A histone methyltransferase activity was purified from embryonic nuclear extracts.

Source was embryonic nuclear extract wild-type fly line; proteins produced from endogenous genes.

The complex of Su(z)12, E(z), Rpd3, esc and Caf1 has an apparent size of 600-650 kDa (gel filtration).

Purified proteins visualized by Coomassie staining.

The E(z), Caf1, Su(z)12 and esc proteins interact as part of the tetrameric Polycomb repressive complex 2 (PRC2) complex.

Analysis of direct interactions suggests that E(z), Caf1, Su(z)12 proteins form a core trimeric complex (all paiwise interactions detected) to which esc protein binds via direct interaction with E(z).

Source was extract of Sf9 cell line; bait produced from transfected construct; prey produced from transfected construct.

Interaction in vitro; bait and prey produced recombinant fusion proteins in baculovirus and insect cell system.

Affinity purification of the esc-E(z) complex was carried out from a mixture of esc, E(z), Su(z)12, and Caf1-55 recombinant proteins. E(z) II domain C363Y results in loss of esc and reduction of E(z) from the complex.

Su(z)12, E(z), Caf1 and esc were coexpressed in Sf9 cells and purified as a complex.

Source was baculovirus-infected Sf9 cell extract; proteins produced from transfected constructs.

Su(z)12, E(z), Caf1 and esc form the PRC2 (Polycomb repressive complex 2).

Deletion of the Su(z)12 N-terminal 104 residues results in PRC2 complexes containing Su(z)12, E(z) and esc, but lacking Caf1@.

Residues 507-630 of Su(z)12 are sufficient for the formation of a PRC2 complex lacking Caf1.