메뉴 건너뛰기




Volumn 5, Issue 12, 2006, Pages 1308-1312

Lysine methylation goes global

Author keywords

Chromatin; Gene regulation; Histone code; Lysine methylation; p53; Post translational modifications

Indexed keywords

ACYLTRANSFERASE; HISTONE; HISTONE METHYLTRANSFERASE; LYSINE; LYSINE METHYLTRANSFERASE; METHYLTRANSFERASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 33745122241     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.5.12.2820     Document Type: Review
Times cited : (45)

References (65)
  • 1
    • 0035859030 scopus 로고    scopus 로고
    • The ins and outs of signalling
    • Downward J. The ins and outs of signalling. Nature 2001; 411:759-62.
    • (2001) Nature , vol.411 , pp. 759-762
    • Downward, J.1
  • 2
    • 0015412099 scopus 로고
    • In vivo turnover and distribution of radio-N-methyl in arginine-rich histones from rat tissues
    • Byvoet P. In vivo turnover and distribution of radio-N-methyl in arginine-rich histones from rat tissues. Arch Biochem Biophys 1972; 152:887-8.
    • (1972) Arch Biochem Biophys , vol.152 , pp. 887-888
    • Byvoet, P.1
  • 3
    • 0016271161 scopus 로고
    • In vivo methylation and turnover of rat brain histones
    • Duerre JA, Lee CT. In vivo methylation and turnover of rat brain histones. J Neurochem 1974; 23:541-7.
    • (1974) J Neurochem , vol.23 , pp. 541-547
    • Duerre, J.A.1    Lee, C.T.2
  • 4
    • 0022126043 scopus 로고
    • Histones in perspective
    • von Holt C. Histones in perspective. Bioessays 1985; 3:120-4.
    • (1985) Bioessays , vol.3 , pp. 120-124
    • Von Holt, C.1
  • 5
    • 33644652364 scopus 로고    scopus 로고
    • Lysine methylation and 'signaling memory'
    • Su IH, Tarakhovsky A. Lysine methylation and 'signaling memory'. Curr Opin Immunol 2006; 18:152-7.
    • (2006) Curr Opin Immunol , vol.18 , pp. 152-157
    • Su, I.H.1    Tarakhovsky, A.2
  • 8
    • 0018132189 scopus 로고
    • Modification of yeast ribosomal proteins. Methylation
    • Kruiswijk T, Kunst A, Planta RJ, Mager WH. Modification of yeast ribosomal proteins. Methylation. Biochem J 1978; 175:221-5.
    • (1978) Biochem J , vol.175 , pp. 221-225
    • Kruiswijk, T.1    Kunst, A.2    Planta, R.J.3    Mager, W.H.4
  • 10
    • 27144441000 scopus 로고    scopus 로고
    • A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in yeast
    • Porras-Yakushi TR, Whitelegge JP, Miranda TB, Clarke S. A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in yeast. J Biol Chem 2005; 280:34590-8.
    • (2005) J Biol Chem , vol.280 , pp. 34590-34598
    • Porras-Yakushi, T.R.1    Whitelegge, J.P.2    Miranda, T.B.3    Clarke, S.4
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides T. Histone methylation in transcriptional control. Curr Opin Genet Dev 2002; 12:198-209.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 14
    • 0037188911 scopus 로고    scopus 로고
    • Histone methylation: Dynamic or static?
    • Bannister AJ, Schneider R, Kouzarides T. Histone methylation: Dynamic or static? Cell 2002; 109:801-6.
    • (2002) Cell , vol.109 , pp. 801-806
    • Bannister, A.J.1    Schneider, R.2    Kouzarides, T.3
  • 15
    • 24144475284 scopus 로고    scopus 로고
    • Reversing histone methylation
    • Bannister AJ, Kouzarides T. Reversing histone methylation. Nature 2005; 436:1103-6.
    • (2005) Nature , vol.436 , pp. 1103-1106
    • Bannister, A.J.1    Kouzarides, T.2
  • 16
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C, Zhang Y. The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 2005; 6:838-49.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 17
    • 14844361808 scopus 로고    scopus 로고
    • Multisite protein modification and intramolecular signaling
