear roles of chromatin remodeling proteins
    • Sandhu K.S. Intrinsic disorder explains diverse nuclear roles of chromatin remodeling proteins. J. Mol. Recognit. 2009, 22:1-8.
    • (2009) J. Mol. Recognit. , vol.22 , pp. 1-8
    • Sandhu, K.S.1
  • 102
    • 7244240818 scopus 로고    scopus 로고
    • POLYVIEW: a flexible visualization tool for structural and functional annotations of proteins
    • Porollo A.A., Adamczak R., Meller J. POLYVIEW: a flexible visualization tool for structural and functional annotations of proteins. Bioinformatics 2004, 20:2460-2462.
    • (2004) Bioinformatics , vol.20 , pp. 2460-2462
    • Porollo, A.A.1    Adamczak, R.2    Meller, J.3
  • 103
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White C.L., Suto R.K., Luger K. Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J. 2001, 20:5207-5218.
    • (2001) EMBO J. , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.