메뉴 건너뛰기




Volumn 49, Issue 44, 2010, Pages 9438-9448

Inhibition of chromatin remodeling by polycomb group protein posterior sex combs is mechanistically distinct from nucleosome binding

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL REGIONS; CHROMATIN REMODELING; CHROMATIN STRUCTURE; COMPLEX 1; E3 LIGASE; GENE SILENCING; IN-VIVO; LINKER DNA; MONONUCLEOSOMES; NONCOVALENT; NUCLEOSOMES; PCG PROTEINS; POLYCOMB; POLYCOMB GROUP; POLYCOMB GROUP PROTEINS; UBIQUITYLATION;

EID: 78149296778     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100532a     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 0021880669 scopus 로고
    • A group of genes controlling the spatial expression of the bithorax complex in Drosophila
    • Jurgens, G. (1985) A group of genes controlling the spatial expression of the bithorax complex in Drosophila Nature 316, 153-155
    • (1985) Nature , vol.316 , pp. 153-155
    • Jurgens, G.1
  • 2
    • 0018240421 scopus 로고
    • A gene complex controlling segmentation in Drosophila
    • Lewis, E. B. (1978) A gene complex controlling segmentation in Drosophila Nature 276 (5688) 565-570
    • (1978) Nature , vol.276 , Issue.5688 , pp. 565-570
    • Lewis, E.B.1
  • 3
    • 33847084602 scopus 로고    scopus 로고
    • Genome regulation by polycomb and trithorax proteins
    • Schuettengruber, B. 2007, Genome regulation by polycomb and trithorax proteins Cell 128 (4) 735-745
    • (2007) Cell , vol.128 , Issue.4 , pp. 735-745
    • Schuettengruber, B.1
  • 4
    • 8844265508 scopus 로고    scopus 로고
    • Epigenetic regulation of cellular memory by the Polycomb and Trithorax group proteins
    • Ringrose, L. and Paro, R. (2004) Epigenetic regulation of cellular memory by the Polycomb and Trithorax group proteins Annu. Rev. Genet. 38, 413-443
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 413-443
    • Ringrose, L.1    Paro, R.2
  • 5
    • 33746069681 scopus 로고    scopus 로고
    • Dosage compensation in mammals: Fine-tuning the expression of the X chromosome
    • Heard, E. and Disteche, C. M. (2006) Dosage compensation in mammals: Fine-tuning the expression of the X chromosome Genes Dev. 20 (14) 1848-1867
    • (2006) Genes Dev. , vol.20 , Issue.14 , pp. 1848-1867
    • Heard, E.1    Disteche, C.M.2
  • 6
    • 1942471150 scopus 로고    scopus 로고
    • Epigenetic regulation of mammalian genomic imprinting
    • Delaval, K. and Feil, R. (2004) Epigenetic regulation of mammalian genomic imprinting Curr. Opin. Genet. Dev. 14 (2) 188-195
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , Issue.2 , pp. 188-195
    • Delaval, K.1    Feil, R.2
  • 7
    • 33845799903 scopus 로고    scopus 로고
    • Polycomb silencing mechanisms and the management of genomic programmes
    • Schwartz, Y. B. and Pirrotta, V. (2007) Polycomb silencing mechanisms and the management of genomic programmes Nat. Rev. Genet. 8 (1) 9-22
    • (2007) Nat. Rev. Genet. , vol.8 , Issue.1 , pp. 9-22
    • Schwartz, Y.B.1    Pirrotta, V.2
  • 8
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: Knowns and unknowns
    • Simon, J. A. and Kingston, R. E. (2009) Mechanisms of polycomb gene silencing: Knowns and unknowns Nat. Rev. Mol. Cell Biol. 10 (10) 697-708
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , Issue.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 9
    • 9444244427 scopus 로고    scopus 로고
    • Chromatin compaction by a polycomb group protein complex
    • Francis, N. J., Kingston, R. E., and Woodcock, C. L. (2004) Chromatin compaction by a polycomb group protein complex Science 306 (5701) 1574-1577
    • (2004) Science , vol.306 , Issue.5701 , pp. 1574-1577
    • Francis, N.J.1    Kingston, R.E.2    Woodcock, C.L.3
  • 10
    • 0036839671 scopus 로고    scopus 로고
