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Volumn 359, Issue 1, 2006, Pages 86-96

Structural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase

Author keywords

lysine 27; structure; vSET

Indexed keywords

ENZYME VARIANT; HISTONE H3; HISTONE METHYLTRANSFERASE; LYSINE; METHYL GROUP; S ADENOSYLHOMOCYSTEINE; VIRUS ENZYME;

EID: 33646203168     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.03.006     Document Type: Article
Times cited : (53)

References (38)
  • 1
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 2
    • 0035371872 scopus 로고    scopus 로고
    • Re-SET-ting heterochromatin by histone methyltransferases
    • Jenuwein T. Re-SET-ting heterochromatin by histone methyltransferases. Trends Cell Biol. 11 (2001) 266-273
    • (2001) Trends Cell Biol. , vol.11 , pp. 266-273
    • Jenuwein, T.1
  • 3
    • 0028110864 scopus 로고
    • The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes
    • Tschiersch B., Hofmann A., Krauss V., Dorn R., Korge G., and Reuter G. The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes. EMBO J. 13 (1994) 3822-3831
    • (1994) EMBO J. , vol.13 , pp. 3822-3831
    • Tschiersch, B.1    Hofmann, A.2    Krauss, V.3    Dorn, R.4    Korge, G.5    Reuter, G.6
  • 4
    • 0027445713 scopus 로고
    • The Drosophila Polycomb-group gene enhancer of zeste contains a region with sequence similarity to trithorax
    • Jones R.S., and Gelbart W.M. The Drosophila Polycomb-group gene enhancer of zeste contains a region with sequence similarity to trithorax. Mol. Cell. Biol. 13 (1993) 6357-6366
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6357-6366
    • Jones, R.S.1    Gelbart, W.M.2
  • 5
    • 0029151566 scopus 로고
    • The Drosophila trithorax proteins contain a novel variant of the nuclear receptor type DNA binding domain and an ancient conserved motif found in other chromosomal proteins
    • Stassen M.J., Bailey D., Nelson S., Chinwalla V., and Harte P.J. The Drosophila trithorax proteins contain a novel variant of the nuclear receptor type DNA binding domain and an ancient conserved motif found in other chromosomal proteins. Mech. Dev. 52 (1995) 209-223
    • (1995) Mech. Dev. , vol.52 , pp. 209-223
    • Stassen, M.J.1    Bailey, D.2    Nelson, S.3    Chinwalla, V.4    Harte, P.J.5
  • 6
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 7
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner B.M. Cellular memory and the histone code. Cell 111 (2002) 285-291
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 8
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner M., O'Sullivan R.J., and Jenuwein T. An epigenetic road map for histone lysine methylation. J. Cell. Sci. 116 (2003) 2117-2124
    • (2003) J. Cell. Sci. , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 9
    • 0037188911 scopus 로고    scopus 로고
    • Histone methylation: dynamic or static?
    • Bannister A.J., Schneider R., and Kouzarides T. Histone methylation: dynamic or static?. Cell 109 (2002) 801-806
    • (2002) Cell , vol.109 , pp. 801-806
    • Bannister, A.J.1    Schneider, R.2    Kouzarides, T.3
  • 11
    • 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., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M., et al. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16 (2002) 1779-1791
    • (2002) Genes Dev. , vol.16 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6
  • 12
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., and Pirrotta V. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 111 (2002) 185-196
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5    Pirrotta, V.6
  • 13
    • 18644383738 scopus 로고    scopus 로고
    • Histone methyltransferase activity of a Drosophila Polycomb group repressor complex
    • Muller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B., et al. Histone methyltransferase activity of a Drosophila Polycomb group repressor complex. Cell 111 (2002) 197-208
    • (2002) Cell , vol.111 , pp. 197-208
    • Muller, J.1    Hart, C.M.2    Francis, N.J.3    Vargas, M.L.4    Sengupta, A.5    Wild, B.6
  • 14
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298 (2002) 1039-1043
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 15
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the enhancer of Zeste protein
    • Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., and Reinberg D. Histone methyltransferase activity associated with a human multiprotein complex containing the enhancer of Zeste protein. Genes Dev. 16 (2002) 2893-2905
    • (2002) Genes Dev. , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 17
    • 0036337759 scopus 로고    scopus 로고
    • Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes
