Set Domain-Dependent Regulation of Transcriptional Silencing and Growth Control by SUV39H1, a Mammalian Ortholog of Drosophila Su(var)3-9

REFERENCES

• Aagaard, L., Laible, G., Selenko, P., Schmid, M., Dorn, R., Schotta, G., Kuhfittig, S., Wolf, A., Lebersorger, A. S., Reuter, G., and Jenuwein, T.. 1999. Functional mammalian homologues of the drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 18:1923–1938
   PubMed Web of Science ®Google Scholar
• Ayer, D. E., Laherty, C. D., Lawrence, Q. A., Armstrong, A. P., and Eisenman, R. N.. 1996. Mad proteins contain a dominant transcription repression domain. Mol. Cell. Biol. 16:5772–5781
   PubMed Web of Science ®Google Scholar
• Baksa, K., Morawietz, H., Dombradi, V., Axton, M., Taubert, H., Szabo, G., Torok, I., Udvardy, A., Gyurkovics, H., and Szoor, B.. 1993. Mutations in the protein phosphatase I gene at 87B can differentially affect suppression of position-effect variegation and mitosis in Drosophila melanogaster. Genetics 135:117–125
   PubMedGoogle Scholar
• Bunker, C. A., and Kingston, R. E.. 1994. Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cells. Mol. Cell. Biol. 14:1721–1732
   PubMedGoogle Scholar
• Cai, H. N., Arnosti, D. N., and Levine, M.. 1996. Long-range repression in Drosophila embryo. Proc. Natl. Acad. Sci. USA 93:9309–9314
   PubMedGoogle Scholar
• Chen, C., and Okayama, H.. 1987. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745–2752
   PubMed Web of Science ®Google Scholar
• Chinwalla, V., Jane, E. P., and Harte, P. J.. 1995. The Drosophila trithorax protein binds to specific chromosomal sites and is co-localized with Polycomb at many sites. EMBO J. 14:2056–2065
   PubMedGoogle Scholar
• Cowell, I. G., and Austin, C. A.. 1997. Self-association of chromo domain peptides. Biochim. Biophys. Acta 1337:198–206
   PubMedGoogle Scholar
• Cui, X., De Vivo, I., Slany, R., Miyamoto, A., Firestein, R., and Cleary, M. L.. 1998. Association of SET domain and myotubularin-related proteins modulates growth control. Nat. Genet. 18:331–337
   PubMed Web of Science ®Google Scholar
• De Vivo, I., Cui, X., Domen, J., and Cleary, M. L.. 1998. Growth stimulation of primary B cell precursors by the anti-phosphatase Sbf1. Proc. Natl. Acad. Sci. USA 95:9471–9476
   PubMedGoogle Scholar
• Dernburg, A. F., Sedat, J. W., and Hawley, R. S.. 1996. Direct evidence of a role for heterochromatin in meiotic chromosome segregation. Cell 86:135–146
   PubMedGoogle Scholar
• Djabali, M., Selleri, L., Parry, L., Bower, M., Young, B. D., and Evans, G. A.. 1992. A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias. Nat. Genet. 2:113–118
   PubMed Web of Science ®Google Scholar
• Dunaief, J. L., Strober, B. E., Guha, S., Khavari, P. A., Alin, K., Luban, J., Begemann, M., Crabtree, G. R., and Goff, S. P.. 1994. The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 79:119–130
   PubMed Web of Science ®Google Scholar
• Fujita, M., Yamada, C., Tsurumi, T., Hanaoka, F., Matsuzawa, K., and Inagaki, M.. 1998. Cell cycle- and chromatin binding state-dependent phosphorylation of human MCM heterohexameric complexes. A role for cdc2 kinase. J. Biol. Chem. 273:17095–17101
   PubMedGoogle Scholar
• Gould, A.. 1997. Functions of mammalian Polycomb group and trithorax group related genes. Curr. Opin. Genet. Dev. 7:488–494
   PubMedGoogle Scholar
• Gu, Y., Nakamura, T., Alder, H., Prasad, R., Canaani, O., Cimino, G., Croce, C. M., and Canaani, E.. 1992. The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene. Cell 71:701–708
   PubMed Web of Science ®Google Scholar
• Harlow, E., and Lane, D.. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
   Google Scholar
• Herrera, R. E., Chen, F., and Weinberg, R. A.. 1996. Increased histone H1 phosphorylation and relaxed chromatin structure in Rb-deficient fibroblasts. Proc. Natl. Acad. Sci. USA 93:11510–11515
   PubMed Web of Science ®Google Scholar
• Hobert, O., Jallal, B., and Ullrich, A.. 1996. Interaction of Vav with ENX-1, a putative transcriptional regulator of homeobox gene expression. Mol. Cell. Biol. 16:3066–3073
