cav and moi, but not Su(var)205 (HP1), pull down purified ver in vitro.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

Su(var)205, cav, moi and ver were co-expressed in bacteria. This was supplemented with purified HipHop, and proteins were separated by heparin-sepharose then size-exclusion chromatography to identify complexes formed.

ver-moi and Su(var)205-cav-HipHop form separate subcomplexes in vitro. All five proteins were not observed to form a single "terminin" complex in vitro.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

Two-hybrid system: yeast LexA-BD/GAL4-AD

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

CG30007, ver and moi were individually purified from bacteria and mixed.

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

Co-expression of bait and prey obtained by anti-flag immune affinity purification.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

Co-expression of bait and prey obtained by anti-flag immune affinity purification.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

Various concentrations of ver and moi were mixed with biotin labeled DNA conjugated to streptavidin-HRP and a chemiluminescent substrate was used for detection.. DNA-protein complexes observed by EMSA were used to deduce protein-protein interactions.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

ver and moi bind ssDNA and dsDNA with similar affinity.