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Volumn 7, Issue 10, 2005, Pages 1007-1013

Ubiquitin ligase component Cul4 associates with Clr4 histone methyltransferase to assemble heterochromatin

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CULLIN; HISTONE; METHYLTRANSFERASE; MUTANT PROTEIN; NEDD8 PROTEIN; PROTEIN CLR4; PROTEIN CUL4; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 27144554969     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1300     Document Type: Article
Times cited : (177)

References (35)
  • 1
    • 2342512876 scopus 로고    scopus 로고
    • Structure and function of heterochromatin: Implications for epigenetic gene silencing and genome organization
    • (ed. Hannon, G.) 205-232 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor)
    • Hall, I. M. & Grewal, S. I. S. Structure and function of heterochromatin: Implications for epigenetic gene silencing and genome organization. In RNAi: A Guide to Gene Silencing(ed. Hannon, G.) 205-232 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 2003).
    • (2003) RNAi: A Guide to Gene Silencing
    • Hall, I.M.1    Grewal, S.I.S.2
  • 2
    • 8344264534 scopus 로고    scopus 로고
    • Heterochromatin regulates cell type-specific long-range chromatin interactions essential for directed recombination
    • Jia, S., Yamada, T. & Grewal, S. I. S. Heterochromatin regulates cell type-specific long-range chromatin interactions essential for directed recombination. Cell 119, 469-480 (2004).
    • (2004) Cell , vol.119 , pp. 469-480
    • Jia, S.1    Yamada, T.2    Grewal, S.I.S.3
  • 3
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. & Allis, C. D. Translating the histone code. Science 293, 1074-1080 (2001).
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 4
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • Nakayama, J., Rice, J. C., Strahl, B. D., Allis, C. D. & Grewal, S. I. S. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110-113 (2001).
    • (2001) Science , vol.292 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.S.5
  • 5
    • 23044498502 scopus 로고    scopus 로고
    • Comprehensive analysis of heterochromatin- and RNAi-mediated epigenetic control of the fission yeast genome
    • Cam, H. et al. Comprehensive analysis of heterochromatin- and RNAi-mediated epigenetic control of the fission yeast genome. Nature Genet. 37, 809-819 (2005).
    • (2005) Nature Genet. , vol.37 , pp. 809-819
    • Cam, H.1
  • 6
    • 3042640887 scopus 로고    scopus 로고
    • The fission yeast heterochromatin protein Rik1 is required for telomere clustering during meiosis
    • Tuzon, C. T. et al. The fission yeast heterochromatin protein Rik1 is required for telomere clustering during meiosis. J. Cell Biol. 165, 759-765 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 759-765
    • Tuzon, C.T.1
  • 7
    • 0035930750 scopus 로고    scopus 로고
    • Requirement of heterochromatin for cohesion at centromeres
    • Bernard, P. et al. Requirement of heterochromatin for cohesion at centromeres. Science 294, 2539-2542 (2001).
    • (2001) Science , vol.294 , pp. 2539-2542
    • Bernard, P.1
  • 8
    • 0036144420 scopus 로고    scopus 로고
    • Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission yeast
    • Nonaka, N. et al. Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission yeast. Nature Cell Biol. 4, 89-93 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 89-93
    • Nonaka, N.1
  • 9
    • 0242348752 scopus 로고    scopus 로고
    • Histone lysine methylation: A signature for chromatin function
    • Sims, R. J. 3rd, Nishioka, K. & Reinberg, D. Histone lysine methylation: a signature for chromatin function. Trends Genet. 19, 629-639 (2003).
    • (2003) Trends Genet. , vol.19 , pp. 629-639
    • Sims III, R.J.1    Nishioka, K.2    Reinberg, D.3
  • 10
    • 3042521583 scopus 로고    scopus 로고
    • RNAi-independent heterochromatin nucleation by the stress-activated ATF/CREB family proteins
    • Jia, S., Noma, K. & Grewal, S. I. S. RNAi-independent heterochromatin nucleation by the stress-activated ATF/CREB family proteins. Science 304, 1971-1976 (2004).
