AGO3 in krimp complexes is mostly devoid of sDMA modification and not loaded with piRNAs.

Source was ovaries of Oregon-R fly line; bait produced from endogenous gene; prey produced from endogenous gene.

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

AGO3 in krimp complexes did not undergo sDMA modification.

Experiments performed in csul mutant fly background.

AGO3 in krimp complexes did not undergo sDMA modification.

Source was ovaries of csul mutant fly line; bait produced from endogenous gene; prey produced from endogenous gene.

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

krimp was pulled-down by non-sDMA-modified AGO3 and not sDMA-modified AGO3.

krimp in ovary lysate interacts with both sDMA-modified AGO3 and non-sDMA-modified AGO3.

Source was ovaries of Oregon-R fly line; bait produced from endogenous gene; prey produced from endogenous gene.

Source was ovaries of transgenic fly line; bait produced from tagged transgenic construct; prey produced from tagged transgenic construct.

Interaction occurs with wild-type AGO3, arginine-methylation-deficient AGO3 and piRNA-binding-deficient AGO3.

Source was cell extract of S2 cell line; bait produced from tagged transfected construct; prey produced from tagged transfected construct.

Either krimp Tud 1 domain or Tud 2 domain is sufficient for the interaction.

Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from transfected construct.

Step two in a two step sequential IP from S2 cells expressing aub, krimp and AGO3. Step one was anti-FLAG(aub) immunoprecipitation. This immunoprecipitate was then subsequently immunoprecipitated with anti-GFP(krimp). The presence of AGO3 in the final precipitate suggests that one molecule of krimp binds aub and AGO3.

Kd = 62.8uM. Methylated AGO3 peptides did not bind to the krimp eTud1 domain.

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