    • Native and recombinant polycomb group complexes establish a selective block to template accessibility to repress transcription in vitro
    • King, I. F., Francis, N. J., and Kingston, R. E. (2002) Native and recombinant polycomb group complexes establish a selective block to template accessibility to repress transcription in vitro Mol. Cell. Biol. 22 (22) 7919-7928
    • (2002) Mol. Cell. Biol. , vol.22 , Issue.22 , pp. 7919-7928
    • King, I.F.1    Francis, N.J.2    Kingston, R.E.3
  • 11
    • 0033538578 scopus 로고    scopus 로고
    • Stabilization of chromatin structure by PRC1, a Polycomb complex
    • Shao, Z. 1999, Stabilization of chromatin structure by PRC1, a Polycomb complex Cell 98 (1) 37-46
    • (1999) Cell , vol.98 , Issue.1 , pp. 37-46
    • Shao, Z.1
  • 12
    • 55949132133 scopus 로고    scopus 로고
    • Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms
    • Margueron, R. 2008, Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms Mol. Cell 32 (4) 503-518
    • (2008) Mol. Cell , vol.32 , Issue.4 , pp. 503-518
    • Margueron, R.1
  • 13
    • 33749054895 scopus 로고    scopus 로고
    • Architecture of a polycomb nucleoprotein complex
    • Mohd-Sarip, A. 2006, Architecture of a polycomb nucleoprotein complex Mol. Cell 24 (1) 91-100
    • (2006) Mol. Cell , vol.24 , Issue.1 , pp. 91-100
    • Mohd-Sarip, A.1
  • 14
    • 0034785891 scopus 로고    scopus 로고
    • Reconstitution of a functional core polycomb repressive complex
    • Francis, N. J. 2001, Reconstitution of a functional core polycomb repressive complex Mol. Cell 8 (3) 545-556
    • (2001) Mol. Cell , vol.8 , Issue.3 , pp. 545-556
    • Francis, N.J.1
  • 15
    • 0035833718 scopus 로고    scopus 로고
    • A Drosophila Polycomb group complex includes Zeste and dTAFII proteins
    • Saurin, A. J. 2001, A Drosophila Polycomb group complex includes Zeste and dTAFII proteins Nature 412 (6847) 655-660
    • (2001) Nature , vol.412 , Issue.6847 , pp. 655-660
    • Saurin, A.J.1
  • 16
    • 0036340237 scopus 로고    scopus 로고
    • The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans
    • Levine, S. S. 2002, The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans Mol. Cell. Biol. 22 (17) 6070-6078
    • (2002) Mol. Cell. Biol. , vol.22 , Issue.17 , pp. 6070-6078
    • Levine, S.S.1
  • 17
    • 1242339582 scopus 로고    scopus 로고
    • Propagation of silencing; Recruitment and repression of naive chromatin in trans by polycomb repressed chromatin
    • Lavigne, M. 2004, Propagation of silencing; recruitment and repression of naive chromatin in trans by polycomb repressed chromatin Mol. Cell 13 (3) 415-425
    • (2004) Mol. Cell , vol.13 , Issue.3 , pp. 415-425
    • Lavigne, M.1
  • 18
    • 22544485646 scopus 로고    scopus 로고
    • Analysis of a polycomb group protein defines regions that link repressive activity on nucleosomal templates to in vivo function
    • King, I. F. 2005, Analysis of a polycomb group protein defines regions that link repressive activity on nucleosomal templates to in vivo function Mol. Cell. Biol. 25 (15) 6578-6591
    • (2005) Mol. Cell. Biol. , vol.25 , Issue.15 , pp. 6578-6591
    • King, I.F.1
  • 19
    • 70350153310 scopus 로고    scopus 로고
    • Molecular genetic analysis of Suppressor 2 of zeste identifies key functional domains
    • Emmons, R. B. 2009, Molecular genetic analysis of Suppressor 2 of zeste identifies key functional domains Genetics 182 (4) 999-1013
    • (2009) Genetics , vol.182 , Issue.4 , pp. 999-1013
    • Emmons, R.B.1
  • 20
    • 0035073765 scopus 로고    scopus 로고
    • Polycomb group proteins and heritable silencing of Drosophila Hox genes
    • Beuchle, D., Struhl, G., and Muller, J. (2001) Polycomb group proteins and heritable silencing of Drosophila Hox genes Development 128 (6) 993-1004
    • (2001) Development , vol.128 , Issue.6 , pp. 993-1004
