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Volumn 7, Issue 3, 2011, Pages

H3 lysine 4 is acetylated at active gene promoters and is regulated by H3 lysine 4 methylation

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE GCN5; HISTONE ACETYLTRANSFERASE RTT109; HISTONE DEACETYLASE 1; HISTONE H3; LYSINE; SIRTUIN 2; UNCLASSIFIED DRUG; GCN5 PROTEIN, S CEREVISIAE; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; HST1 PROTEIN, S CEREVISIAE; RTT109 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SET1 PROTEIN, S CEREVISIAE; SILENT INFORMATION REGULATOR PROTEIN; SIR2 PROTEIN, S CEREVISIAE;

EID: 79953760389     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1001354     Document Type: Article
Times cited : (160)

References (108)
  • 1
    • 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
  • 2
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun ZW, Allis CD, (2002) Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418: 104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 3
    • 0037047323 scopus 로고    scopus 로고
    • Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6
    • Dover J, Schneider J, Tawiah-Boateng MA, Wood A, Dean K, et al. (2002) Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6. J Biol Chem 277: 28368-28371.
    • (2002) J Biol Chem , vol.277 , pp. 28368-28371
    • Dover, J.1    Schneider, J.2    Tawiah-Boateng, M.A.3    Wood, A.4    Dean, K.5
  • 4
    • 28844477653 scopus 로고    scopus 로고
    • Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation
    • Fischle W, Tseng BS, Dormann HL, Ueberheide BM, Garcia BA, et al. (2005) Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature 438: 1116-1122.
    • (2005) Nature , vol.438 , pp. 1116-1122
    • Fischle, W.1    Tseng, B.S.2    Dormann, H.L.3    Ueberheide, B.M.4    Garcia, B.A.5
  • 5
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD, (2001) Translating the histone code. Science 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 6
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner BM, (2002) Cellular memory and the histone code. Cell 111: 285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 7
    • 34548329850 scopus 로고    scopus 로고
    • Functional proteomics in histone research and epigenetics
    • Trelle MB, Jensen ON, (2007) Functional proteomics in histone research and epigenetics. Expert Rev Proteomics 4: 491-503.
    • (2007) Expert Rev Proteomics , vol.4 , pp. 491-503
    • Trelle, M.B.1    Jensen, O.N.2
  • 8
    • 58149151517 scopus 로고    scopus 로고
    • Unraveling the histone's potential: a proteomics perspective
    • Brumbaugh J, Phanstiel D, Coon JJ, (2008) Unraveling the histone's potential: a proteomics perspective. Epigenetics 3: 254-257.
    • (2008) Epigenetics , vol.3 , pp. 254-257
    • Brumbaugh, J.1    Phanstiel, D.2    Coon, J.J.3
  • 9
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone post-translational modifications by peptide mass fingerprinting
    • Zhang L, Eugeni EE, Parthun MR, Freitas MA, (2003) Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 112: 77-86.
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 10
    • 44649139771 scopus 로고    scopus 로고
    • Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation
    • Shilatifard A, (2008) Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation. Curr Opin Cell Biol 20: 341-348.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 341-348
    • Shilatifard, A.1
  • 11
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark
    • Ruthenburg AJ, Allis CD, Wysocka J, (2007) Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Mol Cell 25: 15-30.
    • (2007) Mol Cell , vol.25 , pp. 15-30
    • Ruthenburg, A.J.1    Allis, C.D.2    Wysocka, J.3
  • 13
    • 0033592999 scopus 로고    scopus 로고
    • Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena
    • Strahl BD, Ohba R, Cook RG, Allis CD, (1999) Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena. Proc Natl Acad Sci U S A 96: 14967-14972.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14967-14972
    • Strahl, B.D.1    Ohba, R.2    Cook, R.G.3    Allis, C.D.4
  • 15
    • 2642570305 scopus 로고    scopus 로고
    • The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
    • Schubeler D, MacAlpine DM, Scalzo D, Wirbelauer C, Kooperberg C, et al. (2004) The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev 18: 1263-1271.
    • (2004) Genes Dev , vol.18 , pp. 1263-1271
    • Schubeler, D.1    MacAlpine, D.M.2    Scalzo, D.3    Wirbelauer, C.4    Kooperberg, C.5
  • 17
    • 34447098370 scopus 로고    scopus 로고
    • A chromatin landmark and transcription initiation at most promoters in human cells
    • Guenther MG, Levine SS, Boyer LA, Jaenisch R, Young RA, (2007) A chromatin landmark and transcription initiation at most promoters in human cells. Cell 130: 77-88.
    • (2007) Cell , vol.130 , pp. 77-88
    • Guenther, M.G.1    Levine, S.S.2    Boyer, L.A.3    Jaenisch, R.4    Young, R.A.5
  • 18
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng HH, Robert F, Young RA, Struhl K, (2003) Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol Cell 11: 709-719.
    • (2003) Mol Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 19
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profiling of histone methylations in the human genome
    • Barski A, Cuddapah S, Cui K, Roh TY, Schones DE, et al. (2007) High-resolution profiling of histone methylations in the human genome. Cell 129: 823-837.
