메뉴 건너뛰기




Volumn 19, Issue 11, 2012, Pages 1155-1160

Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation

Author keywords

[No Author keywords available]

Indexed keywords

DNA METHYLTRANSFERASE 1; HISTONE H3; LYSINE; UBIQUITIN LIKE PHD AND RING FINGER DOMAIN CONTAINING 1; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84869087517     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2391     Document Type: Article
Times cited : (290)

References (39)
  • 1
    • 0016221697 scopus 로고
    • Chromatin structure: A repeating unit of histones and DNA
    • Kornberg, R.D. Chromatin structure: a repeating unit of histones and DNA. Science 184, 868-871 (1974).
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 3
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A° resolution
    • DOI 10.1038/38444
    • Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F. & Richmond, T.J. Crystal structure of the nucleosome core particle at 2.8-A° resolution. Nature 389, 251-260 (1997). (Pubitemid 27406632)
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 4
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • DOI 10.1016/j.cell.2007.02.005, PII S0092867407001845
    • Kouzarides, T. Chromatin modifications and their function. Cell 128, 693-705 (2007). (Pubitemid 46273577)
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 5
    • 80052942443 scopus 로고    scopus 로고
    • Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification
    • Tan, M. et al. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146, 1016-1028 (2011).
    • (2011) Cell , vol.146 , pp. 1016-1028
    • Tan, M.1
  • 6
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • DOI 10.1126/science.1124000
    • Shogren-Knaak, M. et al. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311, 844-847 (2006). (Pubitemid 43228847)
    • (2006) Science , vol.311 , Issue.5762 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.-M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 7
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • DOI 10.1038/nsmb1338, PII NSMB1338
    • Taverna, S.D., Li, H., Ruthenburg, A.J., Allis, C.D. & Patel, D.J. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nat. Struct. Mol. Biol. 14, 1025-1040 (2007). (Pubitemid 350060344)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 8
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • DOI 10.1038/47412
    • Strahl, B.D. & Allis, C.D. The language of covalent histone modifications. Nature 403, 41-45 (2000). (Pubitemid 30038513)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 9
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein, T. & Allis, C.D. Translating the histone code. Science 293, 1074-1080 (2001). (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 10
    • 84863986133 scopus 로고    scopus 로고
    • Functions of DNA methylation: Islands, start sites, gene bodies and beyond
    • Jones, P.A. Functions of DNA methylation: islands, start sites, gene bodies and beyond. Nat. Rev. Genet. 13, 484-492 (2012).
    • (2012) Nat. Rev. Genet , vol.13 , pp. 484-492
    • Jones, P.A.1
  • 11
    • 0035891265 scopus 로고    scopus 로고
    • A histone H3 methyltransferase controls DNA methylation in Neurospora crassa
    • DOI 10.1038/35104508
    • Tamaru, H. & Selker, E.U. A histone H3 methyltransferase controls DNA methylation in Neurospora crassa. Nature 414, 277-283 (2001). (Pubitemid 33097798)
    • (2001) Nature , vol.414 , Issue.6861 , pp. 277-283
    • Tamaru, H.1    Selker, E.U.2
  • 12
    • 0037041422 scopus 로고    scopus 로고
    • Control of CpNpG DNA methylation by the KRYPTONITE histone H3 methyltransferase
    • DOI 10.1038/nature731
    • Jackson, J.P., Lindroth, A.M., Cao, X. & Jacobsen, S.E. Control of CpNpG DNA methylation by the KRYPTONITE histone H3 methyltransferase. Nature 416, 556-560 (2002). (Pubitemid 34288860)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 556-560
    • Jackson, J.P.1    Lindroth, A.M.2    Cao, X.3    Jacobsen, S.E.4
  • 14
