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Volumn 10, Issue 5, 2002, Pages 1107-1117

MLL targets SET domain methyltransferase activity to Hox gene promoters

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; HOX PROTEIN; HYBRID PROTEIN; LYSINE; METHYLTRANSFERASE; MIXED LINEAGE LEUKEMIA PROTEIN;

EID: 18744373853     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(02)00741-4     Document Type: Article
Times cited : (903)

References (53)
  • 2
    • 0035839952 scopus 로고    scopus 로고
    • Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins
    • a
    • Ayton P.M., Cleary M.L. Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins. Oncogene. 20:2001;5695-5707. a.
    • (2001) Oncogene , vol.20 , pp. 5695-5707
    • Ayton, P.M.1    Cleary, M.L.2
  • 3
    • 79960971222 scopus 로고    scopus 로고
    • Transformation of myeloid progenitors by MLL fusion proteins requires Hoxa7 and Hoxa9 and their DNA binding partner Pbx2
    • b
    • Ayton P.M., Cleary M.L. Transformation of myeloid progenitors by MLL fusion proteins requires Hoxa7 and Hoxa9 and their DNA binding partner Pbx2. Blood Suppl. 98:2001;800a. b.
    • (2001) Blood Suppl. , vol.98
    • Ayton, P.M.1    Cleary, M.L.2
  • 4
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • Bird A. DNA methylation patterns and epigenetic memory. Genes Dev. 16:2002;6-21.
    • (2002) Genes Dev. , vol.16 , pp. 6-21
    • Bird, A.1
  • 5
    • 0033601073 scopus 로고    scopus 로고
    • Methylation-induced repression - Belts, braces, and chromatin
    • Bird A.P., Wolffe A.P. Methylation-induced repression - belts, braces, and chromatin. Cell. 99:1999;451-454.
    • (1999) Cell , vol.99 , pp. 451-454
    • Bird, A.P.1    Wolffe, A.P.2
  • 6
    • 0037082439 scopus 로고    scopus 로고
    • The MT domain of the proto-oncoprotein MLL binds to CpG-containing DNA and discriminates against methylation
    • Birke M., Schreiner S., Garcia-Cuellar M.P., Mahr K., Titgemeyer F., Slany R.K. The MT domain of the proto-oncoprotein MLL binds to CpG-containing DNA and discriminates against methylation. Nucleic Acids Res. 30:2002;958-965.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 958-965
    • Birke, M.1    Schreiner, S.2    Garcia-Cuellar, M.P.3    Mahr, K.4    Titgemeyer, F.5    Slany, R.K.6
  • 8
    • 0035833726 scopus 로고    scopus 로고
    • General transcription factors bind promoters repressed by Polycomb group proteins
    • Breiling A., Turner B.M., Bianchi M.E., Orlando V. General transcription factors bind promoters repressed by Polycomb group proteins. Nature. 412:2001;651-655.
    • (2001) Nature , vol.412 , pp. 651-655
    • Breiling, A.1    Turner, B.M.2    Bianchi, M.E.3    Orlando, V.4
  • 9
    • 0035313867 scopus 로고    scopus 로고
    • The Polycomb group - No longer an exclusive club?
    • Brock H.W., van Lohuizen M. The Polycomb group - no longer an exclusive club? Curr. Opin. Genet. Dev. 11:2001;175-181.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 175-181
    • Brock, H.W.1    Van Lohuizen, M.2
  • 10
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in polycomb-group silencing
    • in press. Published online September 26, 2002. 10.1126/science.1076997
    • Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y. Role of histone H3 lysine 27 methylation in polycomb-group silencing. Science. in press. 2002;. Published online September 26, 2002. 10.1126/science.1076997.
    • (2002) Science
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6    Jones, R.S.7    Zhang, Y.8
  • 11
    • 0033615616 scopus 로고    scopus 로고
    • Epigenetic inheritance of active chromatin after removal of the main transactivator
    • Cavalli G., Paro R. Epigenetic inheritance of active chromatin after removal of the main transactivator. Science. 286:1999;955-958.
    • (1999) Science , vol.286 , pp. 955-958
    • Cavalli, G.1    Paro, R.2
  • 13
    • 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., 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
  • 14
    • 0035102477 scopus 로고    scopus 로고
    • MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein
    • Ernst P., Wang J., Huang M., Goodman R.H., Korsmeyer S.J. MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein. Mol. Cell. Biol. 21:2001;2249-2258.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2249-2258
    • Ernst, P.1    Wang, J.2    Huang, M.3    Goodman, R.H.4    Korsmeyer, S.J.5
  • 15
    • 0037040543 scopus 로고    scopus 로고
    • Transcription. Unlocking the gates to gene expression
    • Fry C.J., Peterson C.L. Transcription. Unlocking the gates to gene expression. Science. 295:2002;1847-1848.