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1    Cuddapah, S.2    Cui, K.3    Roh, T.Y.4    Schones, D.E.5
  • 20
    • 23944462969 scopus 로고    scopus 로고
    • Genome-wide Map of Nucleosome Acetylation and Methylation in Yeast
    • Pokholok DK, Harbison CT, Levine S, Cole M, Hannett NM, et al. (2005) Genome-wide Map of Nucleosome Acetylation and Methylation in Yeast. Cell 122: 517-527.
    • (2005) Cell , vol.122 , pp. 517-527
    • Pokholok, D.K.1    Harbison, C.T.2    Levine, S.3    Cole, M.4    Hannett, N.M.5
  • 21
    • 26444508841 scopus 로고    scopus 로고
    • Single-Nucleosome Mapping of Histone Modifications in S. cerevisiae
    • doi:10.1371/journal.pbio.0030328
    • Liu CL, Kaplan T, Kim M, Buratowski S, Schreiber SL, et al. (2005) Single-Nucleosome Mapping of Histone Modifications in S. cerevisiae. PLoS Biol 3: e328 doi:10.1371/journal.pbio.0030328.
    • (2005) PLoS Biol , vol.3 , pp. 328
    • Liu, C.L.1    Kaplan, T.2    Kim, M.3    Buratowski, S.4    Schreiber, S.L.5
  • 22
    • 67650091251 scopus 로고    scopus 로고
    • Genome-wide analysis of mono-, di- and trimethylation of histone H3 lysine 4 in Arabidopsis thaliana
    • Zhang X, Bernatavichute YV, Cokus S, Pellegrini M, Jacobsen SE, (2009) Genome-wide analysis of mono-, di- and trimethylation of histone H3 lysine 4 in Arabidopsis thaliana. Genome Biol 10: R62.
    • (2009) Genome Biol , vol.10 , pp. 62
    • Zhang, X.1    Bernatavichute, Y.V.2    Cokus, S.3    Pellegrini, M.4    Jacobsen, S.E.5
  • 23
    • 29244460109 scopus 로고    scopus 로고
    • Double chromodomains cooperate to recognize the methylated histone H3 tail
    • Flanagan JF, Mi LZ, Chruszcz M, Cymborowski M, Clines KL, et al. (2005) Double chromodomains cooperate to recognize the methylated histone H3 tail. Nature 438: 1181-1185.
    • (2005) Nature , vol.438 , pp. 1181-1185
    • Flanagan, J.F.1    Mi, L.Z.2    Chruszcz, M.3    Cymborowski, M.4    Clines, K.L.5
  • 24
    • 33745839365 scopus 로고    scopus 로고
    • A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
    • Wysocka J, Swigut T, Xiao H, Milne TA, Kwon SY, et al. (2006) A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 442: 86-90.
    • (2006) Nature , vol.442 , pp. 86-90
    • Wysocka, J.1    Swigut, T.2    Xiao, H.3    Milne, T.A.4    Kwon, S.Y.5
  • 25
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • Li H, Ilin S, Wang W, Duncan EM, Wysocka J, et al. (2006) Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442: 91-95.
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5
  • 26
    • 33745868054 scopus 로고    scopus 로고
    • ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
    • Shi X, Hong T, Walter KL, Ewalt M, Michishita E, et al. (2006) ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442: 96-99.
    • (2006) Nature , vol.442 , pp. 96-99
    • Shi, X.1    Hong, T.2    Walter, K.L.3    Ewalt, M.4    Michishita, E.5
  • 27
    • 33750328340 scopus 로고    scopus 로고
    • The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3
    • Martin DG, Baetz K, Shi X, Walter KL, MacDonald VE, et al. (2006) The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Mol Cell Biol 26: 7871-7879.
    • (2006) Mol Cell Biol , vol.26 , pp. 7871-7879
    • Martin, D.G.1    Baetz, K.2    Shi, X.3    Walter, K.L.4    MacDonald, V.E.5
  • 28
    • 34047248383 scopus 로고    scopus 로고
    • Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36
    • Shi X, Kachirskaia I, Walter KL, Kuo JH, Lake A, et al. (2007) Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36. J Biol Chem 282: 2450-2455.
    • (2007) J Biol Chem , vol.282 , pp. 2450-2455
    • Shi, X.1    Kachirskaia, I.2    Walter, K.L.3    Kuo, J.H.4    Lake, A.5
  • 29
    • 34547793043 scopus 로고    scopus 로고
    • Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression
    • Lan F, Collins RE, De Cegli R, Alpatov R, Horton JR, et al. (2007) Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression. Nature 448: 718-722.
    • (2007) Nature , vol.448 , pp. 718-722
    • Lan, F.1    Collins, R.E.2    de Cegli, R.3    Alpatov, R.4    Horton, J.R.5
  • 30
    • 37249041657 scopus 로고    scopus 로고
    • RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J recombination
    • Matthews AG, Kuo AJ, Ramon-Maiques S, Han S, Champagne KS, et al. (2007) RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J recombination. Nature 450: 1106-1110.
