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Volumn 7, Issue 4, 2006, Pages 397-403

Tudor, MBT and chromo domains gauge the degree of lysine methylation

Author keywords

Lysine methylation; Protein domain arrays; Tudor domain

Indexed keywords

BINDING PROTEIN; HISTONE; HISTONE H3; HISTONE H4; LYSINE; METHYL GROUP; PEPTIDE DERIVATIVE;

EID: 33645502395     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400625     Document Type: Article
Times cited : (414)

References (29)
  • 1
    • 0032032823 scopus 로고    scopus 로고
    • Protein methylation: A signal event in post-translational modification
    • Aletta JM, Cimato TR, Ettinger MJ (1998) Protein methylation: A signal event in post-translational modification. Trends Biochem Sci 23: 89-91
    • (1998) Trends Biochem Sci , vol.23 , pp. 89-91
    • Aletta, J.M.1    Cimato, T.R.2    Ettinger, M.J.3
  • 3
    • 0038493626 scopus 로고    scopus 로고
    • Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries
    • Behrends U et al (2003) Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries. Int J Cancer 106: 244-251
    • (2003) Int J Cancer , vol.106 , pp. 244-251
    • Behrends, U.1
  • 4
    • 0037561150 scopus 로고    scopus 로고
    • The human L(3)MBT polycomb group protein is a transcriptional repressor and interacts physically and functionally with TEL (ETV6)
    • Boccuni P, MacGrogan D, Scandura JM, Nimer SD (2003) The human L(3)MBT polycomb group protein is a transcriptional repressor and interacts physically and functionally with TEL (ETV6). J Biol Chem 278: 15412-15420
    • (2003) J Biol Chem , vol.278 , pp. 15412-15420
    • Boccuni, P.1    MacGrogan, D.2    Scandura, J.M.3    Nimer, S.D.4
  • 5
    • 0023038380 scopus 로고
    • Phosphorylation of histones is stimulated by phorbol esters in quiescent Reuber H35 hepatoma cells
    • Butler AP, Byus CV, Slaga TJ (1986) Phosphorylation of histones is stimulated by phorbol esters in quiescent Reuber H35 hepatoma cells. J Biol Chem 261: 9421-9425
    • (1986) J Biol Chem , vol.261 , pp. 9421-9425
    • Butler, A.P.1    Byus, C.V.2    Slaga, T.J.3
  • 7
    • 3042522654 scopus 로고    scopus 로고
    • Chromatin dynamics at DNA replication, transcription and repair
    • Ehrenhofer-Murray AE (2004) Chromatin dynamics at DNA replication, transcription and repair. Eur J Biochem 271: 2335-2349
    • (2004) Eur J Biochem , vol.271 , pp. 2335-2349
    • Ehrenhofer-Murray, A.E.1
  • 8
    • 0036846034 scopus 로고    scopus 로고
    • A protein-domain microarray identifies novel protein-protein interactions
    • Espejo A, Cote J, Bednarek A, Richard S, Bedford MT (2002) A protein-domain microarray identifies novel protein-protein interactions. Biochem J 367: 697-702
    • (2002) Biochem J , vol.367 , pp. 697-702
    • Espejo, A.1    Cote, J.2    Bednarek, A.3    Richard, S.4    Bedford, M.T.5
  • 9
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains
    • Fischle W, Wang Y, Jacobs SA, Kim Y, Allis CD, Khorasanizadeh S (2003) Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev 17: 1870-1881
    • (2003) Genes Dev , vol.17 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 10
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • Friesen WJ, Massenet S, Paushkin S, Wyce A, Dreyfuss G (2001) SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol Cell 7: 1111-1117
    • (2001) Mol Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 11
    • 23344436787 scopus 로고    scopus 로고
    • Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
    • Gray SG et al (2005) Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem 280: 28507-28518
    • (2005) J Biol Chem , vol.280 , pp. 28507-28518
    • Gray, S.G.1
  • 13
    • 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
  • 14
    • 16544389546 scopus 로고    scopus 로고
    • Identification and characterization of JMJD2 family genes in silico
    • Katoh M (2004) Identification and characterization of JMJD2 family genes in silico. Int J Oncol 24: 1623-1628
    • (2004) Int J Oncol , vol.24 , pp. 1623-1628
    • Katoh, M.1
  • 15
    • 0033166849 scopus 로고    scopus 로고