    • 67349190247 scopus 로고    scopus 로고
    • Linking DNA methylation and histone modification: Patterns and paradigms
    • Cedar, H. & Bergman, Y. Linking DNA methylation and histone modification: patterns and paradigms. Nat. Rev. Genet. 10, 295-304 (2009).
    • (2009) Nat. Rev. Genet , vol.10 , pp. 295-304
    • Cedar, H.1    Bergman, Y.2
  • 15
    • 34648833002 scopus 로고    scopus 로고
    • UHRF1 plays a role in maintaining DNA methylation in mammalian cells
    • DOI 10.1126/science.1147939
    • Bostick, M. et al. UHRF1 plays a role in maintaining DNA methylation in mammalian cells. Science 317, 1760-1764 (2007). (Pubitemid 47461842)
    • (2007) Science , vol.317 , Issue.5845 , pp. 1760-1764
    • Bostick, M.1    Jong, K.K.2    Esteve, P.-O.3    Clark, A.4    Pradhan, S.5    Jacobsen, S.E.6
  • 17
    • 53649097070 scopus 로고    scopus 로고
    • Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
    • Arita, K., Ariyoshi, M., Tochio, H., Nakamura, Y. & Shirakawa, M. Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism. Nature 455, 818-821 (2008).
    • (2008) Nature , vol.455 , pp. 818-821
    • Arita, K.1    Ariyoshi, M.2    Tochio, H.3    Nakamura, Y.4    Shirakawa, M.5
  • 18
    • 53649088595 scopus 로고    scopus 로고
    • Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1
    • Avvakumov, G.V. et al. Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1. Nature 455, 822-825 (2008).
    • (2008) Nature , vol.455 , pp. 822-825
    • Avvakumov, G.V.1
  • 19
    • 53649089723 scopus 로고    scopus 로고
    • The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix
    • Hashimoto, H. et al. The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix. Nature 455, 826-829 (2008).
    • (2008) Nature , vol.455 , pp. 826-829
    • Hashimoto, H.1
  • 20
    • 79959869345 scopus 로고    scopus 로고
    • Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein
    • Nady, N. et al. Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein. J. Biol. Chem. 286, 24300-24311 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 24300-24311
    • Nady, N.1
  • 21
    • 33745727065 scopus 로고    scopus 로고
    • Histone modification and the control of heterochromatic gene silencing in Drosophila
    • Ebert, A., Lein, S., Schotta, G. & Reuter, G. Histone modification and the control of heterochromatic gene silencing in Drosophila. Chromosome Res. 14, 377-392 (2006).
    • (2006) Chromosome Res , vol.14 , pp. 377-392
    • Ebert, A.1    Lein, S.2    Schotta, G.3    Reuter, G.4
  • 22
    • 34249304470 scopus 로고    scopus 로고
    • Transcription and RNA interference in the formation of heterochromatin
    • DOI 10.1038/nature05914, PII NATURE05914
    • Grewal, S.I. & Elgin, S.C. Transcription and RNA interference in the formation of heterochromatin. Nature 447, 399-406 (2007). (Pubitemid 46816745)
    • (2007) Nature , vol.447 , Issue.7143 , pp. 399-406
    • Grewal, S.I.S.1    Elgin, S.C.R.2
  • 23
    • 77953809032 scopus 로고    scopus 로고
    • Distinct epigenomic landscapes of pluripotent and lineage-committed human cells
    • Hawkins, R.D. et al. Distinct epigenomic landscapes of pluripotent and lineage-committed human cells. Cell Stem Cell 6, 479-491 (2010).
    • (2010) Cell Stem Cell , vol.6 , pp. 479-491
    • Hawkins, R.D.1
  • 24
    • 79955583542 scopus 로고    scopus 로고
    • Mapping and analysis of chromatin state dynamics in nine human cell types
    • Ernst, J. et al. Mapping and analysis of chromatin state dynamics in nine human cell types. Nature 473, 43-49 (2011).
    • (2011) Nature , vol.473 , pp. 43-49
    • Ernst, J.1
  • 26
    • 79151470871 scopus 로고    scopus 로고
    • Influence of combinatorial histone modifications on antibody and effector protein recognition
    • Fuchs, S.M., Krajewski, K., Baker, R.W., Miller, V.L. & Strahl, B.D. Influence of combinatorial histone modifications on antibody and effector protein recognition. Curr. Biol. 21, 53-58 (2011).
    • (2011) Curr. Biol , vol.21 , pp. 53-58