    • (2007) Nature , vol.450 , pp. 1106-1110
    • Matthews, A.G.1    Kuo, A.J.2    Ramon-Maiques, S.3    Han, S.4    Champagne, K.S.5
  • 31
    • 34848911602 scopus 로고    scopus 로고
    • Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4
    • Vermeulen M, Mulder KW, Denissov S, Pijnappel WW, van Schaik FM, et al. (2007) Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4. Cell 131: 58-69.
    • (2007) Cell , vol.131 , pp. 58-69
    • Vermeulen, M.1    Mulder, K.W.2    Denissov, S.3    Pijnappel, W.W.4    van Schaik, F.M.5
  • 32
    • 36249027156 scopus 로고    scopus 로고
    • Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing
    • Sims RJ 3rd, Millhouse S, Chen CF, Lewis BA, Erdjument-Bromage H, et al. (2007) Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. Mol Cell 28: 665-676.
    • (2007) Mol Cell , vol.28 , pp. 665-676
    • Sims III, R.J.1    Millhouse, S.2    Chen, C.F.3    Lewis, B.A.4    Erdjument-Bromage, H.5
  • 33
    • 33751527233 scopus 로고    scopus 로고
    • Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
    • Taverna SD, Ilin S, Rogers RS, Tanny JC, Lavender H, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24: 785-796.
    • (2006) Mol Cell , vol.24 , pp. 785-796
    • Taverna, S.D.1    Ilin, S.2    Rogers, R.S.3    Tanny, J.C.4    Lavender, H.5
  • 34
    • 34547725157 scopus 로고    scopus 로고
    • DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
    • Ooi SK, Qiu C, Bernstein E, Li K, Jia D, et al. (2007) DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA. Nature 448: 714-717.
    • (2007) Nature , vol.448 , pp. 714-717
    • Ooi, S.K.1    Qiu, C.2    Bernstein, E.3    Li, K.4    Jia, D.5
  • 35
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM, (2006) Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312: 748-751.
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 36
    • 33745818717 scopus 로고    scopus 로고
    • Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
    • Pena PV, Davrazou F, Shi X, Walter KL, Verkhusha VV, et al. (2006) Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 442: 100-103.
    • (2006) Nature , vol.442 , pp. 100-103
    • Pena, P.V.1    Davrazou, F.2    Shi, X.3    Walter, K.L.4    Verkhusha, V.V.5
  • 37
    • 0345708105 scopus 로고    scopus 로고
    • Methylation of histone H3 K4 mediates association of the Isw1p ATPase with chromatin
    • Santos-Rosa H, Schneider R, Bernstein BE, Karabetsou N, Morillon A, et al. (2003) Methylation of histone H3 K4 mediates association of the Isw1p ATPase with chromatin. Mol Cell 12: 1325-1332.
    • (2003) Mol Cell , vol.12 , pp. 1325-1332
    • Santos-Rosa, H.1    Schneider, R.2    Bernstein, B.E.3    Karabetsou, N.4    Morillon, A.5
  • 38
    • 0037126594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4
    • Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, et al. (2001) The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. Embo J 20: 7137-7148.
    • (2001) Embo J , vol.20 , pp. 7137-7148
    • Roguev, A.1    Schaft, D.2    Shevchenko, A.3    Pijnappel, W.W.4    Wilm, M.5
  • 39
    • 0037192780 scopus 로고    scopus 로고
    • COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression
    • Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, et al. (2002) COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem 277: 10753-10755.
    • (2002) J Biol Chem , vol.277 , pp. 10753-10755
    • Krogan, N.J.1    Dover, J.2    Khorrami, S.3    Greenblatt, J.F.4    Schneider, J.5
  • 41
    • 0035893240 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae
    • Briggs SD, Bryk M, Strahl BD, Cheung WL, Davie JK, et al. (2001) Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev 15: 3286-3295.
    • (2001) Genes Dev , vol.15 , pp. 3286-3295
    • Briggs, S.D.1    Bryk, M.2    Strahl, B.D.3    Cheung, W.L.4    Davie, J.K.5
  • 42
    • 0037039309 scopus 로고    scopus 로고
    • A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3
    • Nagy PL, Griesenbeck J, Kornberg RD, Cleary ML, (2002) A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3. Proc Natl Acad Sci U S A 99: 90-94.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 90-94
    • Nagy, P.L.1    Griesenbeck, J.2    Kornberg, R.D.3    Cleary, M.L.4
  • 43
    • 55549101555 scopus 로고    scopus 로고
    • Ubiquitylation of the COMPASS component Swd2 links H2B ubiquitylation to H3K4 trimethylation
    • Vitaliano-Prunier A, Menant A, Hobeika M, Geli V, Gwizdek C, et al. (2008) Ubiquitylation of the COMPASS component Swd2 links H2B ubiquitylation to H3K4 trimethylation. Nat Cell Biol 10: 1365-1371.
