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.

esc, E(z), Su(z)12 and Caf1 copurify as part of a polycomb repressive (PRC2) complex.

Source was baculovirus-Sf9 cell system; bait produced from tagged transgenic construct; prey produced from transgenic construct.

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

esc, E(z), Su(z)12 and Caf1 copurify as part of a polycomb repressive (PRC2) complex.

Nuclear extract was fractionated on a QAE-Sepharose comlum, then used for FLAG-affinity purification of esc containing complexes.

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

esc, E(z), Su(z)12 and Caf1 copurify as part of a polycomb repressive (PRC2) complex.

Nuclear extract was fractionated on a QAE-Sepharose comlum, then used for FLAG-affinity purification of esc containing complexes.

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

esc and Su(z)12 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 esc 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.

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. Deletion of E(z) II domain results in loss of Su(z)12 and Caf1-55 from the complex.

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

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. Deletion of the E(z) II domain results in loss of esc and E(z) from the complex. 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).

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

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

PRC2 complex of Su(z)12, E(z), esc and Caf1-55.

Some Su(z)12 mutations have no effect on the Su(z)12-esc interaction: W555C, E574A, V585A, F590A and V591A.

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

HGScore = 37.244396

FLAG-tagged esc was co-expressed with components of the PRC2 complex (Su(z)12, E(z) and Caf1-55) as well as Scm.

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

The PRC1 complex consists of Psc, Pc and Sce.

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