    • (2002) Science , vol.295 , pp. 1847-1848
    • Fry, C.J.1    Peterson, C.L.2
  • 17
    • 0036593394 scopus 로고    scopus 로고
    • Histone methyltransferases, diet nutrients and tumour suppressors
    • Huang S. Histone methyltransferases, diet nutrients and tumour suppressors. Nat. Rev. Cancer. 2:2002;469-476.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 469-476
    • Huang, S.1
  • 18
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., 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
  • 20
    • 0035449377 scopus 로고    scopus 로고
    • A homeotic mutation in the trithorax SET domain impedes histone binding
    • Katsani K.R., Arredondo J.J., Kal A.J., Verrijzer C.P. A homeotic mutation in the trithorax SET domain impedes histone binding. Genes Dev. 15:2001;2197-2202.
    • (2001) Genes Dev. , vol.15 , pp. 2197-2202
    • Katsani, K.R.1    Arredondo, J.J.2    Kal, A.J.3    Verrijzer, C.P.4
  • 21
    • 0032126633 scopus 로고    scopus 로고
    • Hoxa9 transforms primary bone marrow cells through specific collaboration with Meis1a but not Pbx1b
    • Kroon E., Krosl J., Thorsteinsdottir U., Baban S., Buchberg A.M., Sauvageau G. Hoxa9 transforms primary bone marrow cells through specific collaboration with Meis1a but not Pbx1b. EMBO J. 17:1998;3714-3725.
    • (1998) EMBO J. , vol.17 , pp. 3714-3725
    • Kroon, E.1    Krosl, J.2    Thorsteinsdottir, U.3    Baban, S.4    Buchberg, A.M.5    Sauvageau, G.6
  • 22
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multi-protein complex containing the enhancer of Zeste protein
    • in press
    • Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D. Histone methyltransferase activity associated with a human multi-protein complex containing the enhancer of Zeste protein. Genes Dev. in press:2002.
    • (2002) Genes Dev.
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.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. 14:2002;286-298.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 24
    • 0032949304 scopus 로고    scopus 로고
    • Molecular genetics of acute promyelocytic leukemia
    • Lin R.J., Egan D.A., Evans R.M. Molecular genetics of acute promyelocytic leukemia. Trends Genet. 15:1999;179-184.
    • (1999) Trends Genet. , vol.15 , pp. 179-184
    • Lin, R.J.1    Egan, D.A.2    Evans, R.M.3
  • 25
    • 0030729371 scopus 로고    scopus 로고
    • Effects of HOX homeobox genes in blood cell differentiation
    • Magli M.C., Largman C., Lawrence H.J. Effects of HOX homeobox genes in blood cell differentiation. J. Cell. Physiol. 173:1997;168-177.
    • (1997) J. Cell. Physiol. , vol.173 , pp. 168-177
    • Magli, M.C.1    Largman, C.2    Lawrence, H.J.3
  • 27
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan X., Ng H.H., Johnson C.A., Laherty C.D., Turner B.M., Eisenman R.N., Bird A. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature. 393:1998;386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 28
    • 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 C.D., Tempst P., Reinberg D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16:2002;479-489.
    • (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
    • 0034161329 scopus 로고    scopus 로고
    • Mapping chromosomal proteins in vivo by formaldehyde-crosslinked-chromatin immunoprecipitation
    • Orlando V. Mapping chromosomal proteins in vivo by formaldehyde-crosslinked-chromatin immunoprecipitation. Trends Biochem. Sci. 25:2000;99-104.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 99-104
    • Orlando, V.1
  • 30
    • 0032169352 scopus 로고    scopus 로고
    • Binding of trithorax and Polycomb proteins to the bithorax complex: Dynamic changes during early Drosophila embryogenesis
    • Orlando V., Jane E.P., Chinwalla V., Harte P.J., Paro R. Binding of trithorax and Polycomb proteins to the bithorax complex. dynamic changes during early Drosophila embryogenesis EMBO J. 17:1998;5141-5150.
    • (1998) EMBO J. , vol.17 , pp. 5141-5150
    • Orlando, V.1    Jane, E.P.2    Chinwalla, V.3    Harte, P.J.4    Paro, R.5
  • 32
    • 0036142691 scopus 로고    scopus 로고
    • Differential expression of Hox, Meis1, and Pbx1 genes in primitive cells throughout murine hematopoietic ontogeny
    • Pineault N., Helgason C.D., Lawrence H.J., Humphries R.K. Differential expression of Hox, Meis1, and Pbx1 genes in primitive cells throughout murine hematopoietic ontogeny. Exp. Hematol. 30:2002;49-57.
    • (2002) Exp. Hematol. , vol.30 , pp. 49-57
    • Pineault, N.1    Helgason, C.D.2    Lawrence, H.J.3    Humphries, R.K.4
  • 33
    • 0036337565 scopus 로고    scopus 로고
    • The Drosophila trithorax protein is a coactivator required to prevent re-establishment of polycomb silencing
    • Poux S., Horard B., Sigrist C.J., Pirrotta V. The Drosophila trithorax protein is a coactivator required to prevent re-establishment of polycomb silencing. Development. 129:2002;2483-2493.