    • (2004) Science , vol.304 , pp. 1971-1976
    • Jia, S.1    Noma, K.2    Grewal, S.I.S.3
  • 11
    • 10644237968 scopus 로고    scopus 로고
    • RNAi-mediated pathways in the nucleus
    • Matzke, M. A. & Birchler, J. A. RNAi-mediated pathways in the nucleus. Nature Rev. Genet. 6, 24-35 (2005).
    • (2005) Nature Rev. Genet. , vol.6 , pp. 24-35
    • Matzke, M.A.1    Birchler, J.A.2
  • 12
    • 2342517250 scopus 로고    scopus 로고
    • Regulation of heterochromatin by histone methylation and small RNAs
    • Grewal, S. I. S. & Rice, J. C. Regulation of heterochromatin by histone methylation and small RNAs. Curr. Opin. Cell. Biol. 16, 230-238 (2004).
    • (2004) Curr. Opin. Cell. Biol. , vol.16 , pp. 230-238
    • Grewal, S.I.S.1    Rice, J.C.2
  • 13
    • 17744364327 scopus 로고    scopus 로고
    • Gardening the genome: DNA methylation in Arabidopsis thaliana
    • Chan, S. W., Henderson, I. R. & Jacobsen, S. E. Gardening the genome: DNA methylation in Arabidopsis thaliana. Nature Rev. Genet. 6, 351-360 (2005).
    • (2005) Nature Rev. Genet. , vol.6 , pp. 351-360
    • Chan, S.W.1    Henderson, I.R.2    Jacobsen, S.E.3
  • 14
    • 10644221797 scopus 로고    scopus 로고
    • RITS acts in cis to promote RNA interference-mediated transcriptional and post-transcriptional silencing
    • Noma, K. et al. RITS acts in cis to promote RNA interference-mediated transcriptional and post-transcriptional silencing. Nature Genet. 36, 1174-1180 (2004).
    • (2004) Nature Genet. , vol.36 , pp. 1174-1180
    • Noma, K.1
  • 15
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M. D. & Deshaies, R. J. Function and regulation of cullin-RING ubiquitin ligases. Nature Rev. Mol. Cell Biol. 6, 9-20 (2005).
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 16
    • 6344285337 scopus 로고    scopus 로고
    • A chromodomain protein, Chp1, is required for the establishment of heterochromatin in fission yeast
    • Sadaie, M., Iida, T., Urano, T. & Nakayama, J. A chromodomain protein, Chp1, is required for the establishment of heterochromatin in fission yeast. EMBO J. 23, 3825-3835 (2004).
    • (2004) EMBO J. , vol.23 , pp. 3825-3835
    • Sadaie, M.1    Iida, T.2    Urano, T.3    Nakayama, J.4
  • 17
    • 0034666340 scopus 로고    scopus 로고
    • PSI-BLAST searches using hidden markov models of structural repeats: Prediction of an unusual sliding DNA clamp and of β-propellers in UV-damaged DNA-binding protein
    • Neuwald, A. F. & Poleksic, A. PSI-BLAST searches using hidden markov models of structural repeats: Prediction of an unusual sliding DNA clamp and of β-propellers in UV-damaged DNA-binding protein. Nucl. Acids Res. 28, 3570-3580 (2000).
    • (2000) Nucl. Acids Res. , vol.28 , pp. 3570-3580
    • Neuwald, A.F.1    Poleksic, A.2
  • 18
    • 5444274523 scopus 로고    scopus 로고
    • Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage
    • Hu, J., McCall, C. M., Ohta, T. & Xiong, Y. Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage. Nature Cell Biol. 6, 1003-1009 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 1003-1009
    • Hu, J.1    McCall, C.M.2    Ohta, T.3    Xiong, Y.4
  • 19
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms
    • Liu, C. et al. Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms. Genes Dev. 17, 1130-1140 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1130-1140
    • Liu, C.1
  • 20
    • 17044378618 scopus 로고    scopus 로고
    • Ddb1 controls genome stability and meiosis in fission yeast
    • Holmberg, C. et al. Ddb1 controls genome stability and meiosis in fission yeast. Genes Dev. 19, 853-862 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 853-862
    • Holmberg, C.1
  • 21
    • 11844265935 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerase is an essential component of a self-enforcing loop coupling heterochromatin assembly to siRNA production
    • Sugiyama, T., Cam, H., Verdel, A., Moazed, D. & Grewal, S. I. S. RNA-dependent RNA polymerase is an essential component of a self-enforcing loop coupling heterochromatin assembly to siRNA production. Proc. Natl Acad. Sci. USA. 102, 152-157 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 152-157
    • Sugiyama, T.1    Cam, H.2    Verdel, A.3    Moazed, D.4    Grewal, S.I.S.5
  • 22
    • 0022635941 scopus 로고
    • Construction of mini-chromosome by deletion and its mitotic and meiotic behaviour in fission yeast
    • Niwa, O., Matsumoto, T. & Yanagida, M. Construction of mini-chromosome by deletion and its mitotic and meiotic behaviour in fission yeast. Mol. Gen. Genet. 203, 397-405 (1986).
