Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced and labeled by in vitro translation.

Caf1 directly interacts with E(z) and Rpd3, but not with esc, in this assay.

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.

Caf1-55, MTA1-like, HDAC1 and MBD-like were coexpressed in a baculovirus expression system, the core NuRD complex affinity purified, and subject to size exclusion chromatography.

Multi-angle laser light scattering of the complex indicated a molecular mass of ~600 kDa.

Source was cell extract of baculovirus-infected Sf21 cell line; bait produced from transfected construct; prey produced from transfected construct.

Source was nuclear extract of OSC cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Co-elution of Mi-2, MEP-1, HDAC1, MTA1-like and Caf1-55 in gel filtration captured as all possible binary interactions.