References
- Fischle, W., Wang, Y., and Allis, CD.: Histone and chromatin cross-talk. Curr Opin Cell Biol. 15:172-83, 2003 https://doi.org/10.1016/S0955-0674(03)00013-9
- Grunstein, M.: Histone acetylation in chromatin structure and transcription. Nature. 389:349-52, 1997 https://doi.org/10.1038/387349a0
- Jones, R. S. and Gelbart, W. M.: The Drosophila Polycomb-group gene Enhancer of zeste contains a region with sequence similarity to trithorax. Mol. Cell. Biol. 13:6357-66, 1993 https://doi.org/10.1128/MCB.13.10.6357
- Kouzarides, T.: Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12:198-209, 2002 https://doi.org/10.1016/S0959-437X(02)00287-3
- Kurotaki, N., Harada, N., Yoshiura, K., Sugano, S., Niikawa, N., and Matsumoto, N.: Molecular characterization of NSD1, a human homologue of the mouse Nsd1 gene. Gene. 279: 197-204, 2001 https://doi.org/10.1016/S0378-1119(01)00750-8
- Lachner, M. and Jenuwein, T.: The many faces of histone lysine methylation. Curr Opin Cell Biol. 14:286-98, 2002 https://doi.org/10.1016/S0955-0674(02)00335-6
- Lachner, M., O'Sullivan, R. J., and Jenuwein, T.: An epigenetic road map for histone lysine methylation. J Cell Sci. 116: 2117-24, 2003 https://doi.org/10.1242/jcs.00493
- Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J.: Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389:251-60, 1997 https://doi.org/10.1038/38444
- Martin, C. and Zhang, Y.: The diverse function of histone lysine methylation, Nature, 6:838-49, 2005
- O'Carroll, D., Scherthan, H., Peters, A. H., Opravil, S., Haynes, A. R., Laible, G., Rea, S., Schmid, M., Lebersorger, A., Jerratsch, M., Sattler, L., Mattei, M. G., Denny, P., Brown, S. D., Schweizer, D., and Jenuwein, T.: Isolation and characterization of Suv39h2, a second histone H3 methyl-transferase gene that displays testis-specific expression. Mol Cell Biol 20:9423-33, 2000 https://doi.org/10.1128/MCB.20.24.9423-9433.2000
- Ogawa, H., Ishiguro, K., Gaubatz, S., Livingston, D. M., and Nakatani, Y.: A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. Science. 296:1132-36, 2002 https://doi.org/10.1126/science.1069861
- Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z. W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., and Jenuwein, T.: Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 406: 593-9, 2000 https://doi.org/10.1038/35020506
- Richards, E. J. and Elgin, S. C.: Epigenetic codes for heterochromatin formation and silencing: rounding up the usual suspects. Cell. 108:489-500, 2002 https://doi.org/10.1016/S0092-8674(02)00644-X
- Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D., and Jenuwein, T.: A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev. 18:1251-62, 2004 https://doi.org/10.1101/gad.300704
- Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., and Rauscher, F. J.: SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 16:919-32, 2002 https://doi.org/10.1101/gad.973302
- Sims, R. J., Nishioka, K., and Reinberg, D.: Histone lysine methylation: a signature for chromatin function. Trends Genet. 19:629-39, 2003 https://doi.org/10.1016/j.tig.2003.09.007
- Stassen, M. J., Bailey, D., Nelson, S., Chinwalla, V., and Harte, P. J.: The Drosophila trithorax proteins contain a novel variant of the nuclear receptor type DNA binding domain and an ancient conserved motif found in other chromosomal proteins. Mech Dev. 52:209-23, 1995 https://doi.org/10.1016/0925-4773(95)00402-M
- Strahl, B. D. and Allis, C. D.: Gene silencing: trans-histone regulatory pathway in chromatin. Nature. 403:41-5, 2002 https://doi.org/10.1038/47412
- Tachibana, M., Sugimoto, K., Fukushima, T., and Shinkai, Y.: Set domain-containing protein, G9a, is a novel lysinepreferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J Biol Chem. 276:25309-17, 2001 https://doi.org/10.1074/jbc.M101914200
- Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H., and Shinkai, Y.: G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis, Genes Dev. 16:1779-1791. 2002 https://doi.org/10.1101/gad.989402
- Tschiersch, B., Hofmann, A., Krauss, V., Dorn, R., Korge, G., and Reuter, G.: 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. 13:3822-31, 1994
- Turner, B. M.: Histone actylation and an epigenetic code. Bioessay. 22:836-84, 2000 https://doi.org/10.1002/1521-1878(200009)22:9<836::AID-BIES9>3.0.CO;2-X
- Waring, P. M. and Cleary, M. L.: Disruption of a homolog of trithorax by 11q23 translocations: leukemogenic and transcriptional implications. Curr. Top. Microbiol. Immunol. 220:1-23, 1997