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).

A histone methyltransferase activity was purified from embryonic nuclear extracts.

Source was embryonic nuclear extract of transgenic fly line; bait produced from endogenous gene; prey produced from endogenous gene.

Su(z)12 and E(z) cofractionate in a complex of about 600 kDa (as determined by gel filtration).

Source was embryonic nuclear extract of transgenic fly line; bait produced from endogenous gene; prey produced from endogenous gene.

Su(z)12 and E(z) cofractionate in a complex of about 600 kDa (as determined by gel filtration).

Source was embryonic nuclear extract of wild-type fly line; bait produced from endogenous gene; prey produced from endogenous gene.

Su(z)12 and E(z) are present in complexes of about 600 kDa or 1 MDa. The larger 1 MDa PRC2 complex is only observed in 0-16 hr embryos, not in 18-24 hr embryos.

Immunoprecipitation of Su(z)12 from size fractionated extracts containing complexes of about 600 kDa or 1 MDa in size.

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.

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.

Affinity purification of the esc-E(z) complex in Fig2 and 3 was carried out from a mixture of esc, E(z), Su(z)12, and Caf1-55 recombinant proteins. Affinity purification in Fig3 was from a pairwise mixture of E(z) and Su(z)12. E(z) II domain C363Y results in loss of esc and reduction of E(z) from the complex.

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.

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

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

PRC2 complexes were reconstituted from cells infected with baculoviruses for E(z), Su(z)12, Caf1-55 and esc or escl.

Positive control.

Bait endogenous to embryonic nuclear extract.

Prey endogenous to embryonic nuclear extract.

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).

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

Source was embryos of transgenic fly line; bait produced from endogenous gene; prey produced from tagged transgenic construct.

The Su(z)12 zinc finger is not required for PRC2 complex assembly or HMTase activity in vitro, but it is required for interaction in vivo, and for Su(z)12 mutant rescue. PRC2 complexes lacking the Su(z)12 Zinc Finger show diminished chromatin binding as determined by ChIP.

Source was cell extract of S2R+ cell line; proteins produced from transfected construct or endogenous gene.

HGScore = 37.889209