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Volumn 7, Issue 10, 2008, Pages 1423-1432

SET8 plays a role in controlling G1/S transition by blocking lysine acetylation in histone through binding to H4 N-terminal tail

Author keywords

Cell cycle; DNA replication; Histone; Methyltransferase; SET8

Indexed keywords

HISTONE; HISTONE H4; LYSINE; METHYLTRANSFERASE; PROTEIN SET8; S PHASE KINASE ASSOCIATED PROTEIN 2; UBIQUITIN PROTEIN LIGASE;

EID: 45749114468     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.7.10.5867     Document Type: Article
Times cited : (53)

References (55)
  • 1
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001; 293:1074-80.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 2
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 1997; 389:349-52.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 3
    • 0038505671 scopus 로고    scopus 로고
    • Epigenomic replication: Linking epigenetics to DNA replication
    • McNairn AJ, Gilbert DM. Epigenomic replication: linking epigenetics to DNA replication. Bioessays 2003; 25:647-56.
    • (2003) Bioessays , vol.25 , pp. 647-656
    • McNairn, A.J.1    Gilbert, D.M.2
  • 4
    • 33646926758 scopus 로고    scopus 로고
    • Dynamic nucleosomes and gene transcription
    • Mellor J. Dynamic nucleosomes and gene transcription. Trends Genet 2006; 22:320-9.
    • (2006) Trends Genet , vol.22 , pp. 320-329
    • Mellor, J.1
  • 6
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000; 403:41-5.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 7
    • 0242348752 scopus 로고    scopus 로고
    • Histone lysine methylation: A signature for chromatin function
    • Sims RJ, 3rd, Nishioka K, Reinberg D. Histone lysine methylation: a signature for chromatin function. Trends Genet 2003; 19:629-39.
    • (2003) Trends Genet , vol.19 , pp. 629-639
    • Sims 3rd, R.J.1    Nishioka, K.2    Reinberg, D.3
  • 8
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev 2001; 15:2343-60.
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 9
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev 1998; 12:599-606.
    • (1998) Genes Dev , vol.12 , pp. 599-606
    • Struhl, K.1
  • 10
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo MH, Allis CD. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 1998; 20:615-26.
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 11
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner BM. Histone acetylation and an epigenetic code. Bioessays 2000; 22:836-45.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 12
    • 2942519726 scopus 로고    scopus 로고
    • Structures of protein domains that create or recognize histone modifications
    • Bottomley MJ. Structures of protein domains that create or recognize histone modifications. EMBO Rep 2004; 5:464-9.
    • (2004) EMBO Rep , vol.5 , pp. 464-469
    • Bottomley, M.J.1
  • 13
    • 15744396813 scopus 로고    scopus 로고
    • The key to development: Interpreting the histone code?
    • Margueron R, Trojer P, Reinberg D. The key to development: interpreting the histone code? Curr Opin Genet Dev 2005; 15:163-76.
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 163-176
    • Margueron, R.1    Trojer, P.2    Reinberg, D.3
  • 14
    • 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. A role for cell cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 2005; 436:294-8.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 16
    • 0036863542 scopus 로고    scopus 로고
    • Histone acetylation regulates the time of replication origin firing
    • Vogelauer M, Rubbi L, Lucas I, Brewer BJ, Grunstein M. Histone acetylation regulates the time of replication origin firing. Mol Cell 2002; 10:1223-33.
    • (2002) Mol Cell , vol.10 , pp. 1223-1233
    • Vogelauer, M.1    Rubbi, L.2    Lucas, I.3    Brewer, B.J.4    Grunstein, M.5
  • 17
    • 3142768347 scopus 로고    scopus 로고
    • Chromatin regulates origin activity in Drosophila follicle cells
    • Aggarwal BD, Calvi BR. Chromatin regulates origin activity in Drosophila follicle cells. Nature 2004; 430:372-6.
    • (2004) Nature , vol.430 , pp. 372-376
    • Aggarwal, B.D.1    Calvi, B.R.2
  • 18
    • 33646529475 scopus 로고    scopus 로고
