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Molecular and Cellular Biology, May 2003, p. 3352-3362, Vol. 23, No. 9
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.9.3352-3362.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

A 1-Megadalton ESC/E(Z) Complex from Drosophila That Contains Polycomblike and RPD3

Feng Tie,1 Jayashree Prasad-Sinha,1 Anna Birve,2 Åsa Rasmuson-Lestander,2 and Peter J. Harte1*

Department of Genetics, Case Western Reserve University, Cleveland, Ohio 44106,1 Department of Genetics, Umeå University, S-90187 Umeå, Sweden2

Received 17 January 2003/ Accepted 4 February 2003

Polycomb group (PcG) proteins are required to maintain stable repression of the homeotic genes and others throughout development. The PcG proteins ESC and E(Z) are present in a prominent 600-kDa complex as well as in a number of higher-molecular-mass complexes. Here we identify and characterize a 1-MDa ESC/E(Z) complex that is distinguished from the 600-kDa complex by the presence of the PcG protein Polycomblike (PCL) and the histone deacetylase RPD3. In addition, the 1-MDa complex shares with the 600-kDa complex the histone binding protein p55 and the PcG protein SU(Z)12. Coimmunoprecipitation assays performed on embryo extracts and gel filtration column fractions indicate that, during embryogenesis E(Z), SU(Z)12, and p55 are present in all ESC complexes, while PCL and RPD3 are associated with ESC, E(Z), SU(Z)12, and p55 only in the 1-MDa complex. Glutathione transferase pulldown assays demonstrate that RPD3 binds directly to PCL via the conserved PHD fingers of PCL and the N terminus of RPD3. PCL and E(Z) colocalize virtually completely on polytene chromosomes and are associated with a subset of RPD3 sites. As previously shown for E(Z) and RPD3, PCL and SU(Z)12 are also recruited to the insertion site of a minimal Ubx Polycomb response element transgene in vivo. Consistent with these biochemical and cytological results, Rpd3 mutations enhance the phenotypes of Pcl mutants, further indicating that RPD3 is required for PcG silencing and possibly for PCL function. These results suggest that there may be multiple ESC/E(Z) complexes with distinct functions in vivo.

* Corresponding author. Mailing address: Department of Genetics, School of Medicine, Case Western Reserve University, 10900 Euclid Ave., Cleveland, OH 44106-4955. Phone: (216) 368-6417. Fax: (216) 368-3432. E-mail: pjh3{at}po.cwru.edu.

Molecular and Cellular Biology, May 2003, p. 3352-3362, Vol. 23, No. 9
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.9.3352-3362.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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