    • (2008) Nat Cell Biol , vol.10 , pp. 1365-1371
    • Vitaliano-Prunier, A.1    Menant, A.2    Hobeika, M.3    Geli, V.4    Gwizdek, C.5
  • 44
    • 33750698262 scopus 로고    scopus 로고
    • The multiple faces of Set1
    • Dehe PM, Geli V, (2006) The multiple faces of Set1. Biochem Cell Biol 84: 536-548.
    • (2006) Biochem Cell Biol , vol.84 , pp. 536-548
    • Dehe, P.M.1    Geli, V.2
  • 45
    • 34948821302 scopus 로고    scopus 로고
    • Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail
    • Jiang L, Smith JN, Anderson SL, Ma P, Mizzen CA, et al. (2007) Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail. J Biol Chem 282: 27923-27934.
    • (2007) J Biol Chem , vol.282 , pp. 27923-27934
    • Jiang, L.1    Smith, J.N.2    Anderson, S.L.3    Ma, P.4    Mizzen, C.A.5
  • 46
    • 10644260359 scopus 로고    scopus 로고
    • A mass spectrometric "Western blot" to evaluate the correlations between histone methylation and histone acetylation
    • Zhang K, Siino JS, Jones PR, Yau PM, Bradbury EM, (2004) A mass spectrometric "Western blot" to evaluate the correlations between histone methylation and histone acetylation. Proteomics 4: 3765-3775.
    • (2004) Proteomics , vol.4 , pp. 3765-3775
    • Zhang, K.1    Siino, J.S.2    Jones, P.R.3    Yau, P.M.4    Bradbury, E.M.5
  • 47
    • 33947492804 scopus 로고    scopus 로고
    • Cross-talk between histone modifications in response to histone deacetylase inhibitors: MLL4 links histone H3 acetylation and histone H3K4 methylation
    • Nightingale KP, Gendreizig S, White DA, Bradbury C, Hollfelder F, et al. (2007) Cross-talk between histone modifications in response to histone deacetylase inhibitors: MLL4 links histone H3 acetylation and histone H3K4 methylation. J Biol Chem 282: 4408-4416.
    • (2007) J Biol Chem , vol.282 , pp. 4408-4416
    • Nightingale, K.P.1    Gendreizig, S.2    White, D.A.3    Bradbury, C.4    Hollfelder, F.5
  • 49
    • 29144463657 scopus 로고    scopus 로고
    • Dynamic acetylation of all lysine 4-methylated histone H3 in the mouse nucleus: analysis at c-fos and c-jun
    • doi:10.1371/journal.pbio.0030393
    • Hazzalin CA, Mahadevan LC, (2005) Dynamic acetylation of all lysine 4-methylated histone H3 in the mouse nucleus: analysis at c-fos and c-jun. PLoS Biol 3: e393 doi:10.1371/journal.pbio.0030393.
    • (2005) PLoS Biol , vol.3 , pp. 393
    • Hazzalin, C.A.1    Mahadevan, L.C.2
  • 50
    • 64249111489 scopus 로고    scopus 로고
    • Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5′ transcribed regions
    • Kim T, Buratowski S, (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
  • 51
    • 46249112085 scopus 로고    scopus 로고
    • Combinatorial patterns of histone acetylations and methylations in the human genome
    • Wang Z, Zang C, Rosenfeld JA, Schones DE, Barski A, et al. (2008) Combinatorial patterns of histone acetylations and methylations in the human genome. Nat Genet 40: 897-903.
    • (2008) Nat Genet , vol.40 , pp. 897-903
    • Wang, Z.1    Zang, C.2    Rosenfeld, J.A.3    Schones, D.E.4    Barski, A.5
  • 52
    • 34147177521 scopus 로고    scopus 로고
    • Organismal differences in post-translational modifications in histones H3 and H4
    • Garcia BA, Hake SB, Diaz RL, Kauer M, Morris SA, et al. (2007) Organismal differences in post-translational modifications in histones H3 and H4. J Biol Chem 282: 7641-7655.
    • (2007) J Biol Chem , vol.282 , pp. 7641-7655
    • Garcia, B.A.1    Hake, S.B.2    Diaz, R.L.3    Kauer, M.4    Morris, S.A.5
  • 53
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • Suka N, Suka Y, Carmen AA, Wu J, Grunstein M, (2001) Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol Cell 8: 473-479.
    • (2001) Mol Cell , vol.8 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3    Wu, J.4    Grunstein, M.5
  • 54
    • 46149100263 scopus 로고    scopus 로고
    • Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109
    • Fillingham J, Recht J, Silva AC, Suter B, Emili A, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28: 4342-4353.
    • (2008) Mol Cell Biol , vol.28 , pp. 4342-4353
    • Fillingham, J.1    Recht, J.2    Silva, A.C.3    Suter, B.4    Emili, A.5
  • 55
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • Rusche LN, Kirchmaier AL, Rine J, (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
  • 56
    • 6344270167 scopus 로고    scopus 로고
    • Global position and recruitment of HATs and HDACs in the yeast genome
    • Robert F, Pokholok DK, Hannett NM, Rinaldi NJ, Chandy M, et al. (2004) Global position and recruitment of HATs and HDACs in the yeast genome. Mol Cell 16: 199-209.