    • The temporal program of DNA replication: New insights into old questions
    • Zink D. The temporal program of DNA replication: new insights into old questions. Chromosoma 2006; 115:273-87.
    • (2006) Chromosoma , vol.115 , pp. 273-287
    • Zink, D.1
  • 19
    • 0030982575 scopus 로고    scopus 로고
    • Histone H4 acetylation in plant heterochromatin is altered during the cell cycle
    • Belyaev ND, Houben A, Baranczewski P, Schubert I. Histone H4 acetylation in plant heterochromatin is altered during the cell cycle. Chromosoma 1997; 106:193-7.
    • (1997) Chromosoma , vol.106 , pp. 193-197
    • Belyaev, N.D.1    Houben, A.2    Baranczewski, P.3    Schubert, I.4
  • 20
    • 0034520082 scopus 로고    scopus 로고
    • Histone H4 acetylation of euchromatin and heterochromatin is cell cycle dependent and correlated with replication rather than with transcription
    • Jasencakova Z, Meister A, Walter J, Turner BM, Schubert I. Histone H4 acetylation of euchromatin and heterochromatin is cell cycle dependent and correlated with replication rather than with transcription. Plant Cell 2000; 12:2087-100.
    • (2000) Plant Cell , vol.12 , pp. 2087-2100
    • Jasencakova, Z.1    Meister, A.2    Walter, J.3    Turner, B.M.4    Schubert, I.5
  • 22
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • Couture JF, Collazo E, Brunzelle JS, Trievel RC. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev 2005; 19:1455-65.
    • (2005) Genes Dev , vol.19 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 23
    • 24044470628 scopus 로고    scopus 로고
    • SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20
    • Yin Y, Liu C, Tsai SN, Zhou B, Ngai SM, Zhu G. SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20. J Biol Chem 2005; 280:30025-31.
    • (2005) J Biol Chem , vol.280 , pp. 30025-30031
    • Yin, Y.1    Liu, C.2    Tsai, S.N.3    Zhou, B.4    Ngai, S.M.5    Zhu, G.6
  • 25
    • 0036714189 scopus 로고    scopus 로고
    • Mitotic-specific methylation of histone H4 Lys-20 follows increased PR-Set7 expression and its localization to mitotic chromosomes
    • Rice JC, Nishioka K, Sarma K, Steward R, Reinberg D, Allis CD. Mitotic-specific methylation of histone H4 Lys-20 follows increased PR-Set7 expression and its localization to mitotic chromosomes. Genes Dev 2002; 16:2225-30.
    • (2002) Genes Dev , vol.16 , pp. 2225-2230
    • Rice, J.C.1    Nishioka, K.2    Sarma, K.3    Steward, R.4    Reinberg, D.5    Allis, C.D.6
  • 26
    • 8844248619 scopus 로고    scopus 로고
    • Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
    • Sanders SL, Portoso M, Mata J, Bahler J, Allshire RC, Kouzarides T. Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. Cell 2004; 119:603-14.
    • (2004) Cell , vol.119 , pp. 603-614
    • Sanders, S.L.1    Portoso, M.2    Mata, J.3    Bahler, J.4    Allshire, R.C.5    Kouzarides, T.6
  • 27
    • 13844269327 scopus 로고    scopus 로고
    • PR-Set7-dependent methylation of histone H4 Lys-20 functions in repression of gene expression and is essential for mitosis
    • Karachentsev D, Sarma K, Reinberg D, Steward R. PR-Set7-dependent methylation of histone H4 Lys-20 functions in repression of gene expression and is essential for mitosis. Genes Dev 2005; 19:431-5.
    • (2005) Genes Dev , vol.19 , pp. 431-435
    • Karachentsev, D.1    Sarma, K.2    Reinberg, D.3    Steward, R.4
  • 28
    • 0023579723 scopus 로고
    • Existence of two populations of cyclin/proliferating cell nuclear antigen during the cell cycle: Association with DNA replication sites
    • Bravo R, Macdonald-Bravo H. Existence of two populations of cyclin/proliferating cell nuclear antigen during the cell cycle: association with DNA replication sites. J Cell Biol 1987; 105:1549-54.
    • (1987) J Cell Biol , vol.105 , pp. 1549-1554
    • Bravo, R.1    Macdonald-Bravo, H.2
  • 29
    • 0141733088 scopus 로고    scopus 로고
    • Degradation of cyclin B is required for the onset of anaphase in Mammalian cells
    • Chang DC, Xu N, Luo KQ. Degradation of cyclin B is required for the onset of anaphase in Mammalian cells. J Biol Chem 2003; 278:37865-73.
    • (2003) J Biol Chem , vol.278 , pp. 37865-37873
