A drosophila polycomb group complex includes zeste and dTAFII proteins

Nature

Volumn 412, Issue 6847, 2001, Pages 655-660

  Saurin, Andrew J ^a   Shao, Zhaohui ^a,b   Erdjument Bromage, Hediye ^c   Tempst, Paul ^c   Kingston, Robert E ^a  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

^b BIOGEN   (United States)

^c MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA BINDING PROTEIN; DROSOPHILA PROTEIN; INSECT PROTEIN; POLYCOMB PROTEIN, DROSOPHILA; TRANSCRIPTION FACTOR II; TRANSCRIPTION FACTOR IID; ZESTE PROTEIN, DROSOPHILA;

ANIMAL; ARTICLE; CHEMISTRY; DROSOPHILA; GEL CHROMATOGRAPHY; GENE; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; MASS SPECTROMETRY; METABOLISM; PHYSIOLOGY; PROTEIN BINDING; SERODIAGNOSIS; WESTERN BLOTTING;

ANIMALS; BLOTTING, WESTERN; CHROMATOGRAPHY, GEL; DNA; DNA-BINDING PROTEINS; DROSOPHILA; DROSOPHILA PROTEINS; GENE EXPRESSION REGULATION; GENES, INSECT; INSECT PROTEINS; MASS SPECTROMETRY; PRECIPITIN TESTS; PROTEIN BINDING; TRANSCRIPTION FACTOR TFIID; TRANSCRIPTION FACTORS, TFII; TRANSCRIPTION, GENETIC;

EID: 0035833718     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35088096     Document Type: Article

References (29)

1. Hartwell, L. H., Hopfield, J. J., Leiber, S. & Murray, A. W. From molecular to modular cell biology. Nature 402, C47-C52 (1999).
2. Franke, A. et al. Polycomb and polyhomeotic are constituents of a multimeric protein complex in chromatin of Drosophila melanogaster. EMBO J. 11, 2941-2950 (1992).
3. Locke, J., Kotarski, M.A. & Tartof, K. D. Dosage-dependent modifiers ofposition effectvariegation in Drosophila and a mass action model that explains their effect. Genetics 120, 181-198 (1988).
4. Simon, J. Locking in stable states of gene expression: transcriptional control during Drosophila development. Curr. Biol. 7, 376-385 (1995).
5. Shao, Z. et al. Stabilization of chromatin structure by PRC1, a Polycomb complex. Cell 98, 37-46 (1999).
6. Satijn, D. P. E. et al. RING1 is associated with the Polycomb-group protein complex and acts as a transcriptional repressor. Mol. Cell. Biol. 17, 4105-4113 (1997).
7. Schoorlemmer, J. et al. Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain. EMBO J. 16, 5930-5942 (1997).
8. Benson, M. & Pirrota, V. The Drosophila zeste protein binds cooperatively to sites in many gene regulatory regions: implications for transvection and gene regulation. Development 7, 3907-3915 (1988).
9. Albright, S.R. & Tjian, R. TAFs revisited: more data reveal new twists and confirm old ideas. Gene 242, 1-13 (2000).
10. Ng, J., Hart, C.M., Morgan, K. & Simon, J. A. A Drosophila ESC-E(Z) protein complex is distinct from other polycomb group complexes and contains covalently modified ESC. Mol. Cell. Biol. 20, 3069-3078 (2000).
11. Mollaaghababa, R. et al. Mutations in Drosophila heat shock cognate 4 are enhancers of Polycomb. Proc. NatlAcad. Sci. USA 98, 3958-3963 (2001).
12. De Rubertis, F. et al. The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast. Nature 384, 589-591 (1996).
13. Kehle, J. et al. dMi-2, a Hunchback-interacting protein that functions in Polycomb repression. Science 282, 1897-1900 (1998).
14. Pennetta, G. & Pauli, D. The Drosophila Sin3 gene encodes a widely distributed transcription factor essential for embryonic viability. Dev. Genes Evol. 208, 531-536 (1998).
15. Tyler, J., Bulger, M., Kamakaka, R. T., Kobayashi, R. & Kadonaga, J. T. The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein. Mol. Cell. Biol. 16, 6149-6159 (1996).
16. Tsai, C.-C., Kao, H.-Y., Yao, T.-P, McKeown, M. & Evans, R. M. SMRTER, a Drosophila nuclear receptor coregulator, reveals that EcR-mediated repression is critical for development. Mol. Cell 4, 175-186 (1999).
17. Tie, F., Furuyama, T., Prasad-Sinha, J., Jane, E. & Harte, P. J. The Drosophila Polycomb Group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3. Development128, 275-286 (2001).
18. Orlando, V, Jane, E. P., Chinwalla, V., Harte, P. J. & Paro, R. Binding of Trithorax and Polycomb proteins to the bithorax complex: dynamic changes during early Drosophila embryogenesis. EMBO J. 17, 5141-5150 (1998).
19. Hoffman, A. et al. A histone octamer-like structure within TFIID. Nature 380, 356-359 (1996).
20. Nakatani, Y., Bagby, S. & Ikura, M. Thehistone folds in transcription factorTFIID. J. Biol. Chem. 271, 6575-6578 (1996).
21. Xie, X. et al. Structural similaritybetween TAFs and the heterotetrameric core of the histone octamer. Nature 380, 316-322 (1996).
22. Rastelli, L., Chan, C. S. & Pirrotta, V. Related chromosome binding sites for zeste, suppressors of zeste and the Polycomb group proteins in Drosophila and their dependence on Enhancer of zeste function. EMBOJ. 12, 1513-1522 (1993).
23. Kal, A. J., Mahmoudi, T., Zak, N. B. & Verrijzer, C. P. The Drosophila Brahma complex is an essential coactivator for the trithorax group protein Zeste. Genes Dev. 14, 1058-1071 (2000).
24. Lessard, J., Baban, S. & Sauvageau, G. Stage-specific expression of polycomb group genes in human bone marrow cells. Blood91, 1216-1224 (1998).
25. Erdjument-Bromage, H. et al. Micro-tip reversed-phaseliquid chromatographicextraction ofpeptide pools for mass spectrometry. Chromatogr. 826, 157-181 (1998).
26. Geromanos, S., Freckleton, G. & Tempst, P. Tuning of an electrospray ionization source for maximum peptide-ion transmission into a mass spectrometer. Anal. Chem. 72, 779-790 (2000).
27. Mann, M., Hojrup, P. & Roepstorff, P. Use of mass spectrometric molecular weight information to identify proteins in databases. Biol. Mass Spectrom. 22, 338-345 (1993).
28. Mann, M. & Wilm, M. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem. 66, 4390-4399 (1994).
29. Fenyö, D., Qin, J. & Chait, B. T. Protein identification using mass spectrometric information. Electrophoresis 19, 998-1005 (1998).