    • (2002) Development , vol.129 , pp. 2483-2493
    • Poux, S.1    Horard, B.2    Sigrist, C.J.3    Pirrotta, V.4
  • 38
  • 39
    • 0029590307 scopus 로고
    • Regulation of Hoxc-8 during mouse embryonic development: Identification and characterization of critical elements involved in early neural tube expression
    • Shashikant C.S., Bieberich C.J., Belting H.G., Wang J.C., Borbely M.A., Ruddle F.H. Regulation of Hoxc-8 during mouse embryonic development. identification and characterization of critical elements involved in early neural tube expression Development. 121:1995;4339-4347.
    • (1995) Development , vol.121 , pp. 4339-4347
    • Shashikant, C.S.1    Bieberich, C.J.2    Belting, H.G.3    Wang, J.C.4    Borbely, M.A.5    Ruddle, F.H.6
  • 41
    • 0036532114 scopus 로고    scopus 로고
    • Programming off and on states in chromatin: Mechanisms of Polycomb and trithorax group complexes
    • Simon J.A., Tamkun J.W. Programming off and on states in chromatin. mechanisms of Polycomb and trithorax group complexes Curr. Opin. Genet. Dev. 12:2002;210-218.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 210-218
    • Simon, J.A.1    Tamkun, J.W.2
  • 42
    • 0035141264 scopus 로고    scopus 로고
    • The Drosophila Polycomb Group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3
    • Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J. The Drosophila Polycomb Group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3. Development. 128:2001;275-286.
    • (2001) Development , vol.128 , pp. 275-286
    • Tie, F.1    Furuyama, T.2    Prasad-Sinha, J.3    Jane, E.4    Harte, P.J.5
  • 43
    • 0032751323 scopus 로고    scopus 로고
    • Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation
    • van der Vlag J., Otte A.P. Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation. Nat. Genet. 23:1999;474-478.
    • (1999) Nat. Genet. , vol.23 , pp. 474-478
    • Van der Vlag, J.1    Otte, A.P.2
  • 44
    • 0035962668 scopus 로고    scopus 로고
    • Methyl CpG binding proteins: Coupling chromatin architecture to gene regulation
    • Wade P.A. Methyl CpG binding proteins. coupling chromatin architecture to gene regulation Oncogene. 20:2001;3166-3173.
    • (2001) Oncogene , vol.20 , pp. 3166-3173
    • Wade, P.A.1
  • 45
    • 0032169858 scopus 로고    scopus 로고
    • ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex
    • Wang J., Hoshino T., Redner R.L., Kajigaya S., Liu J.M. ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex. Proc. Natl. Acad. Sci. USA. 95:1998;10860-10865.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10860-10865
    • Wang, J.1    Hoshino, T.2    Redner, R.L.3    Kajigaya, S.4    Liu, J.M.5
  • 46
    • 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. 8:2001;1207-1217.
    • (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
  • 47
    • 79960970919 scopus 로고    scopus 로고
    • MLL repression domain activity is mediated through histone deacetylases, HPC2, BMI-1, and CtBP
    • Xia Z.-B., Zeleznik-Le N.J. MLL repression domain activity is mediated through histone deacetylases, HPC2, BMI-1, and CtBP. Blood Suppl. 98:2001;800a.
    • (2001) Blood Suppl. , vol.98
    • Xia, Z.-B.1    Zeleznik-Le, N.J.2
  • 50
    • 0028869112 scopus 로고
    • Altered Hox expression and segmental identity in Mll-mutant mice
    • Yu B.D., Hess J.L., Horning S.E., Brown G.A., Korsmeyer S.J. Altered Hox expression and segmental identity in Mll-mutant mice. Nature. 378:1995;505-508.
    • (1995) Nature , vol.378 , pp. 505-508
    • Yu, B.D.1    Hess, J.L.2    Horning, S.E.3    Brown, G.A.4    Korsmeyer, S.J.5
  • 51
    • 0032168459 scopus 로고    scopus 로고
    • MLL, a mammalian trithorax-group gene, functions as a transcriptional maintenance factor in morphogenesis
    • Yu B.D., Hanson R.D., Hess J.L., Horning S.E., Korsmeyer S.J. MLL, a mammalian trithorax-group gene, functions as a transcriptional maintenance factor in morphogenesis. Proc. Natl. Acad. Sci. USA. 95:1998;10632-10636.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10632-10636
    • Yu, B.D.1    Hanson, R.D.2    Hess, J.L.3    Horning, S.E.4    Korsmeyer, S.J.5
  • 52
    • 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. 277:2002;11621-11624.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 53
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.