Source was purified recombinant proteins in solution.
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Su(var)205 elutes as a dimer. Mutant I191E as a monomer.
S199E, S202E
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Su(var)205 homodimerizes.
Unlike most other species, Drosophila Su(var)205 has an Arg residue at position 188. Mutation of the Arg residue to Gln (as found in human or yeast HP1a) improves the dimerization constant 2.4-fold, to 0.67 uM. This R188Q mutation has no impact on binding of Su(var)205 to other proteins.
Analytical ultracentrifugation was used to assess the stability of Su(var)205 homodimers.
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Interaction in vitro; bait produced as a recombinant fusion protein in baculovirus and Sf21 cell system; prey produced as a recombinant fusion protein in bacterial system.
