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Volumn 112, Issue 5, 2003, Pages 711-723

Structure of the catalytic domain of human Dot1L, a non-SET domain nucleosomal histone methyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

METHYLTRANSFERASE; METHYLTRANSFERASE DOT1L; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

EID: 0344837759     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00114-4     Document Type: Article
Times cited : (347)

References (45)
  • 4
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng X., Roberts R.J. AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res. 29:2001;3784-3795.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3784-3795
    • Cheng, X.1    Roberts, R.J.2
  • 5
    • 0035399471 scopus 로고    scopus 로고
    • Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold
    • Dlakic M. Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold. Trends Biochem. Sci. 26:2001;405-407.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 405-407
    • Dlakic, M.1
  • 8
  • 9
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for processing and analyzing diffraction data from macromolecules
    • Furey W., Swaminathan S. PHASES-95. a program package for processing and analyzing diffraction data from macromolecules Methods Enzymol. 277:1997;590-620.
    • (1997) Methods Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 10
    • 0036532235 scopus 로고    scopus 로고
    • Heterochromatin: New possibilities for the inheritance of structure
    • Grewal S.I., Elgin S.C. Heterochromatin. new possibilities for the inheritance of structure Curr. Opin. Genet. Dev. 12:2002;178-187.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 178-187
    • Grewal, S.I.1    Elgin, S.C.2
  • 11
    • 0035834493 scopus 로고    scopus 로고
    • Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate
    • Griffith S.C., Sawaya M.R., Boutz D.R., Thapar N., Katz J.E., Clarke S., Yeates T.O. Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate. J. Mol. Biol. 313:2001;1103-1116.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1103-1116
    • Griffith, S.C.1    Sawaya, M.R.2    Boutz, D.R.3    Thapar, N.4    Katz, J.E.5    Clarke, S.6    Yeates, T.O.7
  • 12
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson W.A., Horton J.R., LeMaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD). a vehicle for direct determination of three-dimensional structure EMBO J. 9:1990;1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 15
    • 0026244229 scopus 로고
    • Molscript-a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript-a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 16
    • 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. 14:2002;286-298.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 17
    • 0037163016 scopus 로고    scopus 로고
    • Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase
    • Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J. Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase. J. Biol. Chem. 277:2002;30421-30424.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30421-30424
    • Lacoste, N.1    Utley, R.T.2    Hunter, J.M.3    Poirier, G.G.4    Cote, J.5
  • 19
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature. 389:1997;251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 20
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 21
    • 0036829968 scopus 로고    scopus 로고
    • Structure of the SET domain histone lysine methyltransferase Clr4
    • Min J., Zhang X., Cheng X., Grewal S.I., Xu R.M. Structure of the SET domain histone lysine methyltransferase Clr4. Nat. Struct. Biol. 9:2002;828-833.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 828-833
    • Min, J.1    Zhang, X.2    Cheng, X.3    Grewal, S.I.4    Xu, R.M.5
  • 22
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • a
    • Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 16:2002;1518-1527. a.
    • (2002) Genes Dev. , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 23
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3-lysine 79
    • b
    • Ng H.H., Xu R.M., Zhang Y., Struhl K. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3-lysine 79. J. Biol. Chem. 277:2002;34655-34657. b.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0033786367 scopus 로고    scopus 로고
    • Role for the silencing protein Dot1 in meiotic checkpoint control
    • San-Segundo P.A., Roeder G.S. Role for the silencing protein Dot1 in meiotic checkpoint control. Mol. Biol. Cell. 11:2000;3601-3615.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3601-3615
    • San-Segundo, P.A.1    Roeder, G.S.2
  • 31
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., 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
  • 33
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z.W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature. 418:2002;104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 35
    • 0037020199 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of a SET domain protein methyltransferase
    • Trievel R.C., Beach B.M., Dirk L.M.A., Houtz R.L., Hurley J.H. Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell. 111:2002;91-103.
    • (2002) Cell , vol.111 , pp. 91-103
    • Trievel, R.C.1    Beach, B.M.2    Dirk, L.M.A.3    Houtz, R.L.4    Hurley, J.H.5
  • 36
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner B.M. Histone acetylation and an epigenetic code. Bioessays. 22:2000;836-845.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 37
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F., Gafken P.R., Gottschling D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell. 109:2002;745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 38
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren J., Svensson L.A., Liljas A. Crystal structure of catechol O-methyltransferase. Nature. 368:1994;354-358.
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 40
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White C.L., Suto R.K., Luger K. Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J. 20:2001;5207-5218.
    • (2001) EMBO J. , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 42
    • 0034387004 scopus 로고    scopus 로고
    • 25 Years after the nucleosome model: Chromatin modifications
    • Wu J., Grunstein M. 25 years after the nucleosome model. chromatin modifications Trends Biochem. Sci. 25:2000;619-623.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 619-623
    • Wu, J.1    Grunstein, M.2
  • 43
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang X., Zhou L., Cheng X. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. EMBO J. 19:2000;3509-3519.
    • (2000) EMBO J. , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 44
    • 0037020217 scopus 로고    scopus 로고
    • Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase
    • Zhang X., Tamaru H., Khan H.I., Horton J.R., Keefe L.J., Selker E.U., Cheng X. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell. 111:2002;117-127.
    • (2002) Cell , vol.111 , pp. 117-127
    • Zhang, X.1    Tamaru, H.2    Khan, H.I.3    Horton, J.R.4    Keefe, L.J.5    Selker, E.U.6    Cheng, X.7
  • 45
    • 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. 15:2001;2343-2360.
    • (2001) Genes Dev. , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2


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