    • Boggs B.A., Cheung P., Heard E., Spector D.L., Chinault A.C., and Allis C.D. Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes. Nature Genet. 30 (2002) 73-76
    • (2002) Nature Genet. , vol.30 , pp. 73-76
    • Boggs, B.A.1    Cheung, P.2    Heard, E.3    Spector, D.L.4    Chinault, A.C.5    Allis, C.D.6
  • 19
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • Kouskouti A., Scheer E., Staub A., Tora L., and Talianidis I. Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol. Cell. 14 (2004) 175-182
    • (2004) Mol. Cell. , vol.14 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 20
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz J., Milpetz F., Bork P., and Ponting C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl Acad. Sci. USA 95 (1998) 5857-5864
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 21
    • 3142674953 scopus 로고    scopus 로고
    • Structure and function of histone methyltransferases
    • Trievel R.C. Structure and function of histone methyltransferases. Crit. Rev. Eukaryot. Gene Expr. 14 (2004) 147-169
    • (2004) Crit. Rev. Eukaryot. Gene Expr. , vol.14 , pp. 147-169
    • Trievel, R.C.1
  • 23
    • 20544461679 scopus 로고    scopus 로고
    • Structural and sequence motifs of protein (histone) methylation enzymes
    • Cheng X., Collins R.E., and Zhang X. Structural and sequence motifs of protein (histone) methylation enzymes. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 267-294
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 267-294
    • Cheng, X.1    Collins, R.E.2    Zhang, X.3
  • 25
    • 0346599192 scopus 로고    scopus 로고
    • Unusual life style of giant chlorella viruses
    • Van Etten J.L. Unusual life style of giant chlorella viruses. Annu. Rev. Genet. 37 (2003) 153-195
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 153-195
    • Van Etten, J.L.1
  • 26
    • 0028674451 scopus 로고
    • Multidimensional heteronuclear nuclear magnetic resonance of proteins
    • Clore G.M., and Gronenborn A.M. Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol. 239 (1994) 249-363
    • (1994) Methods Enzymol. , vol.239 , pp. 249-363
    • Clore, G.M.1    Gronenborn, A.M.2
  • 27
    • 0042164227 scopus 로고    scopus 로고
    • Structural basis for the product specificity of histone lysine methyltransferases
    • Zhang X., Yang Z., Khan S.I., Horton J.R., Tamaru H., Selker E.U., and Cheng X. Structural basis for the product specificity of histone lysine methyltransferases. Mol. Cell. 12 (2003) 177-185
    • (2003) Mol. Cell. , vol.12 , pp. 177-185
    • Zhang, X.1    Yang, Z.2    Khan, S.I.3    Horton, J.R.4    Tamaru, H.5    Selker, E.U.6    Cheng, X.7
  • 28
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W., Wang Y., and Allis C.D. Binary switches and modification cassettes in histone biology and beyond. Nature 425 (2003) 475-479
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 29
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 30
    • 0037421847 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the human histone methyltransferase SET7/9
    • Xiao B., Jing C., Wilson J.R., Walker P.A., Vasisht N., Kelly G., et al. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 421 (2003) 652-656
    • (2003) Nature , vol.421 , pp. 652-656
    • Xiao, B.1    Jing, C.2    Wilson, J.R.3    Walker, P.A.4    Vasisht, N.5    Kelly, G.6
  • 31
    • 0038419637 scopus 로고    scopus 로고
    • Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
    • Trievel R.C., Flynn E.M., Houtz R.L., and Hurley J.H. Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT. Nature Struct. Biol. 10 (2003) 545-552
    • (2003) Nature Struct. Biol. , vol.10 , pp. 545-552
    • Trievel, R.C.1    Flynn, E.M.2    Houtz, R.L.3    Hurley, J.H.4
  • 33
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • Couture J.F., Collazo E., Brunzelle J.S., and Trievel R.C. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev. 19 (2005) 1455-1465
    • (2005) Genes Dev. , vol.19 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 36
    • 0347988396 scopus 로고    scopus 로고
    • Ambiguous NOEs and automated NOE assignment
    • Nilges M., and O'Donoghue S. Ambiguous NOEs and automated NOE assignment. Prog. NMR Spectrosc. 32 (1998) 107-139
    • (1998) Prog. NMR Spectrosc. , vol.32 , pp. 107-139
    • Nilges, M.1    O'Donoghue, S.2
  • 38
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.-W., Schmid M., et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature (2000) 593-599
    • (2000) Nature , pp. 593-599
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3    Strahl, B.D.4    Sun, Z.-W.5    Schmid, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.