    • Yang XJ. Multisite protein modification and intramolecular signaling. Oncogene 2005; 24:1653-62.
    • (2005) Oncogene , vol.24 , pp. 1653-1662
    • Yang, X.J.1
  • 18
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
    • Pray-Grant MG, Daniel JA, Schieltz D, Yates IIIrd JR, Grant PA. Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Nature 2005; 433:434-8.
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates III, J.R.4    Grant, P.A.5
  • 20
    • 29644433964 scopus 로고    scopus 로고
    • Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains
    • Sims IIIrd RJ, Chen CF, Santos-Rosa H, Kouzarides T, Patel SS, Reinberg D. Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains. J Biol Chem 2005; 280:41789-92.
    • (2005) J Biol Chem , vol.280 , pp. 41789-41792
    • Sims III, R.J.1    Chen, C.F.2    Santos-Rosa, H.3    Kouzarides, T.4    Patel, S.S.5    Reinberg, D.6
  • 21
    • 25444520791 scopus 로고    scopus 로고
    • Effector proteins for methylated histones: An expanding family
    • Daniel JA, Pray-Grant MG, Grant PA. Effector proteins for methylated histones: An expanding family. Cell Cycle 2005; 4:919-26.
    • (2005) Cell Cycle , vol.4 , pp. 919-926
    • Daniel, J.A.1    Pray-Grant, M.G.2    Grant, P.A.3
  • 22
    • 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. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001; 410:116-20.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 23
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner M, Jenuwein T. The many faces of histone lysine methylation. Curr Opin Cell Biol 2002; 14:286-98.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 25
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol Cell 2001; 8:1207-17.
    • (2001) Mol Cell , vol.8 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 26
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev 2002; 16:479-89.
    • (2002) Genes Dev , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7
  • 29
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • Kouskouti A, Scheer E, Staub A, Tora L, Talianidis I. Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol Cell 2004; 14:175-82.
    • (2004) Mol Cell , vol.14 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 31
    • 0033540266 scopus 로고    scopus 로고
    • Regulation of gene expression by multiple forms of TFIID and other novel TAFII-containing complexes
    • Bell B, Tora L. Regulation of gene expression by multiple forms of TFIID and other novel TAFII-containing complexes. Exp Cell Res 1999; 246:11-9.
    • (1999) Exp Cell Res , vol.246 , pp. 11-19
    • Bell, B.1    Tora, L.2
  • 32
    • 0842263778 scopus 로고    scopus 로고
    • The multicoloured world of promoter recognition complexes
    • Muller F, Tora L. The multicoloured world of promoter recognition complexes. EMBO J 2004; 23:2-8.
    • (2004) EMBO J , vol.23 , pp. 2-8
    • Muller, F.1    Tora, L.2
  • 33
    • 0038724283 scopus 로고    scopus 로고
    • TAF10 (TAF(II)30) is necessary for TFIID stability and early embryogenesis in mice
    • Mohan Jr WS, Scheer E, Wendling O, Metzger D, Tora L. TAF10 (TAF(II)30) is necessary for TFIID stability and early embryogenesis in mice. Mol Cell Biol 2003; 23:4307-18.
    • (2003) Mol Cell Biol , vol.23 , pp. 4307-4318
    • Mohan Jr., W.S.1    Scheer, E.2    Wendling, O.3    Metzger, D.4    Tora, L.5
  • 34
    • 0035940471 scopus 로고    scopus 로고
    • TAFII55 binding to TAFII250 inhibits its acetyltransferase activity
    • USA
    • Gegonne A, Weissman JD, Singer DS. TAFII55 binding to TAFII250 inhibits its acetyltransferase activity. Proc Natl Acad Sci USA 2001; 98:12432-7.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 12432-12437
    • Gegonne, A.1    Weissman, J.D.2    Singer, D.S.3
  • 35