    • (2004) Mol Cell , vol.16 , pp. 199-209
    • Robert, F.1    Pokholok, D.K.2    Hannett, N.M.3    Rinaldi, N.J.4    Chandy, M.5
  • 57
    • 34548457748 scopus 로고    scopus 로고
    • Substitution as a mechanism for genetic robustness: the duplicated deacetylases Hst1p and Sir2p in Saccharomyces cerevisiae
    • doi:10.1371/journal.pgen.0030126
    • Hickman MA, Rusche LN, (2007) Substitution as a mechanism for genetic robustness: the duplicated deacetylases Hst1p and Sir2p in Saccharomyces cerevisiae. PLoS Genet 3: e126 doi:10.1371/journal.pgen.0030126.
    • (2007) PLoS Genet , vol.3 , pp. 126
    • Hickman, M.A.1    Rusche, L.N.2
  • 60
    • 35348986412 scopus 로고    scopus 로고
    • Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation
    • Kirmizis A, Santos-Rosa H, Penkett CJ, Singer MA, Vermeulen M, et al. (2007) Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation. Nature 449: 928-932.
    • (2007) Nature , vol.449 , pp. 928-932
    • Kirmizis, A.1    Santos-Rosa, H.2    Penkett, C.J.3    Singer, M.A.4    Vermeulen, M.5
  • 61
    • 33845935260 scopus 로고    scopus 로고
    • Protein interactions within the Set1 complex and their roles in the regulation of histone 3 lysine 4 methylation
    • Dehe PM, Dichtl B, Schaft D, Roguev A, Pamblanco M, et al. (2006) Protein interactions within the Set1 complex and their roles in the regulation of histone 3 lysine 4 methylation. J Biol Chem 281: 35404-35412.
    • (2006) J Biol Chem , vol.281 , pp. 35404-35412
    • Dehe, P.M.1    Dichtl, B.2    Schaft, D.3    Roguev, A.4    Pamblanco, M.5
  • 62
    • 24944520025 scopus 로고    scopus 로고
    • Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression
    • Schneider J, Wood A, Lee JS, Schuster R, Dueker J, et al. (2005) Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression. Mol Cell 19: 849-856.
    • (2005) Mol Cell , vol.19 , pp. 849-856
    • Schneider, J.1    Wood, A.2    Lee, J.S.3    Schuster, R.4    Dueker, J.5
  • 63
    • 20444375490 scopus 로고    scopus 로고
    • Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription
    • Morillon A, Karabetsou N, Nair A, Mellor J, (2005) Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription. Mol Cell 18: 723-734.
    • (2005) Mol Cell , vol.18 , pp. 723-734
    • Morillon, A.1    Karabetsou, N.2    Nair, A.3    Mellor, J.4
  • 64
    • 59549104788 scopus 로고    scopus 로고
    • Flocculation in Saccharomyces cerevisiae is repressed by the COMPASS methylation complex during high-gravity fermentation
    • Dietvorst J, Brandt A, (2008) Flocculation in Saccharomyces cerevisiae is repressed by the COMPASS methylation complex during high-gravity fermentation. Yeast 25: 891-901.
    • (2008) Yeast , vol.25 , pp. 891-901
    • Dietvorst, J.1    Brandt, A.2
  • 65
    • 4043122576 scopus 로고    scopus 로고
    • Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1-10
    • Carvin CD, Kladde MP, (2004) Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1-10. J Biol Chem 279: 33057-33062.
    • (2004) J Biol Chem , vol.279 , pp. 33057-33062
    • Carvin, C.D.1    Kladde, M.P.2
  • 66
    • 67649550089 scopus 로고    scopus 로고
    • H3 lysine 4 di- and tri-methylation deposited by cryptic transcription attenuates promoter activation
    • Pinskaya M, Gourvennec S, Morillon A, (2009) H3 lysine 4 di- and tri-methylation deposited by cryptic transcription attenuates promoter activation. Embo J 28: 1697-1707.
    • (2009) Embo J , vol.28 , pp. 1697-1707
    • Pinskaya, M.1    Gourvennec, S.2    Morillon, A.3
  • 67
    • 77950473704 scopus 로고    scopus 로고
    • A chromodomain switch mediated by histone H3 Lys 4 acetylation regulates heterochromatin assembly
    • Xhemalce B, Kouzarides T, (2010) A chromodomain switch mediated by histone H3 Lys 4 acetylation regulates heterochromatin assembly. Genes Dev 24: 647-652.
    • (2010) Genes Dev , vol.24 , pp. 647-652
    • Xhemalce, B.1    Kouzarides, T.2
  • 68
    • 34547879583 scopus 로고    scopus 로고
    • The SAGA continues: expanding the cellular role of a transcriptional co-activator complex
    • Baker SP, Grant PA, (2007) The SAGA continues: expanding the cellular role of a transcriptional co-activator complex. Oncogene 26: 5329-5340.