    • Chang, D.C.1    Xu, N.2    Luo, K.Q.3
  • 30
    • 16644395267 scopus 로고    scopus 로고
    • 2/M phases of the cell cycle
    • 2/M phases of the cell cycle. Methods Mol Biol 2005; 296:157-66.
    • (2005) Methods Mol Biol , vol.296 , pp. 157-166
    • Harper, J.V.1
  • 33
    • 18344386695 scopus 로고    scopus 로고
    • SCF-mediated protein degradation and cell cycle control
    • Ang XL, Wade Harper J. SCF-mediated protein degradation and cell cycle control. Oncogene 2005; 24:2860-70.
    • (2005) Oncogene , vol.24 , pp. 2860-2870
    • Ang, X.L.1    Wade Harper, J.2
  • 34
    • 0031759479 scopus 로고    scopus 로고
    • Histone H4 acetylation during interleukin-2 stimulation of mouse T cells
    • Taplick J, Kurtev V, Lagger G, Seiser C. Histone H4 acetylation during interleukin-2 stimulation of mouse T cells. FEBS Lett 1998; 436:349-52.
    • (1998) FEBS Lett , vol.436 , pp. 349-352
    • Taplick, J.1    Kurtev, V.2    Lagger, G.3    Seiser, C.4
  • 35
    • 0033120570 scopus 로고    scopus 로고
    • Euchromatic domains in plant chromosomes as revealed by H4 histone acetylation and early DNA replication
    • Vyskot B, Siroky J, Hladilova R, Belyaev ND, Turner BM. Euchromatic domains in plant chromosomes as revealed by H4 histone acetylation and early DNA replication. Genome 1999; 42:343-50.
    • (1999) Genome , vol.42 , pp. 343-350
    • Vyskot, B.1    Siroky, J.2    Hladilova, R.3    Belyaev, N.D.4    Turner, B.M.5
  • 36
    • 0029093123 scopus 로고
    • Temporally restricted spatial localization of acetylated isoforms of histone H4 and RNA polymerase II in the 2-cell mouse embryo
    • Worrad DM, Turner BM, Schultz RM. Temporally restricted spatial localization of acetylated isoforms of histone H4 and RNA polymerase II in the 2-cell mouse embryo. Development 1995; 121:2949-59.
    • (1995) Development , vol.121 , pp. 2949-2959
    • Worrad, D.M.1    Turner, B.M.2    Schultz, R.M.3
  • 37
    • 33947536338 scopus 로고    scopus 로고
    • Simple histone acetylation plays a complex role in the regulation of gene expression
    • Fukuda H, Sano N, Muto S, Horikoshi M. Simple histone acetylation plays a complex role in the regulation of gene expression. Brief Funct Genomic Proteomic 2006; 5:190-208.
    • (2006) Brief Funct Genomic Proteomic , vol.5 , pp. 190-208
    • Fukuda, H.1    Sano, N.2    Muto, S.3    Horikoshi, M.4
  • 39
    • 2942674785 scopus 로고    scopus 로고
    • A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1
    • Julien E, Herr W. A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1. Mol Cell 2004; 14:713-25.
    • (2004) Mol Cell , vol.14 , pp. 713-725
    • Julien, E.1    Herr, W.2
  • 40
    • 0037134538 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex
    • Seo SB, Macfarlan T, McNamara P, Hong R, Mukai Y, Heo S, Chakravarti D. Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex. J Biol Chem 2002; 277:14005-10.
    • (2002) J Biol Chem , vol.277 , pp. 14005-14010
    • Seo, S.B.1    Macfarlan, T.2    McNamara, P.3    Hong, R.4    Mukai, Y.5    Heo, S.6    Chakravarti, D.7
  • 41
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
    • Seo SB, McNamara P, Heo S, Turner A, Lane WS, Chakravarti D. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein. Cell 2001; 104:119-30.
    • (2001) Cell , vol.104 , pp. 119-130
    • Seo, S.B.1    McNamara, P.2    Heo, S.3    Turner, A.4    Lane, W.S.5    Chakravarti, D.6
  • 42
    • 3142730622 scopus 로고    scopus 로고
    • A signaling role of histone-binding proteins and INHAT subunits pp32 and Set/TAF-Ibeta in integrating chromatin hypoacetylation and transcriptional repression
    • Kutney SN, Hong R, Macfarlan T, Chakravarti D. A signaling role of histone-binding proteins and INHAT subunits pp32 and Set/TAF-Ibeta in integrating chromatin hypoacetylation and transcriptional repression. J Biol Chem 2004; 279:30850-5.
    • (2004) J Biol Chem , vol.279 , pp. 30850-30855
    • Kutney, S.N.1    Hong, R.2    Macfarlan, T.3    Chakravarti, D.4
  • 43
    • 14844333086 scopus 로고    scopus 로고
    • Human THAP7 is a chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressor
    • Macfarlan T, Kutney S, Altman B, Montross R, Yu J, Chakravarti D. Human THAP7 is a chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressor. J Biol Chem 2005; 280:7346-58.