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella E, Anderson CW. Post-translational modifications and activation of p53 by genotoxic stresses. Eur J Biochem 2001; 268:2764-72.
    • (2001) Eur J Biochem , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 36
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks CL, Gu W. Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation. Curr Opin Cell Biol 2003; 15:164-71.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 37
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • Bode AM, Dong Z. Post-translational modification of p53 in tumorigenesis. Nat Rev Cancer 2004; 4:793-805.
    • (2004) Nat Rev Cancer , vol.4 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 38
    • 0033732303 scopus 로고    scopus 로고
    • MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins
    • USA
    • Kobet E, Zeng X, Zhu Y, Keller D, Lu H. MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins. Proc Natl Acad Sci USA 2000; 97:12547-52.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 12547-12552
    • Kobet, E.1    Zeng, X.2    Zhu, Y.3    Keller, D.4    Lu, H.5
  • 39
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997; 387:296-9.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 40
    • 31544457877 scopus 로고    scopus 로고
    • p53 Ubiquitination: Mdm2 and beyond
    • Brooks CL, Gu W. p53 Ubiquitination: Mdm2 and beyond. Mol Cell 2006; 21:307-15.
    • (2006) Mol Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 41
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li M, Luo J, Brooks CL, Gu W. Acetylation of p53 inhibits its ubiquitination by Mdm2. J Biol Chem 2002; 277:50607-11.
    • (2002) J Biol Chem , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 42
    • 4644235697 scopus 로고    scopus 로고
    • Monoubiquitination: The signal for p53 nuclear export?
    • Brooks CL, Li M, Gu W. Monoubiquitination: The signal for p53 nuclear export? Cell Cycle 2004; 3:436-8.
    • (2004) Cell Cycle , vol.3 , pp. 436-438
    • Brooks, C.L.1    Li, M.2    Gu, W.3
  • 43
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
    • Zegerman P, Canas B, Pappin D, Kouzarides T. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J Biol Chem 2002; 277:11621-4.
    • (2002) J Biol Chem , vol.277 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 44
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W, Wang Y, Allis CD. Binary switches and modification cassettes in histone biology and beyond. Nature 2003; 425:475-9.
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 45
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo WS, Trievel RC, Rojas JR, Duggan L, Hsu JY, Allis CD, Marmorstein R, Berger L. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Molecular Cell 2000; 5:917-26.
    • (2000) Molecular Cell , vol.5 , pp. 917-926
    • Lo, W.S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.Y.5    Allis, C.D.6    Marmorstein, R.7    Berger, L.8
  • 46
    • 16344395502 scopus 로고    scopus 로고
    • Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms
    • Lo WS, Gamache ER, Henry KW, Yang D, Pillus L, Berger SL. Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms. EMBO J 2005; 24:997-1008.
    • (2005) EMBO J , vol.24 , pp. 997-1008
    • Lo, W.S.1    Gamache, E.R.2    Henry, K.W.3    Yang, D.4    Pillus, L.5    Berger, S.L.6
  • 47
    • 0032540088 scopus 로고    scopus 로고
    • Regulation of the p53 protein by protein kinase C alpha and protein kinase C zeta
    • Youmell M, Park SJ, Basu S, Price BD. Regulation of the p53 protein by protein kinase C alpha and protein kinase C zeta. Biochem Biophys Res Commun 1998; 245:514-8.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 514-518