    • A human homolog of Drosophila lethal(3)malignant brain tumor (l(3)mbt) protein associates with condensed mitotic chromosomes
    • Koga H, Matsui S, Hirota T, Takebayashi S, Okumura K, Saya H (1999) A human homolog of Drosophila lethal(3)malignant brain tumor (l(3)mbt) protein associates with condensed mitotic chromosomes. Oncogene 18: 3799-3809
    • (1999) Oncogene , vol.18 , pp. 3799-3809
    • Koga, H.1    Matsui, S.2    Hirota, T.3    Takebayashi, S.4    Okumura, K.5    Saya, H.6
  • 16
    • 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
  • 17
    • 2442544539 scopus 로고    scopus 로고
    • Imprinting of the human L3MBTL gene, a polycomb family member located in a region of chromosome 20 deleted in human myeloid malignancies
    • Li J, Bench AJ, Vassiliou GS, Fourouclas N, Ferguson-Smith AC, Green AR (2004) Imprinting of the human L3MBTL gene, a polycomb family member located in a region of chromosome 20 deleted in human myeloid malignancies. Proc Natl Acad Sci USA 101: 7341-7346
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7341-7346
    • Li, J.1    Bench, A.J.2    Vassiliou, G.S.3    Fourouclas, N.4    Ferguson-Smith, A.C.5    Green, A.R.6
  • 18
    • 0037112527 scopus 로고    scopus 로고
    • 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s)
    • Liu MY, Cai S, Espejo A, Bedford MT, Walker CL (2002) 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s). Cancer Res 62: 6475-6480
    • (2002) Cancer Res , vol.62 , pp. 6475-6480
    • Liu, M.Y.1    Cai, S.2    Espejo, A.3    Bedford, M.T.4    Walker, C.L.5
  • 19
    • 8744291701 scopus 로고    scopus 로고
    • Sequence family variant loss from the AZFc interval of the human Y chromosome, but not gene copy loss, is strongly associated with male infertility
    • Machev N et al (2004) Sequence family variant loss from the AZFc interval of the human Y chromosome, but not gene copy loss, is strongly associated with male infertility. J Med Genet 41: 814-825
    • (2004) J Med Genet , vol.41 , pp. 814-825
    • Machev, N.1
  • 21
    • 0041624288 scopus 로고    scopus 로고
    • Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
    • Min J, Zhang Y, Xu RM (2003) Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev 17: 1823-1828
    • (2003) Genes Dev , vol.17 , pp. 1823-1828
    • Min, J.1    Zhang, Y.2    Xu, R.M.3
  • 22
    • 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 III JR, Grant PA (2005) Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Nature 433: 434-438
    • (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
  • 23
    • 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 (2004) Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. Cell 119: 603-614
    • (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
  • 25
    • 10344236999 scopus 로고    scopus 로고
    • Tudor domains track down DNA breaks
    • Stucki M, Jackson SP (2004) Tudor domains track down DNA breaks. Nat Cell Biol 6: 1150-1152
    • (2004) Nat Cell Biol , vol.6 , pp. 1150-1152
    • Stucki, M.1    Jackson, S.P.2
  • 26
    • 0037099413 scopus 로고    scopus 로고
    • G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
    • Tachibana M et al (2002) G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev 16: 1779-1791
    • (2002) Genes Dev , vol.16 , pp. 1779-1791
    • Tachibana, M.1
  • 28
    • 0141638426 scopus 로고    scopus 로고
    • N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso
    • Yoon HG, Chan DW, Reynolds AB, Qin J, Wong J (2003) N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso. Mol Cell 12: 723-734
    • (2003) Mol Cell , vol.12 , pp. 723-734
    • Yoon, H.G.1    Chan, D.W.2    Reynolds, A.B.3    Qin, J.4    Wong, J.5
  • 29
    • 22544465244 scopus 로고    scopus 로고
    • JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2)
    • Zhang D, Yoon HG, Wong J (2005) JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2). Mol Cell Biol 25: 6404-6414
    • (2005) Mol Cell Biol , vol.25 , pp. 6404-6414
    • Zhang, D.1    Yoon, H.G.2    Wong, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.