    • Beuchle, D.1    Struhl, G.2    Muller, J.3
  • 21
    • 0028960417 scopus 로고
    • A genetic analysis of the Suppressor 2 of zeste complex of Drosophila melanogaster
    • Wu, C. T. and Howe, M. (1995) A genetic analysis of the Suppressor 2 of zeste complex of Drosophila melanogaster Genetics 140 (1) 139-181
    • (1995) Genetics , vol.140 , Issue.1 , pp. 139-181
    • Wu, C.T.1    Howe, M.2
  • 22
    • 58249119616 scopus 로고    scopus 로고
    • Polycomb group protein Suppressor 2 of zeste is a functional homolog of Posterior Sex Combs
    • Lo, S. M., Ahuja, N. K., and Francis, N. J. (2009) Polycomb group protein Suppressor 2 of zeste is a functional homolog of Posterior Sex Combs Mol. Cell. Biol. 29 (2) 515-525
    • (2009) Mol. Cell. Biol. , vol.29 , Issue.2 , pp. 515-525
    • Lo, S.M.1    Ahuja, N.K.2    Francis, N.J.3
  • 23
    • 0025914005 scopus 로고
    • Drosophila genes Posterior Sex Combs and Suppressor two of zeste encode proteins with homology to the murine bmi-1 oncogene
    • Brunk, B. P., Martin, E. C., and Adler, P. N. (1991) Drosophila genes Posterior Sex Combs and Suppressor two of zeste encode proteins with homology to the murine bmi-1 oncogene Nature 353 (6342) 351-353
    • (1991) Nature , vol.353 , Issue.6342 , pp. 351-353
    • Brunk, B.P.1    Martin, E.C.2    Adler, P.N.3
  • 24
    • 54349083294 scopus 로고    scopus 로고
    • DKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing
    • Lagarou, A. 2008, dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing Genes Dev. 22 (20) 2799-2810
    • (2008) Genes Dev. , vol.22 , Issue.20 , pp. 2799-2810
    • Lagarou, A.1
  • 25
    • 33746008541 scopus 로고    scopus 로고
    • Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex
    • Li, Z. 2006, Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex J. Biol. Chem. 281 (29) 20643-20649
    • (2006) J. Biol. Chem. , vol.281 , Issue.29 , pp. 20643-20649
    • Li, Z.1
  • 26
    • 33745753378 scopus 로고    scopus 로고
    • Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b
    • Buchwald, G. 2006, Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b EMBO J. 25 (11) 2465-2474
    • (2006) EMBO J. , vol.25 , Issue.11 , pp. 2465-2474
    • Buchwald, G.1
  • 27
    • 33751515474 scopus 로고    scopus 로고
    • The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity
    • Ben-Saadon, R. 2006, The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity Mol. Cell 24 (5) 701-711
    • (2006) Mol. Cell , vol.24 , Issue.5 , pp. 701-711
    • Ben-Saadon, R.1
  • 28
    • 0032530154 scopus 로고    scopus 로고
    • Mitotic inactivation of a human SWI/SNF chromatin remodeling complex
    • Sif, S. 1998, Mitotic inactivation of a human SWI/SNF chromatin remodeling complex Genes Dev. 12 (18) 2842-2851
    • (1998) Genes Dev. , vol.12 , Issue.18 , pp. 2842-2851
    • Sif, S.1
  • 29
    • 0020695571 scopus 로고
    • Structural features of a phased nucleosome core particle
    • Simpson, R. T. and Stafford, D. W. (1983) Structural features of a phased nucleosome core particle Proc. Natl. Acad. Sci. U.S.A. 80 (1) 51-55
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , Issue.1 , pp. 51-55
    • Simpson, R.T.1    Stafford, D.W.2
  • 30
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • Lowary, P. T. and Widom, J. (1998) New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning J. Mol. Biol. 276 (1) 19-42
    • (1998) J. Mol. Biol. , vol.276 , Issue.1 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 31
    • 39549115045 scopus 로고    scopus 로고
    • Assembly of nucleosomal templates by salt dialysis
    • Chapter 21, Unit 21.6, Wiley, New York
    • Lee, K. M. and Narlikar, G. (2001) Assembly of nucleosomal templates by salt dialysis. Current Protocols in Molecular Biology, Chapter 21, Unit 21.6, Wiley, New York.