    • Youmell, M.1    Park, S.J.2    Basu, S.3    Price, B.D.4
  • 49
    • 0036848066 scopus 로고    scopus 로고
    • Dam1 is the right one: Phosphoregulation of kinetochore biorientation
    • Courtwright AM, He X. Dam1 is the right one: Phosphoregulation of kinetochore biorientation. Dev Cell 2002; 3:610-1.
    • (2002) Dev Cell , vol.3 , pp. 610-611
    • Courtwright, A.M.1    He, X.2
  • 50
    • 13544272858 scopus 로고    scopus 로고
    • Mechanisms of transformation by MLL
    • Hess JL. Mechanisms of transformation by MLL. Crit Rev Eukaryot Gene Expr 2004; 14:235-54.
    • (2004) Crit Rev Eukaryot Gene Expr , vol.14 , pp. 235-254
    • Hess, J.L.1
  • 51
    • 22544468602 scopus 로고    scopus 로고
    • A COMPASS in the voyage of defining the role of trithorax/MLL-containing complexes: Linking leukemogensis to covalent modifications of chromatin
    • Tenney K, Shilatifard A. A COMPASS in the voyage of defining the role of trithorax/MLL-containing complexes: Linking leukemogensis to covalent modifications of chromatin. J Cell Biochem 2005; 95:429-36.
    • (2005) J Cell Biochem , vol.95 , pp. 429-436
    • Tenney, K.1    Shilatifard, A.2
  • 53
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • Lee MG, Wynder C, Cooch N, Shiekhattar R. An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 2005; 437:432-5.
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 55
    • 24144470824 scopus 로고    scopus 로고
    • Taking LSD 1 to a new high
    • Wysocka J, Milne TA, Allis CD. Taking LSD 1 to a new high. Cell 2005; 122:654-8.
    • (2005) Cell , vol.122 , pp. 654-658
    • Wysocka, J.1    Milne, T.A.2    Allis, C.D.3
  • 57
    • 0035150397 scopus 로고    scopus 로고
    • JmjC: Cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta
    • Clissold PM, Ponting CP. JmjC: Cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta. Trends Biochem Sci 2001; 26:7-9.
    • (2001) Trends Biochem Sci , vol.26 , pp. 7-9
    • Clissold, P.M.1    Ponting, C.P.2
  • 59
    • 0042856303 scopus 로고    scopus 로고
    • SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo
    • Chakraborty S, Sinha KK, Senyuk V, Nucifora G. SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo. Oncogene 2003; 22:5229-37.
    • (2003) Oncogene , vol.22 , pp. 5229-5237
    • Chakraborty, S.1    Sinha, K.K.2    Senyuk, V.3    Nucifora, G.4
  • 60
    • 27944501617 scopus 로고    scopus 로고
    • Histone modifying enzymes and cancer: Going beyond histones
    • Zhang K, Dent SY. Histone modifying enzymes and cancer: Going beyond histones. J Cell Biochem 2005; 96:1137-48.
    • (2005) J Cell Biochem , vol.96 , pp. 1137-1148
    • Zhang, K.1    Dent, S.Y.2
  • 62
    • 33646848438 scopus 로고    scopus 로고
    • Substrate preferences of the EZH2 histone methyltransferase complex
    • Martin C, Cao R, Zhang Y. Substrate preferences of the EZH2 histone methyltransferase complex. J Biol Chem 2006; 281:8365-70.
    • (2006) J Biol Chem , vol.281 , pp. 8365-8370
    • Martin, C.1    Cao, R.2    Zhang, Y.3
  • 63
    • 0024636180 scopus 로고
    • Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase
    • USA
    • Houtz RL, Stults JT, Mulligan RM, Tolbert NE. Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/ oxygenase. Proc Natl Acad Sci USA 1989; 86:1855-9.
    • (1989) Proc Natl Acad Sci , vol.86 , pp. 1855-1859
    • Houtz, R.L.1    Stults, J.T.2    Mulligan, R.M.3    Tolbert, N.E.4
  • 64
    • 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, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J 2001; 20:7137-48.
    • (2001) EMBO J , vol.20 , pp. 7137-7148
    • Roguev, A.1    Schaft, D.2    Shevchenko, A.3    Pijnappel, W.W.4    Wilm, M.5    Aasland, R.6    Stewart, A.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.