   PubMed Web of Science ®Google Scholar
• Huang, D. W., Fanti, L., Pak, D. T., Botchan, M. R., Pimpinelli, S., and Kellum, R.. 1998. Distinct cytoplasmic and nuclear fractions of Drosophila heterochromatin protein 1: their phosphorylation levels and associations with origin recognition complex proteins. J. Cell Biol. 142:307–318
   PubMed Web of Science ®Google Scholar
• Hunter, T.. 1998. Anti-phosphatases take the stage. Nat. Genet. 18:303–305
   PubMedGoogle Scholar
• Ivanova, A. V., Bonaduce, M., Ivanov, S. V., and Klar, A. J.. 1998. The chromo and SET domains of the Clr4 protein are essential for silencing in fission yeast. Nat. Genet. 19:192–195
   PubMedGoogle Scholar
• Jacobs, J. J. L., Kieboom, K., Marino, S., DePinho, R. A., and van Lohuizen, M.. 1999. The oncogene and Polycomb-group gene bmi-1 regulates cell proliferation and senescence through the ink4a locus. Nature 397:164–168
   PubMed Web of Science ®Google Scholar
• Jacobsen, S., and Pillus, L.. 1999. Modifying chromatin and concepts of cancer. Curr. Opin. Genet. Dev. 9:175–184
   PubMedGoogle Scholar
• Jenuwein, T., Laible, G., Dorn, R., and Reuter, G.. 1998. SET domain proteins modulate chromatin domains in eu- and heterochromatin. Cell. Mol. Life Sci. 54:80–93
   PubMedGoogle Scholar
• Lehming, N., Le Saux, A., Schuller, J., and Ptashne, M.. 1998. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl. Acad. Sci. USA 95:7322–7326
   PubMed Web of Science ®Google Scholar
• Lin, R. J., Nagy, L., Inoue, S., Shao, W., Miller, W. H.Jr., and Evans, R. M.. 1998. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391:811–814
   PubMed Web of Science ®Google Scholar
• Lin, Y. S., Carey, M. F., Ptashne, M., and Green, M. R.. 1988. GAL4 derivatives function alone and synergistically with mammalian activators in vitro. Cell 54:659–664
   PubMedGoogle Scholar
• Luo, R. X., Postigo, A. A., and Dean, D. C.. 1998. Rb interacts with histone deacetylase to repress transcription. Cell 92:463–473
   PubMed Web of Science ®Google Scholar
• Magnaghi-Jaulin, L., Groisman, R., Naguibneva, I., Robin, P., Lorain, S., Le Villain, J. P., Troalen, F., Trouche, D., and Harel-Bellan, A.. 1998. Retinoblastoma protein represses transcription by recruiting a histone deacetylase. Nature 391:601–605
   PubMed Web of Science ®Google Scholar
• Melcher, M., Schmid, M., Aagaard, L., Selenko, P., Laible, G., and Jenuwein, T.. 2000. Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression. Mol. Cell. Biol. 20:3728–3741
   PubMed Web of Science ®Google Scholar
• Messmer, S., Franke, A., and Paro, R.. 1992. Analysis of the functional role of the Polycomb chromo domain in Drosophila melanogaster. Genes Dev. 6:1241–1254
   PubMed Web of Science ®Google Scholar
• Miyamoto, A., Cui, X., Naumovski, L., and Cleary, M. L.. 1996. Helix-loop-helix proteins LYL1 and E2a form heterodimeric complexes with distinctive DNA-binding properties in hematolymphoid cells. Mol. Cell. Biol. 16:2394–2401
   PubMedGoogle Scholar
• Muchardt, C., Reyes, J. C., Bourachot, B., Leguoy, E., and Yaniv, M.. 1996. The hbrm and BRG-1 proteins, components of the human SNF/SWI complex, are phosphorylated and excluded from the condensed chromosomes during mitosis. EMBO J. 15:3394–3402
   PubMedGoogle Scholar
• Nigg, E. A.. 1993. Targets of cyclin-dependent protein kinases. Curr. Opin. Cell Biol. 5:187–193
   PubMed Web of Science ®Google Scholar
• Nislow, C., Ray, E., and Pillus, L.. 1997. SET1, a yeast member of the Trithorax family, functions in transcriptional silencing and diverse cellular processes. Mol. Biol. Cell 8:2421–2431
   PubMedGoogle Scholar
• Orlando, V., and Paro, R.. 1995. Chromatin multiprotein complexes involved in the maintenance of transcription patterns. Curr. Opin. Genet. Dev. 5:174–179
   PubMedGoogle Scholar
• Paro, R., Strutt, H., and Cavalli, G.. 1998. Heritable chromatin states induced by the Polycomb and trithorax group genes. Novartis Found. Symp. 214:51–61
   PubMedGoogle Scholar