    • (1986) Mol. Gen. Genet. , vol.203 , pp. 397-405
    • Niwa, O.1    Matsumoto, T.2    Yanagida, M.3
  • 23
    • 0027183895 scopus 로고
    • Directionality of fission yeast mating-type interconversion is controlled by the location of the donor loci
    • Thon, G. & Klar, A. J. Directionality of fission yeast mating-type interconversion is controlled by the location of the donor loci. Genetics 134, 1045-1054 (1993).
    • (1993) Genetics , vol.134 , pp. 1045-1054
    • Thon, G.1    Klar, A.J.2
  • 24
    • 0031865511 scopus 로고    scopus 로고
    • The chromo and SET domains of the Clr4 protein are essential for silencing in fission yeast
    • Ivanova, A. V., Bonaduce, M. J., Ivanov, S. V. & Klar, A. J. The chromo and SET domains of the Clr4 protein are essential for silencing in fission yeast. Nature Genet. 19, 192-195 (1998).
    • (1998) Nature Genet. , vol.19 , pp. 192-195
    • Ivanova, A.V.1    Bonaduce, M.J.2    Ivanov, S.V.3    Klar, A.J.4
  • 25
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: Building an expressway to protein destruction
    • Pan, Z. Q., Kentsis, A., Dias, D. C., Yamoah, K. & Wu, K. Nedd8 on cullin: Building an expressway to protein destruction. Oncogene 23, 1985-1997 (2004).
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 26
    • 0034600951 scopus 로고    scopus 로고
    • Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast
    • Osaka, F. et al. Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast. EMBO J. 19, 3475-3484 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3475-3484
    • Osaka, F.1
  • 27
    • 23044504238 scopus 로고    scopus 로고
    • A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation
    • Horn, P. J., Bastie, J. N. & Peterson, C. L. A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation. Genes Dev. 19, 1705-1714 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 1705-1714
    • Horn, P.J.1    Bastie, J.N.2    Peterson, C.L.3
  • 28
    • 0035875666 scopus 로고    scopus 로고
    • UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation
    • Brand, M. et al. UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. EMBO J. 20, 3187-3196 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3187-3196
    • Brand, M.1
  • 29
    • 0034812915 scopus 로고    scopus 로고
    • Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo
    • Martinez, E. et al. Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol. Cell. Biol. 21, 6782-6795 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6782-6795
    • Martinez, E.1
  • 30
    • 0037183856 scopus 로고    scopus 로고
    • Establishment and maintenance of a heterochromatin domain
    • Hall, I. M. et al. Establishment and maintenance of a heterochromatin domain. Science 297, 2232-2237 (2002).
    • (2002) Science , vol.297 , pp. 2232-2237
    • Hall, I.M.1
  • 31
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang, H. et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature 431, 873-878 (2004).
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1
  • 32
    • 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, 104-108 (2002).
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 33
    • 0037047323 scopus 로고    scopus 로고
    • Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6
    • Dover, J. et al. Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6. J. Biol. Chem. 277, 28368-28371 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 28368-28371
    • Dover, J.1
  • 34
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • 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, 34655-34657 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 35
    • 0036682364 scopus 로고    scopus 로고
    • Gene silencing: Trans-histone regulatory pathway in chromatin
    • Briggs, S. D. et al. Gene silencing: Trans-histone regulatory pathway in chromatin. Nature 418, 498 (2002).
    • (2002) Nature , vol.418 , pp. 498
    • Briggs, S.D.1


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