    • (2007) Oncogene , vol.26 , pp. 5329-5340
    • Baker, S.P.1    Grant, P.A.2
  • 69
    • 34547864553 scopus 로고    scopus 로고
    • Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation
    • Nagy Z, Tora L, (2007) Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation. Oncogene 26: 5341-5357.
    • (2007) Oncogene , vol.26 , pp. 5341-5357
    • Nagy, Z.1    Tora, L.2
  • 70
    • 0034707037 scopus 로고    scopus 로고
    • Global histone acetylation and deacetylation in yeast
    • Vogelauer M, Wu J, Suka N, Grunstein M, (2000) Global histone acetylation and deacetylation in yeast. Nature 408: 495-498.
    • (2000) Nature , vol.408 , pp. 495-498
    • Vogelauer, M.1    Wu, J.2    Suka, N.3    Grunstein, M.4
  • 71
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • Zhang W, Bone JR, Edmondson DG, Turner BM, Roth SY, (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.
    • (1998) Embo J , vol.17 , pp. 3155-3167
    • Zhang, W.1    Bone, J.R.2    Edmondson, D.G.3    Turner, B.M.4    Roth, S.Y.5
  • 72
    • 34147217542 scopus 로고    scopus 로고
    • Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map
    • Collins SR, Miller KM, Maas NL, Roguev A, Fillingham J, et al. (2007) Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446: 806-810.
    • (2007) Nature , vol.446 , pp. 806-810
    • Collins, S.R.1    Miller, K.M.2    Maas, N.L.3    Roguev, A.4    Fillingham, J.5
  • 73
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han J, Zhou H, Horazdovsky B, Zhang K, Xu RM, et al. (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
  • 74
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll R, Hudson A, Jackson SP, (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
  • 75
    • 33846023720 scopus 로고    scopus 로고
    • Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II
    • Schneider J, Bajwa P, Johnson FC, Bhaumik SR, Shilatifard A, (2006) Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II. J Biol Chem 281: 37270-37274.
    • (2006) J Biol Chem , vol.281 , pp. 37270-37274
    • Schneider, J.1    Bajwa, P.2    Johnson, F.C.3    Bhaumik, S.R.4    Shilatifard, A.5
  • 76
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    • Li Q, Zhou H, Wurtele H, Davies B, Horazdovsky B, et al. (2008) Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 134: 244-255.
    • (2008) Cell , vol.134 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5
  • 77
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen CC, Carson JJ, Feser J, Tamburini B, Zabaronick S, et al. (2008) Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 134: 231-243.
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5
  • 78
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto H, Hawke D, Kobayashi R, Verreault A, (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436: 294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 79
    • 79651474413 scopus 로고    scopus 로고
    • Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation
    • Tang Y, Holbert MA, Delgoshaie N, Wurtele H, Guillemette B, et al. (2011) Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation. Structure 19: 221-231.
    • (2011) Structure , vol.19 , pp. 221-231
    • Tang, Y.1    Holbert, M.A.2    Delgoshaie, N.3    Wurtele, H.4    Guillemette, B.5
  • 80
    • 76849084692 scopus 로고    scopus 로고
    • A role for Gcn5 in replication-coupled nucleosome assembly
    • Burgess RJ, Zhou H, Han J, Zhang Z, (2010) A role for Gcn5 in replication-coupled nucleosome assembly. Mol Cell 37: 469-480.
    • (2010) Mol Cell , vol.37 , pp. 469-480
    • Burgess, R.J.1    Zhou, H.2    Han, J.3    Zhang, Z.4
  • 81
    • 0031963197 scopus 로고    scopus 로고
    • The permease homologue Ssy1p controls the expression of amino acid and peptide transporter genes in Saccharomyces cerevisiae
    • Didion T, Regenberg B, Jorgensen MU, Kielland-Brandt MC, Andersen HA, (1998) The permease homologue Ssy1p controls the expression of amino acid and peptide transporter genes in Saccharomyces cerevisiae. Mol Microbiol 27: 643-650.
    • (1998) Mol Microbiol , vol.27 , pp. 643-650
    • Didion, T.1    Regenberg, B.2    Jorgensen, M.U.3    Kielland-Brandt, M.C.4    Andersen, H.A.5
  • 82
    • 0035142946 scopus 로고    scopus 로고
    • Transcriptional regulation of the Saccharomyces cerevisiae amino acid permease gene BAP2
    • Nielsen PS, van den Hazel B, Didion T, de Boer M, Jorgensen M, et al. (2001) Transcriptional regulation of the Saccharomyces cerevisiae amino acid permease gene BAP2. Mol Gen Genet 264: 613-622.
    • (2001) Mol Gen Genet , vol.264 , pp. 613-622
    • Nielsen, P.S.1    van den Hazel, B.2    Didion, T.3    de Boer, M.4    Jorgensen, M.5
  • 83
    • 0027959012 scopus 로고
    • Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake
    • Schmidt A, Hall MN, Koller A, (1994) Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake. Mol Cell Biol 14: 6597-6606.