    • (2005) J Biol Chem , vol.280 , pp. 7346-7358
    • Macfarlan, T.1    Kutney, S.2    Altman, B.3    Montross, R.4    Yu, J.5    Chakravarti, D.6
  • 44
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner BM, Birley AJ, Lavender J. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 1992; 69:375-84.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 46
    • 17244368913 scopus 로고    scopus 로고
    • Genomic characterization reveals a simple histone H4 acetylation code
    • Dion MF, Altschuler SJ, Wu LF, Rando OJ. Genomic characterization reveals a simple histone H4 acetylation code. Proc Natl Acad Sci USA 2005; 102:5501-6.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5501-5506
    • Dion, M.F.1    Altschuler, S.J.2    Wu, L.F.3    Rando, O.J.4
  • 48
    • 0037123767 scopus 로고    scopus 로고
    • Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases
    • Robyr D, Suka Y, Xenarios I, Kurdistani SK, Wang A, Suka N, Grunstein M. Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 2002; 109:437-46.
    • (2002) Cell , vol.109 , pp. 437-446
    • Robyr, D.1    Suka, Y.2    Xenarios, I.3    Kurdistani, S.K.4    Wang, A.5    Suka, N.6    Grunstein, M.7
  • 49
    • 2442660397 scopus 로고    scopus 로고
    • The Rpd3-Sin3 histone deacetylase regulates replication timing and enables intra-S origin control in Saccharomyces cerevisiae
    • Aparicio JG, Viggiani CJ, Gibson DG, Aparicio OM. The Rpd3-Sin3 histone deacetylase regulates replication timing and enables intra-S origin control in Saccharomyces cerevisiae. Mol Cell Biol 2004; 24:4769-80.
    • (2004) Mol Cell Biol , vol.24 , pp. 4769-4780
    • Aparicio, J.G.1    Viggiani, C.J.2    Gibson, D.G.3    Aparicio, O.M.4
  • 50
    • 33947177072 scopus 로고    scopus 로고
    • Developmentally regulated histone modifications in Drosophila follicle cells: Initiation of gene amplification is associated with histone H3 and H4 hyperacetylation and H1 phosphorylation
    • Hartl T, Boswell C, Orr-Weaver TL, Bosco G. Developmentally regulated histone modifications in Drosophila follicle cells: initiation of gene amplification is associated with histone H3 and H4 hyperacetylation and H1 phosphorylation. Chromosoma 2007; 116:197-214.
    • (2007) Chromosoma , vol.116 , pp. 197-214
    • Hartl, T.1    Boswell, C.2    Orr-Weaver, T.L.3    Bosco, G.4
  • 51
    • 0033551686 scopus 로고    scopus 로고
    • Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein
    • Iizuka M, Stillman B. Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein. J Biol Chem 1999; 274:23027-34.
    • (1999) J Biol Chem , vol.274 , pp. 23027-23034
    • Iizuka, M.1    Stillman, B.2
  • 52
    • 0035805606 scopus 로고    scopus 로고
    • Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1
    • Burke TW, Cook JG, Asano M, Nevins JR. Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1. J Biol Chem 2001; 276:15397-408.
    • (2001) J Biol Chem , vol.276 , pp. 15397-15408
    • Burke, T.W.1    Cook, J.G.2    Asano, M.3    Nevins, J.R.4
  • 53
    • 31344462362 scopus 로고    scopus 로고
    • Regulation of replication licensing by acetyltransferase Hbo1
    • Iizuka M, Matsui T, Takisawa H, Smith MM. Regulation of replication licensing by acetyltransferase Hbo1. Mol Cell Biol 2006; 26:1098-108.
    • (2006) Mol Cell Biol , vol.26 , pp. 1098-1108
    • Iizuka, M.1    Matsui, T.2    Takisawa, H.3    Smith, M.M.4
  • 54
    • 0033711708 scopus 로고    scopus 로고
    • Regulation of G(1) cyclin-dependent kinases in the mammalian cell cycle
    • Ekholm SV, Reed SI. Regulation of G(1) cyclin-dependent kinases in the mammalian cell cycle. Curr Opin Cell Biol 2000; 12:676-84.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 676-684
    • Ekholm, S.V.1    Reed, S.I.2
  • 55
    • 0035012849 scopus 로고    scopus 로고
    • Initiating DNA synthesis: From recruiting to activating the MCM complex
    • Lei M, Tye BK. Initiating DNA synthesis: from recruiting to activating the MCM complex. J Cell Sci 2001; 114:1447-54.
    • (2001) J Cell Sci , vol.114 , pp. 1447-1454
    • Lei, M.1    Tye, B.K.2


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