Source was adult heads of wild-type fly line; bait produced from endogenous gene; prey produced from endogenous gene.
Source was adult heads of wild-type fly line; bait produced from endogenous gene; prey produced from endogenous gene.
Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey from embryo cDNA expression library).
Two-hybrid system: yeast LexA-BD/B42-AD
Interaction in vitro; bait derived from wild-type embryonic extract; prey synthesized by in vitro translation.
Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.
V190E blocks chromoshadow binding
excess PRMVI peptide blocks chromoshadow binding
Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.
cav interacts with Su(var)205, but not with HP1b or HP1c.
Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.
cav pulls down Su(var)205, but not HP1b or HP1c.
Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced and labeled by in vitro translation.
Cloned GST-Su(var)205 construct incubated with lysate from S2 cell line transfected with tagged cav construct.
Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.
Positive control.
Source was a chromatin extract from embryos derived from transgenic line carrying tagged cav construct.
Source was extract from embryos derived from transgenic line carrying tagged cav construct.
Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein.
Two-hybrid system: yeast GAL4-BD/GAL4-AD
Positive control.
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.