    • (1994) Mol Cell Biol , vol.14 , pp. 6597-6606
    • Schmidt, A.1    Hall, M.N.2    Koller, A.3
  • 84
    • 0029785647 scopus 로고    scopus 로고
    • GNP1, the high-affinity glutamine permease of S. cerevisiae
    • Zhu X, Garrett J, Schreve J, Michaeli T, (1996) GNP1, the high-affinity glutamine permease of S. cerevisiae. Curr Genet 30: 107-114.
    • (1996) Curr Genet , vol.30 , pp. 107-114
    • Zhu, X.1    Garrett, J.2    Schreve, J.3    Michaeli, T.4
  • 85
    • 0035871393 scopus 로고    scopus 로고
    • Conversion of a gene-specific repressor to a regional silencer
    • Rusche LN, Rine J, (2001) Conversion of a gene-specific repressor to a regional silencer. Genes Dev 15: 955-967.
    • (2001) Genes Dev , vol.15 , pp. 955-967
    • Rusche, L.N.1    Rine, J.2
  • 86
    • 0037370393 scopus 로고    scopus 로고
    • Rfm1, a novel tethering factor required to recruit the Hst1 histone deacetylase for repression of middle sporulation genes
    • McCord R, Pierce M, Xie J, Wonkatal S, Mickel C, et al. (2003) Rfm1, a novel tethering factor required to recruit the Hst1 histone deacetylase for repression of middle sporulation genes. Mol Cell Biol 23: 2009-2016.
    • (2003) Mol Cell Biol , vol.23 , pp. 2009-2016
    • McCord, R.1    Pierce, M.2    Xie, J.3    Wonkatal, S.4    Mickel, C.5
  • 87
    • 0035890135 scopus 로고    scopus 로고
    • The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program
    • Pijnappel WW, Schaft D, Roguev A, Shevchenko A, Tekotte H, et al. (2001) The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program. Genes Dev 15: 2991-3004.
    • (2001) Genes Dev , vol.15 , pp. 2991-3004
    • Pijnappel, W.W.1    Schaft, D.2    Roguev, A.3    Shevchenko, A.4    Tekotte, H.5
  • 88
    • 0033570901 scopus 로고    scopus 로고
    • Sum1 and Hst1 repress middle sporulation-specific gene expression during mitosis in Saccharomyces cerevisiae
    • Xie J, Pierce M, Gailus-Durner V, Wagner M, Winter E, et al. (1999) Sum1 and Hst1 repress middle sporulation-specific gene expression during mitosis in Saccharomyces cerevisiae. Embo J 18: 6448-6454.
    • (1999) Embo J , vol.18 , pp. 6448-6454
    • Xie, J.1    Pierce, M.2    Gailus-Durner, V.3    Wagner, M.4    Winter, E.5
  • 89
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann CB, Sherman JM, Devine SE, Cameron EE, Pillus L, et al. (1995) The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev 9: 2888-2902.
    • (1995) Genes Dev , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5
  • 90
    • 0029893985 scopus 로고    scopus 로고
    • HST1, a new member of the SIR2 family of genes
    • Derbyshire MK, Weinstock KG, Strathern JN, (1996) HST1, a new member of the SIR2 family of genes. Yeast 12: 631-640.
    • (1996) Yeast , vol.12 , pp. 631-640
    • Derbyshire, M.K.1    Weinstock, K.G.2    Strathern, J.N.3
  • 91
    • 36749009061 scopus 로고    scopus 로고
    • Genome-wide, as opposed to local, antisilencing is mediated redundantly by the euchromatic factors Set1 and H2A.Z
    • Venkatasubrahmanyam S, Hwang WW, Meneghini MD, Tong AH, Madhani HD, (2007) Genome-wide, as opposed to local, antisilencing is mediated redundantly by the euchromatic factors Set1 and H2A.Z. Proc Natl Acad Sci U S A 104: 16609-16614.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16609-16614
    • Venkatasubrahmanyam, S.1    Hwang, W.W.2    Meneghini, M.D.3    Tong, A.H.4    Madhani, H.D.5
  • 92
    • 43049124410 scopus 로고    scopus 로고
    • An ARS element inhibits DNA replication through a SIR2-dependent mechanism
    • Crampton A, Chang F, Pappas DL Jr, Frisch RL, Weinreich M, (2008) An ARS element inhibits DNA replication through a SIR2-dependent mechanism. Mol Cell 30: 156-166.
    • (2008) Mol Cell , vol.30 , pp. 156-166
    • Crampton, A.1    Chang, F.2    Pappas Jr., D.L.3    Frisch, R.L.4    Weinreich, M.5
  • 93
    • 34147216783 scopus 로고    scopus 로고
    • Swapping the gene-specific and regional silencing specificities of the Hst1 and Sir2 histone deacetylases
    • Mead J, McCord R, Youngster L, Sharma M, Gartenberg MR, et al. (2007) Swapping the gene-specific and regional silencing specificities of the Hst1 and Sir2 histone deacetylases. Mol Cell Biol 27: 2466-2475.