    • Fuchs, S.M.1    Krajewski, K.2    Baker, R.W.3    Miller, V.L.4    Strahl, B.D.5
  • 27
    • 80052140473 scopus 로고    scopus 로고
    • Application of Celluspots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails
    • Bock, I. et al. Application of Celluspots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails. BMC Biochem. 12, 48 (2011).
    • (2011) BMC Biochem , vol.12 , pp. 48
    • Bock, I.1
  • 28
    • 77949874334 scopus 로고    scopus 로고
    • Combinatorial profiling of chromatin-binding modules reveals multisite discrimination
    • Garske, A.L. et al. Combinatorial profiling of chromatin-binding modules reveals multisite discrimination. Nat. Chem. Biol. 6, 283-290 (2010).
    • (2010) Nat. Chem. Biol , vol.6 , pp. 283-290
    • Garske, A.L.1
  • 30
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • DOI 10.1038/nature04254
    • Hirota, T., Lipp, J.J., Toh, B.H. & Peters, J.M. Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 438, 1176-1180 (2005). (Pubitemid 41831689)
    • (2005) Nature , vol.438 , Issue.7071 , pp. 1176-1180
    • Hirota, T.1    Lipp, J.J.2    Toh, B.-H.3    Peters, J.-M.4
  • 31
    • 79955468817 scopus 로고    scopus 로고
    • Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: Potential effect of phosphorylation on methyl-lysine binding
    • Chang, Y., Horton, J.R., Bedford, M.T., Zhang, X. & Cheng, X. Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: potential effect of phosphorylation on methyl-lysine binding. J. Mol. Biol. 408, 807-814 (2011).
    • (2011) J. Mol. Biol , vol.408 , pp. 807-814
    • Chang, Y.1    Horton, J.R.2    Bedford, M.T.3    Zhang, X.4    Cheng, X.5
  • 32
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • DOI 10.1126/science.1069473
    • Jacobs, S.A. & Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080-2083 (2002). (Pubitemid 34229471)
    • (2002) Science , vol.295 , Issue.5562 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 33
    • 79960464001 scopus 로고    scopus 로고
    • PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression
    • Rajakumara, E. et al. PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression. Mol. Cell 43, 275-284 (2011).
    • (2011) Mol. Cell , vol.43 , pp. 275-284
    • Rajakumara, E.1
  • 34
    • 70349322609 scopus 로고    scopus 로고
    • Selective anchoring of DNA methyltransferases 3A and 3B to nucleosomes containing methylated DNA
    • Jeong, S. et al. Selective anchoring of DNA methyltransferases 3A and 3B to nucleosomes containing methylated DNA. Mol. Cell. Biol. 29, 5366-5376 (2009).
    • (2009) Mol. Cell. Biol , vol.29 , pp. 5366-5376
    • Jeong, S.1
  • 37
    • 79952258043 scopus 로고    scopus 로고
    • Nucleosomes containing methylated DNA stabilize DNA methyltransferases 3A/3B and ensure faithful epigenetic inheritance
    • Sharma, S., De Carvalho, D.D., Jeong, S., Jones, P.A. & Liang, G. Nucleosomes containing methylated DNA stabilize DNA methyltransferases 3A/3B and ensure faithful epigenetic inheritance. PLoS Genet. 7, e1001286 (2011).
    • (2011) PLoS Genet , vol.7
    • Sharma, S.1    De Carvalho, D.D.2    Jeong, S.3    Jones, P.A.4    Liang, G.5
  • 38
    • 84862818911 scopus 로고    scopus 로고
    • The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier-Gorlin syndrome
    • Kuo, A.J. et al. The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier-Gorlin syndrome. Nature 484, 115-119 (2012).
    • (2012) Nature , vol.484 , pp. 115-119
    • Kuo, A.J.1
  • 39
    • 77951850381 scopus 로고    scopus 로고
    • BISMA-fast and accurate bisulfite sequencing data analysis of individual clones from unique and repetitive sequences
    • Rohde, C., Zhang, Y., Reinhardt, R. & Jeltsch, A. BISMA-fast and accurate bisulfite sequencing data analysis of individual clones from unique and repetitive sequences. BMC Bioinformatics 11, 230 (2010).
    • (2010) BMC Bioinformatics , vol.11 , pp. 230
    • Rohde, C.1    Zhang, Y.2    Reinhardt, R.3    Jeltsch, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.