    • (2001) Current Protocols in Molecular Biology
    • Lee, K.M.1    Narlikar, G.2
  • 32
    • 0035281938 scopus 로고    scopus 로고
    • Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes
    • Sif, S. 2001, Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes Genes Dev. 15 (5) 603-618
    • (2001) Genes Dev. , vol.15 , Issue.5 , pp. 603-618
    • Sif, S.1
  • 33
    • 0033067219 scopus 로고    scopus 로고
    • Assembly of defined nucleosomal and chromatin arrays from pure components
    • Carruthers, L. M. 1999, Assembly of defined nucleosomal and chromatin arrays from pure components Methods Enzymol. 304, 19-35
    • (1999) Methods Enzymol. , vol.304 , pp. 19-35
    • Carruthers, L.M.1
  • 34
    • 0002470839 scopus 로고    scopus 로고
    • Preparation of nuclear and cytoplasmic extracts from mammalian cells
    • Chapter 12, Unit 12.1, Wiley, New York
    • Abmayr, S. M., (2006) Preparation of nuclear and cytoplasmic extracts from mammalian cells. Current Protocols in Molecular Biology, Chapter 12, Unit 12.1, Wiley, New York.
    • (2006) Current Protocols in Molecular Biology
    • Abmayr, S.M.1
  • 35
    • 0035691979 scopus 로고    scopus 로고
    • Generation and interconversion of multiple distinct nucleosomal states as a mechanism for catalyzing chromatin fluidity
    • Narlikar, G. J., Phelan, M. L., and Kingston, R. E. (2001) Generation and interconversion of multiple distinct nucleosomal states as a mechanism for catalyzing chromatin fluidity Mol. Cell 8 (6) 1219-1230
    • (2001) Mol. Cell , vol.8 , Issue.6 , pp. 1219-1230
    • Narlikar, G.J.1    Phelan, M.L.2    Kingston, R.E.3
  • 36
    • 33750442129 scopus 로고    scopus 로고
    • Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II
    • Bondarenko, V. A. 2006, Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II Mol. Cell 24 (3) 469-479
    • (2006) Mol. Cell , vol.24 , Issue.3 , pp. 469-479
    • Bondarenko, V.A.1
  • 37
    • 0037225966 scopus 로고    scopus 로고
    • Dimerization of the Polycomb-group protein Mel-18 is regulated by PKC phosphorylation
    • Fujisaki, S. 2003, Dimerization of the Polycomb-group protein Mel-18 is regulated by PKC phosphorylation Biochem. Biophys. Res. Commun. 300 (1) 135-140
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , Issue.1 , pp. 135-140
    • Fujisaki, S.1
  • 38
    • 70449453475 scopus 로고    scopus 로고
    • Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins
    • Bezsonova, I. 2009, Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins Biochemistry 48 (44) 10542-10548
    • (2009) Biochemistry , vol.48 , Issue.44 , pp. 10542-10548
    • Bezsonova, I.1
  • 39
    • 35848939627 scopus 로고    scopus 로고
    • The isolated C-terminal domain of Ring1B is a dimer made of stable, well-structured monomers
    • Czypionka, A. 2007, The isolated C-terminal domain of Ring1B is a dimer made of stable, well-structured monomers Biochemistry 46 (44) 12764-12776
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12764-12776
    • Czypionka, A.1
  • 40
    • 48649096892 scopus 로고    scopus 로고
    • Structural transitions of the RING1B C-terminal region upon binding the polycomb cbox domain
    • Wang, R. 2008, Structural transitions of the RING1B C-terminal region upon binding the polycomb cbox domain Biochemistry 47 (31) 8007-8015
    • (2008) Biochemistry , vol.47 , Issue.31 , pp. 8007-8015
    • Wang, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.