    • (2007) Mol Cell Biol , vol.27 , pp. 2466-2475
    • Mead, J.1    McCord, R.2    Youngster, L.3    Sharma, M.4    Gartenberg, M.R.5
  • 94
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye RA, (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273: 793-798.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 95
    • 0036850346 scopus 로고    scopus 로고
    • Deciphering the transcriptional histone acetylation code for a human gene
    • Agalioti T, Chen G, Thanos D, (2002) Deciphering the transcriptional histone acetylation code for a human gene. Cell 111: 381-392.
    • (2002) Cell , vol.111 , pp. 381-392
    • Agalioti, T.1    Chen, G.2    Thanos, D.3
  • 96
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T, (2001) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410: 116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 97
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • Bannister AJ, Zegerman P, Partridge JF, Miska EA, Thomas JO, et al. (2001) Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410: 120-124.
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1    Zegerman, P.2    Partridge, J.F.3    Miska, E.A.4    Thomas, J.O.5
  • 98
    • 0038714132 scopus 로고    scopus 로고
    • Sir2 regulates histone H3 lysine 9 methylation and heterochromatin assembly in fission yeast
    • Shankaranarayana GD, Motamedi MR, Moazed D, Grewal SI, (2003) Sir2 regulates histone H3 lysine 9 methylation and heterochromatin assembly in fission yeast. Curr Biol 13: 1240-1246.
    • (2003) Curr Biol , vol.13 , pp. 1240-1246
    • Shankaranarayana, G.D.1    Motamedi, M.R.2    Moazed, D.3    Grewal, S.I.4
  • 99
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • Nakayama J, Rice JC, Strahl BD, Allis CD, Grewal SI, (2001) Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292: 110-113.
    • (2001) Science , vol.292 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.5
  • 100
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, et al. (2000) Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406: 593-599.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3    Strahl, B.D.4    Sun, Z.W.5
  • 101
    • 34147128561 scopus 로고    scopus 로고
    • Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification
    • Morris SA, Rao B, Garcia BA, Hake SB, Diaz RL, et al. (2007) Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification. J Biol Chem 282: 7632-7640.
    • (2007) J Biol Chem , vol.282 , pp. 7632-7640
    • Morris, S.A.1    Rao, B.2    Garcia, B.A.3    Hake, S.B.4    Diaz, R.L.5
  • 102
    • 69949085947 scopus 로고    scopus 로고
    • Histone H3 lysine 4 di-methylation: A novel mark for transcriptional fidelity?
    • Pinskaya M, Morillon A, (2009) Histone H3 lysine 4 di-methylation: A novel mark for transcriptional fidelity? Epigenetics 4.
    • (2009) Epigenetics , vol.4
    • Pinskaya, M.1    Morillon, A.2
  • 103
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov VV, (2000) Rapid and reliable protein extraction from yeast. Yeast 16: 857-860.
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 104
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4
    • Edmondson DG, Smith MM, Roth SY, (1996) Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4. Genes Dev 10: 1247-1259.
    • (1996) Genes Dev , vol.10 , pp. 1247-1259
    • Edmondson, D.G.1    Smith, M.M.2    Roth, S.Y.3
  • 105
    • 51549115454 scopus 로고    scopus 로고
    • Comprehensive profiling of histone modifications using a label-free approach and its applications in determining structure-function relationships
    • Drogaris P, Wurtele H, Masumoto H, Verreault A, Thibault P, (2008) Comprehensive profiling of histone modifications using a label-free approach and its applications in determining structure-function relationships. Anal Chem 80: 6698-6707.
    • (2008) Anal Chem , vol.80 , pp. 6698-6707
    • Drogaris, P.1    Wurtele, H.2    Masumoto, H.3    Verreault, A.4    Thibault, P.5
  • 106
    • 0036081355 scopus 로고    scopus 로고
    • Gene Expression Omnibus: NCBI gene expression and hybridization array data repository
    • Edgar R, Domrachev M, Lash AE, (2002) Gene Expression Omnibus: NCBI gene expression and hybridization array data repository. Nucleic Acids Res 30: 207-210.
    • (2002) Nucleic Acids Res , vol.30 , pp. 207-210
    • Edgar, R.1    Domrachev, M.2    Lash, A.E.3
  • 107
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt ME, Brown TA, Trumpower BL, (1990) A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res 18: 3091-3092.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 108
    • 28744458859 scopus 로고    scopus 로고
    • Bioconductor: open software development for computational biology and bioinformatics
    • Gentleman RC, Carey VJ, Bates DM, Bolstad B, Dettling M, et al. (2004) Bioconductor: open software development for computational biology and bioinformatics. Genome Biol 5: R80.
    • (2004) Genome Biol , vol.5 , pp. 80
    • Gentleman, R.C.1    Carey, V.J.2    Bates, D.M.3    Bolstad, B.4    Dettling, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.