• Pirrotta, V.. 1997. Chromatin-silencing mechanisms in Drosophila maintain patterns of gene expression. Trends Genet. 13:314–318
   PubMed Web of Science ®Google Scholar
• Platero, J. S., Hartnett, T., and Eissenberg, J. C.. 1995. Functional analysis of the chromo domain of HP1. EMBO J. 14:3977–3986
   PubMed Web of Science ®Google Scholar
• Rastelli, L., Chan, C. S., and Pirrotta, V.. 1993. Related chromosome binding sites for zeste, suppressors of zeste and Polycomb group proteins in Drosophila and their dependence on Enhancer of zeste function. EMBO J. 12:1513–1522
   PubMedGoogle Scholar
• Reed, S. I.. 1997. Control of the G1/S transition. Cancer Surv. 29:7–23
   PubMedGoogle Scholar
• Reuter, G., and Spierer, P.. 1992. Position effect variegation and chromatin proteins. Bioessays 14:605–612
   PubMedGoogle Scholar
• Rozenblatt-Rosen, O., Rozovskaia, T., Burakov, D., Sedkov, Y., Tillib, S., Blechman, J., Nakamura, T., Croce, C. M., Mazo, A., and Canaani, E.. 1998. The C-terminal SET domains of ALL-1 and TRITHORAX interact with the INI1 and SNR1 proteins, components of the SWI/SNF complex. Proc. Natl. Acad. Sci. USA 95:4152–4157
   PubMed Web of Science ®Google Scholar
• Sadowski, I., Bell, B., Broad, P., and Hollis, M.. 1992. GAL4 fusion vectors for expression in yeast or mammalian cells. Gene 118:137–141
   PubMed Web of Science ®Google Scholar
• Shao, Z., Raible, F., Mollaaghababa, R., Guyon, J. R., Wu, C. T., Bender, W., and Kingston, R. E.. 1999. Stabilization of chromatin structure by PRC1, a Polycomb complex. Cell 98:37–46
   PubMedGoogle Scholar
• Strutt, H., and Paro, R.. 1997. The polycomb group protein complex of Drosophila melanogaster has different compositions at different target genes. Mol. Cell. Biol. 17:6773–6783
   PubMedGoogle Scholar
• Swirnoff, A. H., Apel, E. D., Svaren, J., Sevetson, B. R., Zimonjic, D. B., Popescu, N. C., and Milbrandt, J.. 1998. Nab1, a corepressor of NGFI-A (Egr-1), contains an active transcriptional repression domain. Mol. Cell. Biol. 18:512–524
   PubMedGoogle Scholar
• Tkachuk, D. C., Kohler, S., and Cleary, M. L.. 1992. Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell 71:691–700
   PubMed Web of Science ®Google Scholar
• Trouche, D., LeChaloney, C., Muchardt, C., Yaniv, M., and Kouzarides, T.. 1997. RB and hbrm cooperate to repress the activation functions of E2F1. Proc. Natl. Acad. Sci. USA 94:11268–11273
   PubMed Web of Science ®Google Scholar
• Tschiersch, B., Hoffman, A., Krauss, V., Dorn, R., Korge, G., Korge, G., and Reuter, G.. 1994. The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes. EMBO J. 13:3822–3831
   PubMed Web of Science ®Google Scholar
• van Lohuizen, M., Tijms, M., Voncken, J. W., Schumacher, A., Magnuson, T., and Wientjens, E.. 1998. Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexes. Mol. Cell. Biol. 18:3572–3579
   PubMedGoogle Scholar
• Versteege, I., Sevenet, N., Lange, J., Rousseau-Merck, M. F., Ambros, P., Handgretinger, R., Aurias, A., and Delattre, O.. 1998. Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer. Nature 394:203–206
   PubMed Web of Science ®Google Scholar
• Waring, P., and Cleary, M. L.. 1997. Disruption of a homolog of trithorax by 11q23 translocations: leukemogenic and transcriptional implications. Curr. Top. Microbiol. Immunol. 220:1–23
   PubMedGoogle Scholar
• Wei, Y., Yu, L., Bowen, J., Gorovsky, M. A., and Allis, C. D.. 1999. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97:99–109
   PubMed Web of Science ®Google Scholar
• Wishart, M. J., and Dixon, J. E.. 1998. Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains. Trends Biochem. Sci. 23:301–306
   PubMedGoogle Scholar
• Zhao, K., Wang, W., Rando, O. J., Xue, Y., Swiderek, K., Kuo, A., and Crabtree, G. R.. 1998. Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell 95:625–636
   PubMed Web of Science ®Google Scholar
• Zhao, T., and Eissenberg, J. C.. 1999. Phosphorylation of heterochromatin protein 1 by casein kinase II is required for efficient heterochromatin binding in Drosophila. J. Biol. Chem. 274:15095–15100
   PubMedGoogle Scholar